|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
1-535 |
0e+00 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 1103.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 1 MNPQEEFIFRSKLPDIYIPKNLPLHSYVLENLSNHSSKPCLINGANGDVYTYADVELTARRVASGLNKIGIQQGDVIMLF 80
Cdd:PLN02246 2 ASASEEFIFRSKLPDIYIPNHLPLHDYCFERLSEFSDRPCLIDGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 81 LPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQACYYEKVKDFARESDVKVMCVDSAPDGCLHFS 160
Cdd:PLN02246 82 LPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 161 ELTQADENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQVDGDNPNLYFHSEDVILCVLPMFHIYALNS 240
Cdd:PLN02246 162 ELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYSLNS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 241 IMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAK 320
Cdd:PLN02246 242 VLLCGLRVGAAILIMPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 321 FPQARLGQGYGMTEAGPVLAMCLAFAKEPFDIKPGACGTVVRNAEMKIVDPETGASLPRNQPGEICIRGDQIMKGYLNDP 400
Cdd:PLN02246 322 LPNAVLGQGYGMTEAGPVLAMCLAFAKEPFPVKSGSCGTVVRNAELKIVDPETGASLPRNQPGEICIRGPQIMKGYLNDP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 401 EATSRTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFV 480
Cdd:PLN02246 402 EATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFV 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 306440447 481 VKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEKLAG 535
Cdd:PLN02246 482 VRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAKLAA 536
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
18-529 |
0e+00 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 812.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 18 IPKNLPLHSYVLENLSNHSSKPCLINGANGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHR 97
Cdd:cd05904 1 LPTDLPLDSVSFLFASAHPSRPALIDAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 98 GAIITAANPFSTPAELAKHAKASRAKLLITQACYYEKVKDFAresdVKVMCVDSAPDGCLHFSELTQ-ADENEAPQVDIS 176
Cdd:cd05904 81 GAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLASLA----LPVVLLDSAEFDSLSFSDLLFeADEAEPPVVVIK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 177 PDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQVDGDNPNlyFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMP 256
Cdd:cd05904 157 QDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSN--SDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 257 KFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEAG 336
Cdd:cd05904 235 RFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTEST 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 337 PVLAMCLAFAKEPfdIKPGACGTVVRNAEMKIVDPETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTG 416
Cdd:cd05904 315 GVVAMCFAPEKDR--AKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWLHTG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 417 DIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQY 496
Cdd:cd05904 393 DLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDF 472
|
490 500 510
....*....|....*....|....*....|...
gi 306440447 497 ISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNL 529
Cdd:cd05904 473 VAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
40-525 |
0e+00 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 616.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 40 CLINGANGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKA 119
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 120 SRAKLLITQACYYEKVKDFARE--SDVKVMCVDSAPDGCLHFSELTQ-----ADENEAPQVDISPDDVVALPYSSGTTGL 192
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKElgPKDKIIVLDDKPDGVLSIEDLLSptlgeEDEDLPPPLKDGKDDTAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 193 PKGVMLTHKGLITSVAQQVDGDNPNlyFHSEDVILCVLPMFHIYALNSIMLCGLRvGAPILIMPKFEIGSLLGLIEKYKV 272
Cdd:cd05911 161 PKGVCLSHRNLIANLSQVQTFLYGN--DGSNDVILGFLPLYHIYGLFTTLASLLN-GATVIIMPKFDSELFLDLIEKYKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 273 SIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEAGPVLAMCLafakePFDI 352
Cdd:cd05911 238 TFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVNP-----DGDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 353 KPGACGTVVRNAEMKIVDPETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIVDR 432
Cdd:cd05911 313 KPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 433 LKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRI-KRVF 511
Cdd:cd05911 393 KKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYKQLrGGVV 472
|
490
....*....|....
gi 306440447 512 FIEAIPKAPSGKIL 525
Cdd:cd05911 473 FVDEIPKSASGKIL 486
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
24-534 |
1.23e-149 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 436.55 E-value: 1.23e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 24 LHSYVLENLSNHSSKPCLINGanGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITA 103
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG--GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 104 ANPFSTPAELAKHAKASRAKLLITqacyyekvkdfaresdvkvmcvdsapdgclhfseltqadeneapqvdispddvVAL 183
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVT-----------------------------------------------------ALI 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 184 PYSSGTTGLPKGVMLTHKGLITSVAQQVDGdnpnLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSL 263
Cdd:COG0318 106 LYTSGTTGRPKGVMLTHRNLLANAAAIAAA----LGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERV 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 264 LGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFpQARLGQGYGMTEAGPVLAMCL 343
Cdd:COG0318 182 LELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 344 AfakEPFDIKPGACGTVVRNAEMKIVDPEtGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDD 423
Cdd:COG0318 261 E---DPGERRPGSVGRPLPGVEVRIVDED-GRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDE 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 424 DDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIF 503
Cdd:COG0318 336 DGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLAR 415
|
490 500 510
....*....|....*....|....*....|.
gi 306440447 504 YKRIKRVFFIEAIPKAPSGKILRKNLKEKLA 534
Cdd:COG0318 416 YKVPRRVEFVDELPRTASGKIDRRALRERYA 446
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
4-536 |
8.91e-149 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 437.87 E-value: 8.91e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 4 QEEFIFRSKLPDIYIPKNLPLHSYVLENLSNHSSKPCLINGANGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPS 83
Cdd:PLN02330 10 DNEHIFRSRYPSVPVPDKLTLPDFVLQDAELYADKVAFVEAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 84 SPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQACYYEKVKDFarESDVKVMCvDSAPDGCLHFSELT 163
Cdd:PLN02330 90 VAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGL--GLPVIVLG-EEKIEGAVNWKELL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 164 QADENEAPQVD---ISPDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQVDGDNPNLYfhSEDVILCVLPMFHIYALNS 240
Cdd:PLN02330 167 EAADRAGDTSDneeILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVGPEMI--GQVVTLGLIPFFHIYGITG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 241 IMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRM--IKSGGAPLGKELEDTVR 318
Cdd:PLN02330 245 ICCATLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLqaIMTAAAPLAPELLTAFE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 319 AKFPQARLGQGYGMTEAGpvlamCLAFAKEPFD-----IKPGACGTVVRNAEMKIVDPETGASLPRNQPGEICIRGDQIM 393
Cdd:PLN02330 325 AKFPGVQVQEAYGLTEHS-----CITLTHGDPEkghgiAKKNSVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 394 KGYLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAG 473
Cdd:PLN02330 400 QGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAG 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 306440447 474 EVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEKLAGI 536
Cdd:PLN02330 480 EIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLSI 542
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
30-530 |
7.02e-136 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 401.94 E-value: 7.02e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 30 ENLSNHSSKPCLINGanGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFST 109
Cdd:cd05936 7 EAARRFPDKTALIFM--GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 110 PAELAKHAKASRAKLLItqacyyekvkdfaresdvkvmCVDSapdgclhFSELTQADENEAPQVDISPDDVVALPYSSGT 189
Cdd:cd05936 85 PRELEHILNDSGAKALI---------------------VAVS-------FTDLLAAGAPLGERVALTPEDVAVLQYTSGT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 190 TGLPKGVMLTHKGLItSVAQQVDGDNPNLYfHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGLIEK 269
Cdd:cd05936 137 TGVPKGAMLTHRNLV-ANALQIKAWLEDLL-EGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLKEIRK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 270 YKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFpQARLGQGYGMTEAGPVLAMClafakeP 349
Cdd:cd05936 215 HRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELT-GVPIVEGYGLTETSPVVAVN------P 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 350 FDI--KPGACGTVVRNAEMKIVDPEtGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDEL 427
Cdd:cd05936 288 LDGprKPGSIGIPLPGTEVKIVDDD-GEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYF 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 428 FIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRI 507
Cdd:cd05936 366 FIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVP 445
|
490 500
....*....|....*....|...
gi 306440447 508 KRVFFIEAIPKAPSGKILRKNLK 530
Cdd:cd05936 446 RQVEFRDELPKSAVGKILRRELR 468
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
8-534 |
2.93e-132 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 396.13 E-value: 2.93e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 8 IFRSKLPDIYIPK--NLPLHSYVLENlSNHSSKPCLINGANGDVYTYADVELTARRVASGL-NKIGIQQGDVIMLFLPSS 84
Cdd:PLN02574 24 IYSSKHPPVPLPSdpNLDAVSFIFSH-HNHNGDTALIDSSTGFSISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 85 PEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQACYYEKVKDFAresdVKVMCV------DSAPDGCLH 158
Cdd:PLN02574 103 VYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLG----VPVIGVpenydfDSKRIEFPK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 159 FSELTQADENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQVDGDNPNL-YFHSEDVILCVLPMFHIYA 237
Cdd:PLN02574 179 FYELIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYeYPGSDNVYLAALPMFHIYG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 238 LNSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPD-LDKHDLSSLRMIKSGGAPL-GKELED 315
Cdd:PLN02574 259 LSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKgVCGEVLKSLKQVSCGAAPLsGKFIQD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 316 TVRAkFPQARLGQGYGMTEAGPVLAMclAFAKEPFDiKPGACGTVVRNAEMKIVDPETGASLPRNQPGEICIRGDQIMKG 395
Cdd:PLN02574 339 FVQT-LPHVDFIQGYGMTESTAVGTR--GFNTEKLS-KYSSVGLLAPNMQAKVVDWSTGCLLPPGNCGELWIQGPGVMKG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 396 YLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEV 475
Cdd:PLN02574 415 YLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEI 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 306440447 476 PVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEKLA 534
Cdd:PLN02574 495 PVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSLT 553
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
51-532 |
2.04e-125 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 376.94 E-value: 2.04e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQAC 130
Cdd:PRK07656 32 TYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 131 Y---YEKVKDFARESDVKVMCVDSAPDG----CLHFSELTQADENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGL 203
Cdd:PRK07656 112 FlgvDYSATTRLPALEHVVICETEEDDPhtekMKTFTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 204 ITSVAQQVDgdnpNLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMM 283
Cdd:PRK07656 192 LSNAADWAE----YLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEVFRLIETERITVLPGPPTMYN 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 284 SIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEAGPVLAMCLAfaKEPFDIKPGACGTVVRN 363
Cdd:PRK07656 268 SLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEASGVTTFNRL--DDDRKTVAGTIGTAIAG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 364 AEMKIVDPEtGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQ 443
Cdd:PRK07656 346 VENKIVNEL-GEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFN 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 444 VAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGK 523
Cdd:PRK07656 425 VYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGK 504
|
....*....
gi 306440447 524 ILRKNLKEK 532
Cdd:PRK07656 505 VLKRALREK 513
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
30-440 |
8.36e-125 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 372.03 E-value: 8.36e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 30 ENLSNHSSKPCLINGAnGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFST 109
Cdd:pfam00501 3 RQAARTPDKTALEVGE-GRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 110 PAELAKHAKASRAKLLITQ-ACYYEKVKDFARESDVKVMCVDSAPDGCLHFSELTQADENEAPQ----VDISPDDVVALP 184
Cdd:pfam00501 82 AEELAYILEDSGAKVLITDdALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPppppPPPDPDDLAYII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 185 YSSGTTGLPKGVMLTHKGLITSVAQQVDGDNPNLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFE---IG 261
Cdd:pfam00501 162 YTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPaldPA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 262 SLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQArLGQGYGMTEAGPVlaM 341
Cdd:pfam00501 242 ALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGV--V 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 342 CLAFAKEPFDIKPGACGTVVRNAEMKIVDPETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDIGYI 421
Cdd:pfam00501 319 TTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRR 398
|
410
....*....|....*....
gi 306440447 422 DDDDELFIVDRLKELIKYK 440
Cdd:pfam00501 399 DEDGYLEIVGRKKDQIKLG 417
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
27-531 |
8.93e-124 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 373.40 E-value: 8.93e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 27 YVLENLSNHSSKPCLINGANGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANP 106
Cdd:cd17642 22 KAMKRYASVPGTIAFTDAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTND 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 107 FSTPAELAKHAKASRAKLLITQACYYEKVKDFARESDV--KVMCVDSAPD----GCLHfSELTQADENEAPQVDISP--- 177
Cdd:cd17642 102 IYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIikTIIILDSKEDykgyQCLY-TFITQNLPPGFNEYDFKPpsf 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 178 --DDVVAL-PYSSGTTGLPKGVMLTHKGLITSVAQQVD---GDNPNlyfhSEDVILCVLPMFHIYALNSIM---LCGLRV 248
Cdd:cd17642 181 drDEQVALiMNSSGSTGLPKGVQLTHKNIVARFSHARDpifGNQII----PDTAILTVIPFHHGFGMFTTLgylICGFRV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 249 gapiLIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQ 328
Cdd:cd17642 257 ----VLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGIRQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 329 GYGMTEAgpvlamCLAFAKEP-FDIKPGACGTVVRNAEMKIVDPETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTI 407
Cdd:cd17642 333 GYGLTET------TSAILITPeGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALI 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 408 DKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQ 487
Cdd:cd17642 407 DKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKT 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 306440447 488 ATEDEIKQYISKQVIFYKRIK-RVFFIEAIPKAPSGKILRKNLKE 531
Cdd:cd17642 487 MTEKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
47-534 |
2.45e-123 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 371.83 E-value: 2.45e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 47 GDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELA---KHAKAsraK 123
Cdd:PRK06187 29 GRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAyilNDAED---R 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 124 LLITQACY---YEKVKD-FARESDVKVMCvDSAPDGC----LHFSELTQADENEAPQVDISPDDVVALPYSSGTTGLPKG 195
Cdd:PRK06187 106 VVLVDSEFvplLAAILPqLPTVRTVIVEG-DGPAAPLapevGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 196 VMLTHKGLITSVAQQVDGdnpnLYFHSEDVILCVLPMFHIYALNsIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVSIA 275
Cdd:PRK06187 185 VVLSHRNLFLHSLAVCAW----LKLSRDDVYLVIVPMFHVHAWG-LPYLALMAGAKQVIPRRFDPENLLDLIETERVTFF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 276 PVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFpQARLGQGYGMTEAGPVLAMCLAFAKEPFDI-KP 354
Cdd:PRK06187 260 FAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKF-GIDLVQGYGMTETSPVVSVLPPEDQLPGQWtKR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 355 GACGTVVRNAEMKIVDPEtGASLPRN--QPGEICIRGDQIMKGYLNDPEATSRTIDKeGWLHTGDIGYIDDDDELFIVDR 432
Cdd:PRK06187 339 RSAGRPLPGVEARIVDDD-GDELPPDggEVGEIIVRGPWLMQGYWNRPEATAETIDG-GWLHTGDVGYIDEDGYLYITDR 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 433 LKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVFF 512
Cdd:PRK06187 417 IKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAF 496
|
490 500
....*....|....*....|..
gi 306440447 513 IEAIPKAPSGKILRKNLKEKLA 534
Cdd:PRK06187 497 VDELPRTSVGKILKRVLREQYA 518
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
35-526 |
1.56e-118 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 356.53 E-value: 1.56e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 35 HSSKPCLINGanGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELA 114
Cdd:cd17631 8 HPDRTALVFG--GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 115 KHAKASRAKLLItqacyyekvkdfaresdvkvmcvdsapdgclhfseltqadeneapqvdispDDVVALPYSSGTTGLPK 194
Cdd:cd17631 86 YILADSGAKVLF---------------------------------------------------DDLALLMYTSGTTGRPK 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 195 GVMLTHKGLITSVAQQVDGDNPNlyfhSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVSI 274
Cdd:cd17631 115 GAMLTHRNLLWNAVNALAALDLG----PDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHRVTS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 275 APVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPqaRLGQGYGMTEAGPVLAMCLAfakEPFDIKP 354
Cdd:cd17631 191 FFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQARGV--KFVQGYGMTETSPGVTFLSP---EDHRRKL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 355 GACGTVVRNAEMKIVDPEtGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFIVDRLK 434
Cdd:cd17631 266 GSAGRPVFFVEVRIVDPD-GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKK 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 435 ELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIE 514
Cdd:cd17631 344 DMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVD 423
|
490
....*....|..
gi 306440447 515 AIPKAPSGKILR 526
Cdd:cd17631 424 ALPRNATGKILK 435
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
179-525 |
1.09e-112 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 337.72 E-value: 1.09e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 179 DVVALPYSSGTTGLPKGVMLTHKGLITSVAQQVDgdnpNLYFHSEDVILCVLPMFHIYALNSIMLCgLRVGAPILIMPKF 258
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAA----SGGLTEGDVFLSTLPLFHIGGLFGLLGA-LLAGGTVVLLPKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 259 EIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPqARLGQGYGMTEAGPV 338
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPG-IKLVNGYGLTETGGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 339 LAMCLAFAKepfDIKPGACGTVVRNAEMKIVDPETGAsLPRNQPGEICIRGDQIMKGYLNDPEATSRTiDKEGWLHTGDI 418
Cdd:cd04433 155 VATGPPDDD---ARKPGSVGRPVPGVEVRIVDPDGGE-LPPGEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 419 GYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYIS 498
Cdd:cd04433 230 GRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHVR 309
|
330 340
....*....|....*....|....*..
gi 306440447 499 KQVIFYKRIKRVFFIEAIPKAPSGKIL 525
Cdd:cd04433 310 ERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
38-535 |
4.53e-100 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 313.20 E-value: 4.53e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 38 KPCLI-NGANGDV--YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELA 114
Cdd:COG0365 25 KVALIwEGEDGEErtLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 115 KHAKASRAKLLITQACYYEKVKDFARESDV-----------KVMCV-----DSAPDGCLHFSELTQADENEAPQVDISPD 178
Cdd:COG0365 105 DRIEDAEAKVLITADGGLRGGKVIDLKEKVdealeelpsleHVIVVgrtgaDVPMEGDLDWDELLAAASAEFEPEPTDAD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 179 DVVALPYSSGTTGLPKGVMLTHKGLITsvaqQVDGDNPNLY-FHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIM-- 255
Cdd:COG0365 185 DPLFILYTSGTTGKPKGVVHTHGGYLV----HAATTAKYVLdLKPGDVFWCTADIGWATGHSYIVYGPLLNGATVVLYeg 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 256 -PKF-EIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPD--LDKHDLSSLRMIKSGGAPLGKELEDTVRAKFpQARLGQGYG 331
Cdd:COG0365 261 rPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDepLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAV-GVPIVDGWG 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 332 MTEAGPVLAMCLAFakepFDIKPGACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQ--IMKGYLNDPEATSRT--- 406
Cdd:COG0365 340 QTETGGIFISNLPG----LPVKPGSMGKPVPGYDVAVVD-EDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETyfg 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 407 -------------IDKEGWLhtgdigyiddddelFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAG 473
Cdd:COG0365 415 rfpgwyrtgdgarRDEDGYF--------------WILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRG 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 306440447 474 EVPVAFVV---KSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEKLAG 535
Cdd:COG0365 481 QVVKAFVVlkpGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEG 545
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
35-536 |
6.91e-100 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 311.48 E-value: 6.91e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 35 HSSKPCLINGanGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELA 114
Cdd:PRK08316 24 YPDKTALVFG--DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 115 KHAKASRAKLLITQACYYEKVKDFARES---DVKVMCV---DSAPDGCLHFSELTQADENEAPQVDISPDDVVALPYSSG 188
Cdd:PRK08316 102 YILDHSGARAFLVDPALAPTAEAALALLpvdTLILSLVlggREAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 189 TTGLPKGVMLTHKGLITS-VAQQVDGDnpnlyFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGLI 267
Cdd:PRK08316 182 TESLPKGAMLTHRALIAEyVSCIVAGD-----MSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELILRTI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 268 EKYKVSI--APvvPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEAGPvLAMCLAf 345
Cdd:PRK08316 257 EAERITSffAP--PTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEIAP-LATVLG- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 346 aKEPFDIKPGACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDD 425
Cdd:PRK08316 333 -PEEHLRRPGSAGRPVLNVETRVVD-DDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 426 ELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIFYK 505
Cdd:PRK08316 410 YITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELIAHCRARLAGFK 489
|
490 500 510
....*....|....*....|....*....|.
gi 306440447 506 RIKRVFFIEAIPKAPSGKILRKNLKEKLAGI 536
Cdd:PRK08316 490 VPKRVIFVDELPRNPSGKILKRELRERYAGA 520
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
51-529 |
2.87e-96 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 299.01 E-value: 2.87e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQac 130
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 131 yyekvkdfaresdvkvmcvdsapdgclhfSELtqadeneapqvdispDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQ 210
Cdd:cd05935 81 -----------------------------SEL---------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 211 VDGDNpnlyFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPD 290
Cdd:cd05935 117 AVWTG----LTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLATPE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 291 LDKHDLSSLRMIKSGGAPLGKELEDTVRAKFpQARLGQGYGMTEAgpvlaMCLAFAKEPFDIKPGACGTVVRNAEMKIVD 370
Cdd:cd05935 193 FKTRDLSSLKVLTGGGAPMPPAVAEKLLKLT-GLRFVEGYGLTET-----MSQTHTNPPLRPKLQCLGIP*FGVDARVID 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 371 PETGASLPRNQPGEICIRGDQIMKGYLNDPEATSR---TIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPA 447
Cdd:cd05935 267 IETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEEsfiEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPA 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 448 ELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSE--KSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKIL 525
Cdd:cd05935 347 EVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPeyRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKIL 426
|
....
gi 306440447 526 RKNL 529
Cdd:cd05935 427 WRLL 430
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
36-531 |
1.90e-95 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 298.84 E-value: 1.90e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 36 SSKPCLINGANGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAK 115
Cdd:cd05926 1 PDAPALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 116 HAKASRAKLLITQACYYE-------KVKDFARESDVKVMCVDSAPDGclhfSELTQADE---NEAPQVDISPDDVVALPY 185
Cdd:cd05926 81 YLADLGSKLVLTPKGELGpasraasKLGLAILELALDVGVLIRAPSA----ESLSNLLAdkkNAKSEGVPLPDDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 186 SSGTTGLPKGVMLTHKGLITSVAQQVDGDNPNlyfhSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLG 265
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNLAASATNITNTYKLT----PDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 266 LIEKYKVSIAPVVPPVMMSIAKSPDLDK-HDLSSLRMIKSGGAPLGKELEDTVRAKFpQARLGQGYGMTEAgpvlamCLA 344
Cdd:cd05926 233 DVRDYNATWYTAVPTIHQILLNRPEPNPeSPPPKLRFIRSCSASLPPAVLEALEATF-GAPVLEAYGMTEA------AHQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 345 FAKEPFDIKPGACGTVVR--NAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDIGYID 422
Cdd:cd05926 306 MTSNPLPPGPRKPGSVGKpvGVEVRILD-EDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 423 DDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVI 502
Cdd:cd05926 385 ADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLA 464
|
490 500
....*....|....*....|....*....
gi 306440447 503 FYKRIKRVFFIEAIPKAPSGKILRKNLKE 531
Cdd:cd05926 465 AFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
47-532 |
8.10e-95 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 298.80 E-value: 8.10e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 47 GDVYTYADVELTARRVASGL-NKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLL 125
Cdd:PRK08314 33 GRAISYRELLEEAERLAGYLqQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 126 ITQACYYEKVKDFARESDVKVMCV------------DSAPDGCLHFSELTQADENEA-------------PQVDISPDDV 180
Cdd:PRK08314 113 IVGSELAPKVAPAVGNLRLRHVIVaqysdylpaepeIAVPAWLRAEPPLQALAPGGVvawkealaaglapPPHTAGPDDL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 181 VALPYSSGTTGLPKGVMLTHKGLITSVAQQVDGDNpnlyFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEI 260
Cdd:PRK08314 193 AVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSN----STPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPRWDR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 261 GSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLgkeledtvrakfPQA---RLGQ--------G 329
Cdd:PRK08314 269 EAAARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAM------------PEAvaeRLKEltgldyveG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 330 YGMTE-AGPVLAmclafakEPFD-IKPGACGTVVRNAEMKIVDPETGASLPRNQPGEICIRGDQIMKGYLNDPEATSR-- 405
Cdd:PRK08314 337 YGLTEtMAQTHS-------NPPDrPKLQCLGIPTFGVDARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEaf 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 406 -TIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVV-KS 483
Cdd:PRK08314 410 iEIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVlRP 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 306440447 484 E-KSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEK 532
Cdd:PRK08314 490 EaRGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQ 539
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
30-534 |
5.24e-86 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 276.88 E-value: 5.24e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 30 ENLSNHSSKPCL-INGANgdvYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFS 108
Cdd:PRK05605 40 NAVARFGDRPALdFFGAT---TTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 109 TPAELAKHAKASRAKLLITqacyYEKVKDFAR--------ESDVKVMCVDSAP-------------------------DG 155
Cdd:PRK05605 117 TAHELEHPFEDHGARVAIV----WDKVAPTVErlrrttplETIVSVNMIAAMPllqrlalrlpipalrkaraaltgpaPG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 156 CLHFSELTQA----DENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQ---VDG--DNPnlyfhseDVI 226
Cdd:PRK05605 193 TVPWETLVDAaiggDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQGkawVPGlgDGP-------ERV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 227 LCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGG 306
Cdd:PRK05605 266 LAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 307 APLGkelEDTVR--AKFPQARLGQGYGMTEAGPVLAmclafaKEPF--DIKPGACGTVVRNAEMKIVDPET-GASLPRNQ 381
Cdd:PRK05605 346 MALP---VSTVElwEKLTGGLLVEGYGLTETSPIIV------GNPMsdDRRPGYVGVPFPDTEVRIVDPEDpDETMPDGE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 382 PGEICIRGDQIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISD 461
Cdd:PRK05605 417 EGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVED 495
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 306440447 462 AAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEKLA 534
Cdd:PRK05605 496 AAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELL 568
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
23-532 |
9.02e-84 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 270.75 E-value: 9.02e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 23 PLHSYVLENLSNHSSKPCLinGANGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIIT 102
Cdd:PRK06710 25 PLHKYVEQMASRYPEKKAL--HFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 103 AANPFSTPAELAKHAKASRAKLLITQACYYEKVKDFARESDVKVMCVDSAPD---------------------------G 155
Cdd:PRK06710 103 QTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIEHVIVTRIADflpfpknllypfvqkkqsnlvvkvsesE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 156 CLHFSELTQADENEAPQVDISPD-DVVALPYSSGTTGLPKGVMLTHKGLITSVAQQVDGdnpnLY--FHSEDVILCVLPM 232
Cdd:PRK06710 183 TIHLWNSVEKEVNTGVEVPCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQW----LYncKEGEEVVLGVLPF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 233 FHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKE 312
Cdd:PRK06710 259 FHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 313 LEDTVRaKFPQARLGQGYGMTEAGPVLAMCLAFAKEpfdiKPGACGTVVRNAEMKIVDPETGASLPRNQPGEICIRGDQI 392
Cdd:PRK06710 339 VQEKFE-TVTGGKLVEGYGLTESSPVTHSNFLWEKR----VPGSIGVPWPDTEAMIMSLETGEALPPGEIGEIVVKGPQI 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 393 MKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDA 472
Cdd:PRK06710 414 MKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYR 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 473 GEVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEK 532
Cdd:PRK06710 493 GETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEE 552
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
177-530 |
2.62e-81 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 257.59 E-value: 2.62e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 177 PDDVVALPYSSGTTGLPKGVMLTHKGLITSvAQQVdGDNpnLYFHSEDVILCVLPMFHIYALN-SIMLCGLRVGAPILIM 255
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN-GYFI-GER--LGLTEQDRLCIPVPLFHCFGSVlGVLACLTHGATMVFPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 256 PKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEA 335
Cdd:cd05917 77 PSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 336 GPVLAMclAFAKEPFDIKPGACGTVVRNAEMKIVDPETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHT 415
Cdd:cd05917 157 SPVSTQ--TRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 416 GDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQ 495
Cdd:cd05917 235 GDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEEDIKA 314
|
330 340 350
....*....|....*....|....*....|....*
gi 306440447 496 YISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLK 530
Cdd:cd05917 315 YCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
50-531 |
6.19e-81 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 258.82 E-value: 6.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKasrakllitqa 129
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLK----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 130 cyyekvkdfarESDVKVmcvdsapdgclhfseltqadeneapqvdispDDVVALPYSSGTTGLPKGVMLTHKGLITSVAq 209
Cdd:cd05912 71 -----------DSDVKL-------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAI- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 210 qvdGDNPNLYFHSEDVILCVLPMFHIYALnSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKsp 289
Cdd:cd05912 108 ---GSALNLGLTEDDNWLCALPLFHISGL-SILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLE-- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 290 DLDKHDLSSLRMIKSGGAPLGKELEDTVRAK-FPqarLGQGYGMTEAGpvlAMCLAFAKEPFDIKPGACGTVVRNAEMKI 368
Cdd:cd05912 182 ILGEGYPNNLRCILLGGGPAPKPLLEQCKEKgIP---VYQSYGMTETC---SQIVTLSPEDALNKIGSAGKPLFPVELKI 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 369 VDPETgaslPRNQPGEICIRGDQIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAE 448
Cdd:cd05912 256 EDDGQ----PPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAE 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 449 LEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKsqATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKN 528
Cdd:cd05912 331 IEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERP--ISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHE 408
|
...
gi 306440447 529 LKE 531
Cdd:cd05912 409 LKQ 411
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
51-533 |
2.26e-80 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 259.51 E-value: 2.26e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQAC 130
Cdd:PRK03640 29 TFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 131 YYEKVKdfaresdvkvmcvdsaPDGCLHFSELTQADENEA-PQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLITSVAq 209
Cdd:PRK03640 109 FEAKLI----------------PGISVKFAELMNGPKEEAeIQEEFDLDEVATIMYTSGTTGKPKGVIQTYGNHWWSAV- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 210 qvdGDNPNLYFHSEDVILCVLPMFHIYALnSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPpVMMS--IAK 287
Cdd:PRK03640 172 ---GSALNLGLTEDDCWLAAVPIFHISGL-SILMRSVIYGMRVVLVEKFDAEKINKLLQTGGVTIISVVS-TMLQrlLER 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 288 SPDLDKHdlSSLRMIKSGGAPLGKE-LEDTVRAKFPqarLGQGYGMTE-AGPVLAMCLAFAKEpfdiKPGACGTVVRNAE 365
Cdd:PRK03640 247 LGEGTYP--SSFRCMLLGGGPAPKPlLEQCKEKGIP---VYQSYGMTEtASQIVTLSPEDALT----KLGSAGKPLFPCE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 366 MKIVDpeTGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVA 445
Cdd:PRK03640 318 LKIEK--DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 446 PAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKsqATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKIL 525
Cdd:PRK03640 395 PAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGE--VTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLL 472
|
....*...
gi 306440447 526 RKNLKEKL 533
Cdd:PRK03640 473 RHELKQLV 480
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
47-535 |
3.16e-80 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 261.51 E-value: 3.16e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 47 GDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLI 126
Cdd:PRK06178 56 GHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 127 TQACYYEKVKDFARESDVKVMCVDS----------------------APDGCLHFSELTQADENEAPQVDISPDDVVALP 184
Cdd:PRK06178 136 ALDQLAPVVEQVRAETSLRHVIVTSladvlpaeptlplpdslraprlAAAGAIDLLPALRACTAPVPLPPPALDALAALN 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 185 YSSGTTGLPKGVMLTHKGLI----TSVAQQVDGDNPnlyfhseDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEI 260
Cdd:PRK06178 216 YTGGTTGMPKGCEHTQRDMVytaaAAYAVAVVGGED-------SVFLSFLPEFWIAGENFGLLFPLFSGATLVLLARWDA 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 261 GSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRmiKSGGAPLGKELEDTVRAKFPQAR---LGQG-YGMTEAG 336
Cdd:PRK06178 289 VAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLR--QVRVVSFVKKLNPDYRQRWRALTgsvLAEAaWGMTETH 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 337 PVLAMCLAFAKEPFDIK--PGACGTVVRNAEMKIVDPETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIdKEGWLH 414
Cdd:PRK06178 367 TCDTFTAGFQDDDFDLLsqPVFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLH 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 415 TGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIK 494
Cdd:PRK06178 446 TGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQ 525
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 306440447 495 QYISKQVIFYKrIKRVFFIEAIPKAPSGKILRKNLKEKLAG 535
Cdd:PRK06178 526 AWCRENMAVYK-VPEIRIVDALPMTATGKVRKQDLQALAEE 565
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
50-531 |
5.44e-80 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 259.48 E-value: 5.44e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELA---KHAK-------A 119
Cdd:cd12119 26 YTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAyiiNHAEdrvvfvdR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 120 SRAKLLITQACYYEKVKDFARESDVKVMCVDsAPDGCLHFSELTQADENEAPQVDISPDDVVALPYSSGTTGLPKGVMLT 199
Cdd:cd12119 106 DFLPLLEAIAPRLPTVEHVVVMTDDAAMPEP-AGVGVLAYEELLAAESPEYDWPDFDENTAAAICYTSGTTGNPKGVVYS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 200 HKGLI--TSVAQQVDGdnpnLYFHSEDVILCVLPMFHIYALNSIMLCGLrVGAPiLIMP--KFEIGSLLGLIEKYKVSIA 275
Cdd:cd12119 185 HRSLVlhAMAALLTDG----LGLSESDVVLPVVPMFHVNAWGLPYAAAM-VGAK-LVLPgpYLDPASLAELIEREGVTFA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 276 PVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARlgQGYGMTEAGPVLAMCL---AFAKEPFD- 351
Cdd:cd12119 259 AGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVRVI--HAWGMTETSPLGTVARppsEHSNLSEDe 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 352 -----IKPG--ACGTvvrnaEMKIVDPETGAsLPR--NQPGEICIRGDQIMKGYLNDPEATSRtIDKEGWLHTGDIGYID 422
Cdd:cd12119 337 qlalrAKQGrpVPGV-----ELRIVDDDGRE-LPWdgKAVGELQVRGPWVTKSYYKNDEESEA-LTEDGWLRTGDVATID 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 423 DDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVI 502
Cdd:cd12119 410 EDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVA 489
|
490 500
....*....|....*....|....*....
gi 306440447 503 FYKRIKRVFFIEAIPKAPSGKILRKNLKE 531
Cdd:cd12119 490 KWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
33-530 |
5.01e-79 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 256.53 E-value: 5.01e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 33 SNHSSKPCLINGAngDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAE 112
Cdd:cd05959 15 EGRGDKTAFIDDA--GSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 113 LAKHAKASRAKLLITQACYYEKVKDFAR---ESDVKVMCVDSAP--DGCLHFSELTQADENEAPQVDISPDDVVALPYSS 187
Cdd:cd05959 93 YAYYLEDSRARVVVVSGELAPVLAAALTkseHTLVVLIVSGGAGpeAGALLLAELVAAEAEQLKPAATHADDPAFWLYSS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 188 GTTGLPKGVMLTHKGLITSV---AQQVDGDNPNlyfhseDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKF-EIGSL 263
Cdd:cd05959 173 GSTGRPKGVVHLHADIYWTAelyARNVLGIRED------DVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERpTPAAV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 264 LGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLgQGYGMTEAGPVLamcl 343
Cdd:cd05959 247 FKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDIL-DGIGSTEMLHIF---- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 344 aFAKEPFDIKPGACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDD 423
Cdd:cd05959 322 -LSNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 424 DDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVV---KSEKSQATEDEIKQYISKQ 500
Cdd:cd05959 399 DGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVlrpGYEDSEALEEELKEFVKDR 478
|
490 500 510
....*....|....*....|....*....|
gi 306440447 501 VIFYKRIKRVFFIEAIPKAPSGKILRKNLK 530
Cdd:cd05959 479 LAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
22-534 |
3.56e-78 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 255.07 E-value: 3.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 22 LPLHSYVLENLSNHSSKPCLINGanGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIi 101
Cdd:COG1021 25 ETLGDLLRRRAERHPDRIAVVDG--ERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 102 taanP-FSTPA----ELAKHAKASRAKLLITQACY----YekvKDFARE-----SDVKVMCVDSAPDGCLHFSELTQADE 167
Cdd:COG1021 102 ----PvFALPAhrraEISHFAEQSEAVAYIIPDRHrgfdY---RALARElqaevPSLRHVLVVGDAGEFTSLDALLAAPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 168 nEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQVD--GdnpnlyFHSEDVILCVLPMFHIYALNSIMLCG 245
Cdd:COG1021 175 -DLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEicG------LDADTVYLAALPAAHNFPLSSPGVLG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 246 -LRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPqA 324
Cdd:COG1021 248 vLYAGGTVVLAPDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALG-C 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 325 RLGQGYGMTEaGPVL-----------------AMClafakePFDikpgacgtvvrnaEMKIVDPEtGASLPRNQPGEICI 387
Cdd:COG1021 327 TLQQVFGMAE-GLVNytrlddpeevilttqgrPIS------PDD-------------EVRIVDED-GNPVPPGEVGELLT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 388 RGDQIMKGYLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGL 467
Cdd:COG1021 386 RGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAM 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 306440447 468 KDEDAGEVPVAFVVKSEKSQaTEDEIKQYI-SKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEKLA 534
Cdd:COG1021 466 PDEYLGERSCAFVVPRGEPL-TLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
47-530 |
2.00e-77 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 249.90 E-value: 2.00e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 47 GDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLI 126
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 127 TqacyyekvkdfaresdvkvmcvdsapdgclhfseltqadeneapqvdispdDVVALPYSSGTTGLPKGVMLTHKGLITS 206
Cdd:cd05934 81 V---------------------------------------------------DPASILYTSGTTGPPKGVVITHANLTFA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 207 VAQQVDGdnpnLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVSIA---PVVPPVMM 283
Cdd:cd05934 110 GYYSARR----FGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRRYGATVTnylGAMLSYLL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 284 SIAKSPDlDKHDLssLRMIksGGAPLGKELEDTVRAKFpQARLGQGYGMTEAGPVLAmclafAKEPFDIKPGACGTVVRN 363
Cdd:cd05934 186 AQPPSPD-DRAHR--LRAA--YGAPNPPELHEEFEERF-GVRLLEGYGMTETIVGVI-----GPRDEPRRPGSIGRPAPG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 364 AEMKIVDPEtGASLPRNQPGEICIRGDQ---IMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFIVDRLKELIKYK 440
Cdd:cd05934 255 YEVRIVDDD-GQELPAGEPGELVIRGLRgwgFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRR 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 441 GFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAP 520
Cdd:cd05934 333 GENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTP 412
|
490
....*....|
gi 306440447 521 SGKILRKNLK 530
Cdd:cd05934 413 TEKVAKAQLR 422
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
47-535 |
8.66e-77 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 252.01 E-value: 8.66e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 47 GDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLI 126
Cdd:PRK07786 40 GNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 127 TQACYYE---KVKDFARESDVKVMCVDSAPDGCLHFSELTQADENEAPQVDIsPDDVVAL-PYSSGTTGLPKGVMLTHKG 202
Cdd:PRK07786 120 TEAALAPvatAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDI-PNDSPALiMYTSGTTGRPKGAVLTHAN 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 203 LitsVAQQVDGDNPNLYFHSEDVILCVLPMFHIYALNSiMLCGLRVGAPILIMP--KFEIGSLLGLIEKYKVSIAPVVPP 280
Cdd:PRK07786 199 L---TGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGS-MLPGLLLGAPTVIYPlgAFDPGQLLDVLEAEKVTGIFLVPA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 281 VMMSIAKSPDLDKHDLSsLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEAGPVLAMCLAfakEPFDIKPGACGTV 360
Cdd:PRK07786 275 QWQAVCAEQQARPRDLA-LRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPVTCMLLG---EDAIRKLGSVGKV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 361 VRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKeGWLHTGDIGYIDDDDELFIVDRLKELIKYK 440
Cdd:PRK07786 351 IPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAG-GWFHSGDLVRQDEEGYVWVVDRKKDMIISG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 441 GFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFV-VKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKA 519
Cdd:PRK07786 429 GENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAaVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRN 508
|
490
....*....|....*.
gi 306440447 520 PSGKILRKNLKEKLAG 535
Cdd:PRK07786 509 PAGKVLKTELRERYGA 524
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
45-533 |
1.82e-75 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 247.08 E-value: 1.82e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 45 ANGDVYTYADVELTARRVASGL-NKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAK 123
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 124 LLITQACYYEKVKDFARESDVKVMCVDSAPdgclhfSELTQADENEApqVDISPDDVVALPYSSGTTGLPKGVMLTHKGL 203
Cdd:PRK06839 103 VLFVEKTFQNMALSMQKVSYVQRVISITSL------KEIEDRKIDNF--VEKNESASFIICYTSGTTGKPKGAVLTQENM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 204 ITSVAQQVdgdnPNLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMM 283
Cdd:PRK06839 175 FWNALNNT----FAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 284 SIAKSPDLDKHDLSSLRMIKSGGAPLGKELedtVRAKFPQA-RLGQGYGMTEAGPVLAMclaFAKEPFDIKPGACGTVVR 362
Cdd:PRK06839 251 ALINCSKFETTNLQSVRWFYNGGAPCPEEL---MREFIDRGfLFGQGFGMTETSPTVFM---LSEEDARRKVGSIGKPVL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 363 NAEMKIVDPETGaSLPRNQPGEICIRGDQIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGF 442
Cdd:PRK06839 325 FCDYELIDENKN-KVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 443 QVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSG 522
Cdd:PRK06839 403 NIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATG 482
|
490
....*....|.
gi 306440447 523 KILRKNLKEKL 533
Cdd:PRK06839 483 KIQKAQLVNQL 493
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
50-531 |
3.94e-75 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 247.76 E-value: 3.94e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLIT-- 127
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICad 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 128 --QACYY-----EKVKDFARESDVKVMCVD------------SAPDGCLHFSELTQADEN------EAPQVDISPDDVVA 182
Cdd:PRK12583 126 afKTSDYhamlqELLPGLAEGQPGALACERlpelrgvvslapAPPPGFLAWHELQARGETvsrealAERQASLDRDDPIN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 183 LPYSSGTTGLPKGVMLTHKGLITS---VAQQvdgdnpnLYFHSEDViLCV-LPMFHIYALNSIMLCGLRVGApILIMPKF 258
Cdd:PRK12583 206 IQYTSGTTGFPKGATLSHHNILNNgyfVAES-------LGLTEHDR-LCVpVPLYHCFGMVLANLGCMTVGA-CLVYPNE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 259 EIGSLLGL--IEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEAG 336
Cdd:PRK12583 277 AFDPLATLqaVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 337 PVLAmcLAFAKEPFDIKPGACGTVVRNAEMKIVDPEtGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTG 416
Cdd:PRK12583 357 PVSL--QTTAADDLERRVETVGRTQPHLEVKVVDPD-GATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTG 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 417 DIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQY 496
Cdd:PRK12583 434 DLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREF 513
|
490 500 510
....*....|....*....|....*....|....*
gi 306440447 497 ISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKE 531
Cdd:PRK12583 514 CKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMRE 548
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
50-533 |
4.79e-73 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 242.41 E-value: 4.79e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLIT-- 127
Cdd:PRK08315 44 WTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAad 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 128 ---QACYYEKVKDFARE-----------------SDVKVMCvDSAPDGCLHFSEL------TQADENEAPQVDISPDDVV 181
Cdd:PRK08315 124 gfkDSDYVAMLYELAPElatcepgqlqsarlpelRRVIFLG-DEKHPGMLNFDELlalgraVDDAELAARQATLDPDDPI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 182 ALPYSSGTTGLPKGVMLTHKGLIT---SVAQqvdgdnpNLYFHSEDVILCVLPMFHIYALnsIM--LCGLRVGAPILIM- 255
Cdd:PRK08315 203 NIQYTSGTTGFPKGATLTHRNILNngyFIGE-------AMKLTEEDRLCIPVPLYHCFGM--VLgnLACVTHGATMVYPg 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 256 PKFEIGSLLGLIEKYKVSIAPVVPpvMMSIAK--SPDLDKHDLSSLR---MiksGGAPLGKELEDTVRAKFPQARLGQGY 330
Cdd:PRK08315 274 EGFDPLATLAAVEEERCTALYGVP--TMFIAEldHPDFARFDLSSLRtgiM---AGSPCPIEVMKRVIDKMHMSEVTIAY 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 331 GMTEAGPVlaMCLAFAKEPFDIKpgaCGTVVR---NAEMKIVDPETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTI 407
Cdd:PRK08315 349 GMTETSPV--STQTRTDDPLEKR---VTTVGRalpHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAI 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 408 DKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQ 487
Cdd:PRK08315 424 DADGWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGAT 503
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 306440447 488 ATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKI----LRKNLKEKL 533
Cdd:PRK08315 504 LTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIqkfkMREMMIEEL 553
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
33-531 |
6.23e-73 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 242.27 E-value: 6.23e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 33 SNHSSKPCLINgaNGDVYTYADVELTARRVASGL-NKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPA 111
Cdd:PRK08974 34 ARYADQPAFIN--MGEVMTFRKLEERSRAFAAYLqNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 112 ELAKHAKASRAKLLITqacyyekVKDFAR--ESDVKVMCVD-----------SAPDGCL--------------------- 157
Cdd:PRK08974 112 ELEHQLNDSGAKAIVI-------VSNFAHtlEKVVFKTPVKhviltrmgdqlSTAKGTLvnfvvkyikrlvpkyhlpdai 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 158 HFSE-LTQADENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLITSVaQQVDGDNPNLYFHSEDVILCVLPMFHIY 236
Cdd:PRK08974 185 SFRSaLHKGRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANL-EQAKAAYGPLLHPGKELVVTALPLYHIF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 237 ALNSIMLCGLRVGAP-ILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELED 315
Cdd:PRK08974 264 ALTVNCLLFIELGGQnLLITNPRDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQAVAE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 316 TvRAKFPQARLGQGYGMTEAGPVLAMClafakePFDIK--PGACGTVVRNAEMKIVDPEtGASLPRNQPGEICIRGDQIM 393
Cdd:PRK08974 344 R-WVKLTGQYLLEGYGLTECSPLVSVN------PYDLDyySGSIGLPVPSTEIKLVDDD-GNEVPPGEPGELWVKGPQVM 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 394 KGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAG 473
Cdd:PRK08974 416 LGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSG 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 306440447 474 EVPVAFVVKSEKSqATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKE 531
Cdd:PRK08974 495 EAVKIFVVKKDPS-LTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRD 551
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
30-530 |
8.07e-73 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 241.85 E-value: 8.07e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 30 ENLSNHSSKPCLIngANGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFST 109
Cdd:PRK07059 31 ESFRQYADRPAFI--CMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 110 PAELAKHAKASRAKLLITQACYYEKVKDFARESDVKVMCVDSAPD--------------------------GCLHFSELT 163
Cdd:PRK07059 109 PRELEHQLKDSGAEAIVVLENFATTVQQVLAKTAVKHVVVASMGDllgfkghivnfvvrrvkkmvpawslpGHVRFNDAL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 164 QADENEAPQ-VDISPDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQVDGDNPNLYFHSED---VILCVLPMFHIYALN 239
Cdd:PRK07059 189 AEGARQTFKpVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQPAFEKKPRPdqlNFVCALPLYHIFALT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 240 SIMLCGLRVGA-PILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELedtvr 318
Cdd:PRK07059 269 VCGLLGMRTGGrNILIPNPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQRPV----- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 319 AKFPQARLG----QGYGMTEAGPVlAMClafakEPFDIK--PGACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQI 392
Cdd:PRK07059 344 AERWLEMTGcpitEGYGLSETSPV-ATC-----NPVDATefSGTIGLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQV 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 393 MKGYLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDA 472
Cdd:PRK07059 417 MAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHS 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 306440447 473 GEVPVAFVVKSEKSqATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLK 530
Cdd:PRK07059 497 GEAVKLFVVKKDPA-LTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
18-531 |
1.77e-71 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 238.18 E-value: 1.77e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 18 IPKNLPLHSY--VLE----NLSNHSSKPCLINgaNGDVYTYADVELTARRVASGLNK-IGIQQGDVIMLFLPSSPEFVLA 90
Cdd:PRK12492 14 VPSTIDLAAYksVVEvferSCKKFADRPAFSN--LGVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 91 FLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQACYYEKVKDFARESD--------------------------- 143
Cdd:PRK12492 92 VFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGieylieakmgdllpaakgwlvntvvdk 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 144 VKVMCVDSAPDGCLHFSELTQADENEAPQ-VDISPDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQ------QVDGDNP 216
Cdd:PRK12492 172 VKKMVPAYHLPQAVPFKQALRQGRGLSLKpVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQvraclsQLGPDGQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 217 NLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGA-PILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHD 295
Cdd:PRK12492 252 PLMKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNhNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 296 LSSLRMIKSGGAPLGKELEDTvRAKFPQARLGQGYGMTEAGPVLAmclafaKEPFDIKP--GACGTVVRNAEMKIVDPEt 373
Cdd:PRK12492 332 FSALKLTNSGGTALVKATAER-WEQLTGCTIVEGYGLTETSPVAS------TNPYGELArlGTVGIPVPGTALKVIDDD- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 374 GASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALL 453
Cdd:PRK12492 404 GNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVV 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 306440447 454 IAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSqATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKE 531
Cdd:PRK12492 484 MAHPKVANCAAIGVPDERSGEAVKLFVVARDPG-LSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
47-531 |
3.04e-70 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 235.04 E-value: 3.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 47 GDVYTYADVELTARRVASGL-NKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLL 125
Cdd:PRK05677 47 GKTLTYGELYKLSGAFAAWLqQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 126 ITQACYYEKVKDFARESDVKVMCVDSAPD---------------------------GCLHFSE-LTQADENEAPQVDISP 177
Cdd:PRK05677 127 VCLANMAHLAEKVLPKTGVKHVIVTEVADmlpplkrllinavvkhvkkmvpayhlpQAVKFNDaLAKGAGQPVTEANPQA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 178 DDVVALPYSSGTTGLPKGVMLTHKGLITSVAQ--QVDGDNPNlyfHSEDVILCVLPMFHIYALN----SIMLCGlrvGAP 251
Cdd:PRK05677 207 DDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQcrALMGSNLN---EGCEILIAPLPLYHIYAFTfhcmAMMLIG---NHN 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 252 ILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELedtvrAKFPQARLG---- 327
Cdd:PRK05677 281 ILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQLAT-----AERWKEVTGcaic 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 328 QGYGMTEAGPVLAMclafakEPFD-IKPGACGTVVRNAEMKIVDPEtGASLPRNQPGEICIRGDQIMKGYLNDPEATSRT 406
Cdd:PRK05677 356 EGYGMTETSPVVSV------NPSQaIQVGTIGIPVPSTLCKVIDDD-GNELPLGEVGELCVKGPQVMKGYWQRPEATDEI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 407 IDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKS 486
Cdd:PRK05677 429 LDSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGE 508
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 306440447 487 QATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKE 531
Cdd:PRK05677 509 TLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRD 553
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
38-531 |
1.01e-69 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 230.25 E-value: 1.01e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 38 KPCLINGanGDVYTYADVELTARRVASGLN-KIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAkh 116
Cdd:cd05941 2 RIAIVDD--GDSITYADLVARAARLANRLLaLGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELE-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 117 akasrakLLITqacyyekvkdfaresdvkvmcvDSAP----DGCLhfseltqadeneapqvdispddvvaLPYSSGTTGL 192
Cdd:cd05941 78 -------YVIT----------------------DSEPslvlDPAL-------------------------ILYTSGTTGR 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 193 PKGVMLTHKGLITSVAQQVDGDNpnlyFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKV 272
Cdd:cd05941 104 PKGVVLTHANLAANVRALVDAWR----WTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVAISRLMPSI 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 273 SIAPVVPPVMMSIAKSPDLDKHD--------LSSLRMIKSGGAPLGKEledtVRAKFpQARLGQG----YGMTEAGpvla 340
Cdd:cd05941 180 TVFMGVPTIYTRLLQYYEAHFTDpqfaraaaAERLRLMVSGSAALPVP----TLEEW-EAITGHTllerYGMTEIG---- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 341 MCLAfakEPFD--IKPGACGTVVRNAEMKIVDPETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDI 418
Cdd:cd05941 251 MALS---NPLDgeRRPGTVGMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDL 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 419 GYIDDDDELFIVDRLK-ELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVV-KSEKSQATEDEIKQY 496
Cdd:cd05941 328 GVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVlRAGAAALSLEELKEW 407
|
490 500 510
....*....|....*....|....*....|....*
gi 306440447 497 ISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKE 531
Cdd:cd05941 408 AKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
179-526 |
7.78e-68 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 221.99 E-value: 7.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 179 DVVALPYSSGTTGLPKGVMLTHKGLITSVAQQVDgdnpNLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKF 258
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWAD----CADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 259 EIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEAGpV 338
Cdd:cd17638 77 DVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAG-V 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 339 LAMCLAfaKEPFDIKPGACGTVVRNAEMKIVDPetgaslprnqpGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDI 418
Cdd:cd17638 156 ATMCRP--GDDAETVATTCGRACPGFEVRIADD-----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 419 GYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYIS 498
Cdd:cd17638 223 GELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCR 302
|
330 340
....*....|....*....|....*...
gi 306440447 499 KQVIFYKRIKRVFFIEAIPKAPSGKILR 526
Cdd:cd17638 303 ERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
37-535 |
2.00e-67 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 225.92 E-value: 2.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 37 SKPCLINGanGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKH 116
Cdd:PRK06145 17 DRAALVYR--DQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 117 AKASRAKLLITQAcyyEKVKDFARESDVKVMCVDSAPDGclhfSELTQADENEAPQVDISPDDVVALPYSSGTTGLPKGV 196
Cdd:PRK06145 95 LGDAGAKLLLVDE---EFDAIVALETPKIVIDAAAQADS----RRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 197 MLTHKGLITSVAQQVDGdnpnLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVSIAP 276
Cdd:PRK06145 168 MHSYGNLHWKSIDHVIA----LGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 277 VVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAplgKELEDTVRA---KFPQARLGQGYGMTEAgpVLAMCLAFAKEPFDiK 353
Cdd:PRK06145 244 MAPVMLSRVLTVPDRDRFDLDSLAWCIGGGE---KTPESRIRDftrVFTRARYIDAYGLTET--CSGDTLMEAGREIE-K 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 354 PGACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFIVDRL 433
Cdd:PRK06145 318 IGSTGRALAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 434 KELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVFFI 513
Cdd:PRK06145 396 KDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVR 475
|
490 500
....*....|....*....|..
gi 306440447 514 EAIPKAPSGKILRKNLKEKLAG 535
Cdd:PRK06145 476 DELPRNPSGKVLKRVLRDELNG 497
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
28-466 |
7.29e-67 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 226.91 E-value: 7.29e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 28 VLENLSNHSSKPCLINGANGD--VYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAAN 105
Cdd:COG1022 17 LRRRAARFPDRVALREKEDGIwqSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 106 PFSTPAELA---KHakaSRAKLLI--TQAcYYEKVKDFARE--SDVKVMCVD----SAPDGCLHFSELTQA-------DE 167
Cdd:COG1022 97 PTSSAEEVAyilND---SGAKVLFveDQE-QLDKLLEVRDElpSLRHIVVLDprglRDDPRLLSLDELLALgrevadpAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 168 NEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQVDGDNpnlyFHSEDVILCVLPMFHIYAlNSIMLCGLR 247
Cdd:COG1022 173 LEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLP----LGPGDRTLSFLPLAHVFE-RTVSYYALA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 248 VGAPILIMPkfEIGSLLGLIEKYKVSIAPVVPPV--------MMSIAKSPDL---------------------------- 291
Cdd:COG1022 248 AGATVAFAE--SPDTLAEDLREVKPTFMLAVPRVwekvyagiQAKAEEAGGLkrklfrwalavgrryararlagkspsll 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 292 --------DKHDLSSLR---------MIkSGGAPLGKELEDTVRAkfpqarLG----QGYGMTEAGPVLAMClafakEPF 350
Cdd:COG1022 326 lrlkhalaDKLVFSKLRealggrlrfAV-SGGAALGPELARFFRA------LGipvlEGYGLTETSPVITVN-----RPG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 351 DIKPGACGTVVRNAEMKIVDPetgaslprnqpGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIV 430
Cdd:COG1022 394 DNRIGTVGPPLPGVEVKIAED-----------GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRIT 462
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 306440447 431 DRLKELI-----KYkgfqVAPAELEALLIAHPEISDAAVVG 466
Cdd:COG1022 463 GRKKDLIvtsggKN----VAPQPIENALKASPLIEQAVVVG 499
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
31-533 |
1.67e-66 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 224.15 E-value: 1.67e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 31 NLSN--------HSSKPCLINGANgdVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIIT 102
Cdd:PRK07470 8 NLAHflrqaarrFPDRIALVWGDR--SWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 103 AANPFSTPAELAKHAKASRAKLLITQACYYEKVKDFARES-DVKVMCVDSAPDGCLHFSELTQADENEAPQV-DISPDDV 180
Cdd:PRK07470 86 PTNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASpDLTHVVAIGGARAGLDYEALVARHLGARVANaAVDHDDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 181 VALPYSSGTTGLPKGVMLTHKGLITSVAQQVDGDNPNLYFHseDVILCVLPMFH---IYALnsimlCGLRVGAPILIMP- 256
Cdd:PRK07470 166 CWFFFTSGTTGRPKAAVLTHGQMAFVITNHLADLMPGTTEQ--DASLVVAPLSHgagIHQL-----CQVARGAATVLLPs 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 257 -KFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKEleDTVRAKfpqARLG----QGYG 331
Cdd:PRK07470 239 eRFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRA--DQKRAL---AKLGkvlvQYFG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 332 MTEAG---PVLAMCLAFAKEPFDIKPGACGTVVRNAEMKIVDPEtGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTId 408
Cdd:PRK07470 314 LGEVTgniTVLPPALHDAEDGPDARIGTCGFERTGMEVQIQDDE-GRELPPGETGEICVIGPAVFAGYYNNPEANAKAF- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 409 KEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQA 488
Cdd:PRK07470 392 RDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPV 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 306440447 489 TEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEKL 533
Cdd:PRK07470 472 DEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREEL 516
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
34-528 |
3.33e-66 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 222.17 E-value: 3.33e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 34 NHSSKPCLINGANgdVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAEL 113
Cdd:cd12118 16 VYPDRTSIVYGDR--RYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 114 AkhakasrakLLItqacyyekvkdfaRESDVKVMCVDSAPDG-CLhfseLTQADENEAPQVDISPDDVVALPYSSGTTGL 192
Cdd:cd12118 94 A---------FIL-------------RHSEAKVLFVDREFEYeDL----LAEGDPDFEWIPPADEWDPIALNYTSGTTGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 193 PKGVMLTHKG-LITSVAQQVDGDnpnlyFHSEDVILCVLPMFH------IYALNSimlcglrVGAPILIMPKFEIGSLLG 265
Cdd:cd12118 148 PKGVVYHHRGaYLNALANILEWE-----MKQHPVYLWTLPMFHcngwcfPWTVAA-------VGGTNVCLRKVDAKAIYD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 266 LIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLS-SLRMIKSGGAPLGKELEDTVRAKFpqaRLGQGYGMTEA-GPVLAmCL 343
Cdd:cd12118 216 LIEKHKVTHFCGAPTVLNMLANAPPSDARPLPhRVHVMTAGAPPPAAVLAKMEELGF---DVTHVYGLTETyGPATV-CA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 344 afAKEPFDIKPGAcgtvvRNAEMK--------------IVDPETGASLPRN--QPGEICIRGDQIMKGYLNDPEATSRTI 407
Cdd:cd12118 292 --WKPEWDELPTE-----ERARLKarqgvryvgleevdVLDPETMKPVPRDgkTIGEIVFRGNIVMKGYLKNPEATAEAF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 408 dKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQ 487
Cdd:cd12118 365 -RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAK 443
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 306440447 488 ATEDEIKQYISKQVIFYKRIKRVFFIEaIPKAPSGKIlRKN 528
Cdd:cd12118 444 VTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKI-QKF 482
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
50-530 |
1.55e-65 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 218.75 E-value: 1.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQA 129
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 130 cyyekvkdfaresdvkvmcvdsapdgclhfseltqadeneapqvdispDDVVALPYSSGTTGLPKGVMLTHK---GLITS 206
Cdd:cd05972 81 ------------------------------------------------EDPALIYFTSGTTGLPKGVLHTHSyplGHIPT 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 207 VAQQVDgdnpnlyFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILI--MPKFEIGSLLGLIEKYKVSIAPVVPPVMMS 284
Cdd:cd05972 113 AAYWLG-------LRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVyeGPRFDAERILELLERYGVTSFCGPPTAYRM 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 285 IAKsPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFpQARLGQGYGMTEAGPVLAMCLAFakepfDIKPGACGTVVRNA 364
Cdd:cd05972 186 LIK-QDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAAT-GLPIRDGYGQTETGLTVGNFPDM-----PVKPGSMGRPTPGY 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 365 EMKIVDPEtGASLPRNQPGEICIRGD--QIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGF 442
Cdd:cd05972 259 DVAIIDDD-GRELPPGEEGDIAIKLPppGLFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 443 QVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATE---DEIKQYISKQVIFYKRIKRVFFIEAIPKA 519
Cdd:cd05972 337 RIGPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEelaEELQGHVKKVLAPYKYPREIEFVEELPKT 416
|
490
....*....|.
gi 306440447 520 PSGKILRKNLK 530
Cdd:cd05972 417 ISGKIRRVELR 427
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
49-531 |
2.73e-64 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 216.09 E-value: 2.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 49 VYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQ 128
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 129 ACYyekvkdfaRESDVKVMcvdsapdgclhfseltqadeneapqvdisPDDVVALPYSSGTTGLPKGVMLTHKGLITSVA 208
Cdd:cd05903 81 ERF--------RQFDPAAM-----------------------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 209 QQVDgdnpNLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKS 288
Cdd:cd05903 124 QYAE----RLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMMGATPFLTDLLNA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 289 PDLDKHDLSSLRMIKSGGAPLGKELedTVRAkfpQARLG----QGYGMTEAGPVLAMClafakEPFDIKPGAC--GTVVR 362
Cdd:cd05903 200 VEEAGEPLSRLRTFVCGGATVPRSL--ARRA---AELLGakvcSAYGSTECPGAVTSI-----TPAPEDRRLYtdGRPLP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 363 NAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTiDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGF 442
Cdd:cd05903 270 GVEIKVVD-DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADA-APEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 443 QVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQ-VIFYKRIKRVFFIEAIPKAPS 521
Cdd:cd05903 348 NIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPS 427
|
490
....*....|
gi 306440447 522 GKILRKNLKE 531
Cdd:cd05903 428 GKVQKFRLRE 437
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
38-530 |
6.20e-64 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 215.03 E-value: 6.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 38 KPCLINGanGDVYTYADVELTARRVASGL-NKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAElakh 116
Cdd:cd05958 1 RTCLRSP--EREWTYRDLLALANRIANVLvGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKE---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 117 akasrakllitqacyYEKVKDFARESdvKVMCVDsapdgclhfsELTQADeneapqvdispdDVVALPYSSGTTGLPKGV 196
Cdd:cd05958 75 ---------------LAYILDKARIT--VALCAH----------ALTASD------------DICILAFTSGTTGAPKAT 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 197 MLTHKGLITSV---AQQVDGDNPnlyfhsEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVS 273
Cdd:cd05958 116 MHFHRDPLASAdryAVNVLRLRE------DDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLLLSAIARYKPT 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 274 IAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFpQARLGQGYGMTEAGPVLamclaFAKEPFDIK 353
Cdd:cd05958 190 VLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKEAT-GIPIIDGIGSTEMFHIF-----ISARPGDAR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 354 PGACGTVVRNAEMKIVDPEtGASLPRNQPGEICIRGDQimkGYLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIVDRL 433
Cdd:cd05958 264 PGATGKPVPGYEAKVVDDE-GNPVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRS 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 434 KELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATED---EIKQYISKQVIFYKRIKRV 510
Cdd:cd05958 340 DDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVlarELQDHAKAHIAPYKYPRAI 419
|
490 500
....*....|....*....|
gi 306440447 511 FFIEAIPKAPSGKILRKNLK 530
Cdd:cd05958 420 EFVTELPRTATGKLQRFALR 439
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
35-530 |
6.55e-64 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 217.24 E-value: 6.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 35 HSSKPCLI-NGANGDV--YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPA 111
Cdd:PRK08008 20 YGHKTALIfESSGGVVrrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 112 ELAKHAKASRAKLLITQACYYEKVKDFARESD--VKVMCV----DSAPDGCLHFSEL--TQADE-NEAPQvdISPDDVVA 182
Cdd:PRK08008 100 ESAWILQNSQASLLVTSAQFYPMYRQIQQEDAtpLRHICLtrvaLPADDGVSSFTQLkaQQPATlCYAPP--LSTDDTAE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 183 LPYSSGTTGLPKGVMLTHKGLITS---VAQQVDgdnpnlyFHSEDVILCVLPMFHI-YALNSIMlCGLRVGAPILIMPKF 258
Cdd:PRK08008 178 ILFTSGTTSRPKGVVITHYNLRFAgyySAWQCA-------LRDDDVYLTVMPAFHIdCQCTAAM-AAFSAGATFVLLEKY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 259 EIGSLLGLIEKYKVSIAPVVPPV---MMSIAKSPDLDKHDLSSLRMIksggAPLGKELEDTVRAKFpQARLGQGYGMTEA 335
Cdd:PRK08008 250 SARAFWGQVCKYRATITECIPMMirtLMVQPPSANDRQHCLREVMFY----LNLSDQEKDAFEERF-GVRLLTSYGMTET 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 336 gpvlaMCLAFAKEPFDIK-------PGACgtvvrnAEMKIVDpETGASLPRNQPGEICIRG---DQIMKGYLNDPEATSR 405
Cdd:PRK08008 325 -----IVGIIGDRPGDKRrwpsigrPGFC------YEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 406 TIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEK 485
Cdd:PRK08008 393 VLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEG 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 306440447 486 SQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLK 530
Cdd:PRK08008 473 ETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
51-530 |
1.04e-63 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 214.25 E-value: 1.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQAc 130
Cdd:cd05919 12 TYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 131 yyekvkdfaresdvkvmcvdsapdgclhfseltqadeneapqvdispDDVVALPYSSGTTGLPKGVMLTHKGLITSV--- 207
Cdd:cd05919 91 -----------------------------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFAdam 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 208 AQQVDGDNPNlyfhseDVILCVLPMFHIYAL-NSIMLcGLRVGAPILIMPKFEIGS-LLGLIEKYKVSIAPVVPPVMMSI 285
Cdd:cd05919 124 AREALGLTPG------DRVFSSAKMFFGYGLgNSLWF-PLAVGASAVLNPGWPTAErVLATLARFRPTVLYGVPTFYANL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 286 AKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLgQGYGMTEAGPVLamclaFAKEPFDIKPGACGTVVRNAE 365
Cdd:cd05919 197 LDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPIL-DGIGATEVGHIF-----LSNRPGAWRLGSTGRPVPGYE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 366 MKIVDPEtGASLPRNQPGEICIRGDQIMKGYLNDPEaTSRTIDKEGWLHTGdigyiddddELFIVD---------RLKEL 436
Cdd:cd05919 271 IRLVDEE-GHTIPPGEEGDLLVRGPSAAVGYWNNPE-KSRATFNGGWYRTG---------DKFCRDadgwythagRADDM 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 437 IKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVV---KSEKSQATEDEIKQYISKQVIFYKRIKRVFFI 513
Cdd:cd05919 340 LKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVlksPAAPQESLARDIHRHLLERLSAHKVPRRIAFV 419
|
490
....*....|....*..
gi 306440447 514 EAIPKAPSGKILRKNLK 530
Cdd:cd05919 420 DELPRTATGKLQRFKLR 436
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
45-534 |
1.24e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 215.44 E-value: 1.24e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 45 ANGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKL 124
Cdd:PRK09088 18 ALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 125 LITQA------CYYEKVKDFARESDvkvmcvdsapdgclhfseltQADENEAPQVDisPDDVVALPYSSGTTGLPKGVML 198
Cdd:PRK09088 98 LLGDDavaagrTDVEDLAAFIASAD--------------------ALEPADTPSIP--PERVSLILFTSGTSGQPKGVML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 199 THKGLIT-----SVAQQVDgdnpnlyfhSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVS 273
Cdd:PRK09088 156 SERNLQQtahnfGVLGRVD---------AHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDPALG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 274 IAPV--VPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPlgkELEDTVRAKFPQA-RLGQGYGMTEAGPVLAMCLAFAKepF 350
Cdd:PRK09088 227 ITHYfcVPQMAQAFRAQPGFDAAALRHLTALFTGGAP---HAAEDILGWLDDGiPMVDGFGMSEAGTVFGMSVDCDV--I 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 351 DIKPGACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIV 430
Cdd:PRK09088 302 RAKAGAAGIPTPTVQTRVVD-DQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 431 DRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRV 510
Cdd:PRK09088 381 DRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHL 460
|
490 500
....*....|....*....|....
gi 306440447 511 FFIEAIPKAPSGKILRKNLKEKLA 534
Cdd:PRK09088 461 RLVDALPRTASGKLQKARLRDALA 484
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
32-532 |
2.20e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 216.01 E-value: 2.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 32 LSNHSSKPCLINGanGDVYTYAdvELTAR--RVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFst 109
Cdd:PRK06188 22 LKRYPDRPALVLG--DTRLTYG--QLADRisRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 110 pAELAKHA----KASRAKLLITQACYYEKVKDF-ARESDVK-VMCVDSAPDGClhfSELTQADENE-APQVDIS-PDDVV 181
Cdd:PRK06188 96 -GSLDDHAyvleDAGISTLIVDPAPFVERALALlARVPSLKhVLTLGPVPDGV---DLLAAAAKFGpAPLVAAAlPPDIA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 182 ALPYSSGTTGLPKGVMLTHKGLIT-SVAQQVDGDNPnlyfhsEDV-ILCVLPMFHiyALNSIMLCGLRVGAPILIMPKFE 259
Cdd:PRK06188 172 GLAYTGGTTGKPKGVMGTHRSIATmAQIQLAEWEWP------ADPrFLMCTPLSH--AGGAFFLPTLLRGGTVIVLAKFD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 260 IGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLgkeleDTVRAKFPQARLG----QGYGMTEA 335
Cdd:PRK06188 244 PAEVLRAIEEQRITATFLVPTMIYALLDHPDLRTRDLSSLETVYYGASPM-----SPVRLAEAIERFGpifaQYYGQTEA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 336 GpvlaMCLAF-AKEPFDIKP----GACGTVVRNAEMKIVDPEtGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIdKE 410
Cdd:PRK06188 319 P----MVITYlRKRDHDPDDpkrlTSCGRPTPGLRVALLDED-GREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 411 GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATE 490
Cdd:PRK06188 393 GWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDA 472
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 306440447 491 DEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEK 532
Cdd:PRK06188 473 AELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
47-531 |
3.20e-63 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 216.28 E-value: 3.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 47 GDVYTYADVELTARRVASGL-NKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLL 125
Cdd:PRK08751 48 GKTITYREADQLVEQFAAYLlGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 126 IT---------QACYYEKVK-----------DFARES-------DVKVMCVDSAPDGCLHFSE-LTQADENEAPQVDISP 177
Cdd:PRK08751 128 VVidnfgttvqQVIADTPVKqvittglgdmlGFPKAAlvnfvvkYVKKLVPEYRINGAIRFREaLALGRKHSMPTLQIEP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 178 DDVVALPYSSGTTGLPKGVMLTHKGLITSVaQQVDG--DNPNLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGA-PILI 254
Cdd:PRK08751 208 DDIAFLQYTGGTTGVAKGAMLTHRNLVANM-QQAHQwlAGTGKLEEGCEVVITALPLYHIFALTANGLVFMKIGGcNHLI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 255 MPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRaKFPQARLGQGYGMTE 334
Cdd:PRK08751 287 SNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWK-QVTGLTLVEAYGLTE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 335 AGPvlAMCLafakEPFDIKP--GACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGW 412
Cdd:PRK08751 366 TSP--AACI----NPLTLKEynGSIGLPIPSTDACIKD-DAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGW 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 413 LHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSqATEDE 492
Cdd:PRK08751 439 LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPA-LTAED 517
|
490 500 510
....*....|....*....|....*....|....*....
gi 306440447 493 IKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKE 531
Cdd:PRK08751 518 VKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRD 556
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
50-527 |
2.93e-62 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 210.91 E-value: 2.93e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQA 129
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 130 cyyekvkdfaresdvkvmcvdsapdgclhfseltqadeneapqvdisPDDVVALPYSSGTTGLPKGVMLTHKglitSVAQ 209
Cdd:cd05907 86 -----------------------------------------------PDDLATIIYTSGTTGRPKGVMLSHR----NILS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 210 QVDGDNPNLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIgsLLGLIEKYKVSIAPVVPPVM------M 283
Cdd:cd05907 115 NALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAET--LLDDLSEVRPTVFLAVPRVWekvyaaI 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 284 SIAKSPDL-----DKHDLSSLRMIKSGGAPLGKELedtvrAKFPQArLG----QGYGMTEAGPVLAMCLafakePFDIKP 354
Cdd:cd05907 193 KVKAVPGLkrklfDLAVGGRLRFAASGGAPLPAEL-----LHFFRA-LGipvyEGYGLTETSAVVTLNP-----PGDNRI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 355 GACGTVVRNAEMKIVDPetgaslprnqpGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIVDRLK 434
Cdd:cd05907 262 GTVGKPLPGVEVRIADD-----------GEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKK 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 435 ELIKY-KGFQVAPAELEALLIAHPEISDAAVVG--------------------LKDEDAGEVPVAFVVKSEKSQAT-EDE 492
Cdd:cd05907 331 DLIITsGGKNISPEPIENALKASPLISQAVVIGdgrpflvalivpdpealeawAEEHGIAYTDVAELAANPAVRAEiEAA 410
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 306440447 493 IKQyISKQVIFYKRIKRV------FFIEAIPKAPSGKILRK 527
Cdd:cd05907 411 VEA-ANARLSRYEQIKKFlllpepFTIENGELTPTLKLKRP 450
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-530 |
2.21e-61 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 208.44 E-value: 2.21e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 49 VYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITq 128
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 129 acyyekvkdfaresdvkvmcvdsapDGclhfseltqadeneapqvdisPDDVVALPYSSGTTGLPKGVMLTHKGLItsva 208
Cdd:cd05971 85 -------------------------DG---------------------SDDPALIIYTSGTTGPPKGALHAHRVLL---- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 209 qqvdGDNPNLYF------HSEDVILCVLPMFHIYALNSIMLCGLRVGAPILI--MPKFEIGSLLGLIEKYKVSIAPVVPP 280
Cdd:cd05971 115 ----GHLPGVQFpfnlfpRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAhrMTKFDPKAALDLMSRYGVTTAFLPPT 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 281 VMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFpQARLGQGYGMTEAGPVLAMCLAFakepFDIKPGACGTV 360
Cdd:cd05971 191 ALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQF-GVEVNEFYGQTECNLVIGNCSAL----FPIKPGSMGKP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 361 VRNAEMKIVDPEtGASLPRNQPGEICIRGDQ--IMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFIVDRLKELIK 438
Cdd:cd05971 266 IPGHRVAIVDDN-GTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVIT 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 439 YKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKS---EKSQATEDEIKQYISKQVIFYKRIKRVFFIEA 515
Cdd:cd05971 344 SSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNpgeTPSDALAREIQELVKTRLAAHEYPREIEFVNE 423
|
490
....*....|....*
gi 306440447 516 IPKAPSGKILRKNLK 530
Cdd:cd05971 424 LPRTATGKIRRRELR 438
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
45-531 |
4.34e-61 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 212.12 E-value: 4.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 45 ANGDVYTYAdvELTAR--RVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGaIITAANPFSTPAELAKHAKASRA 122
Cdd:PRK07529 54 DRPETWTYA--ELLADvtRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 123 KLLITQACY-----YEKVKDFARE-SDVK-VMCVDSAPDGCLHFSELTQADENEAPQVD--------------------I 175
Cdd:PRK07529 131 KVLVTLGPFpgtdiWQKVAEVLAAlPELRtVVEVDLARYLPGPKRLAVPLIRRKAHARIldfdaelarqpgdrlfsgrpI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 176 SPDDVVALPYSSGTTGLPKGVMLTHKGLITS--VAQQVDGDNPnlyfhsEDVILCVLPMFHIYALNSIMLCGLRVGAPIL 253
Cdd:PRK07529 211 GPDDVAAYFHTGGTTGMPKLAQHTHGNEVANawLGALLLGLGP------GDTVFCGLPLFHVNALLVTGLAPLARGAHVV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 254 IMP------KFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPdLDKHDLSSLRMIKSGGAPLGKEledtVRAKFpQARLG 327
Cdd:PRK07529 285 LATpqgyrgPGVIANFWKIVERYRINFLSGVPTVYAALLQVP-VDGHDISSLRYALCGAAPLPVE----VFRRF-EAATG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 328 ----QGYGMTEAGPVLAMclAFAKEPfdIKPGACGTVVRNAEMKIV--DPETGAS--LPRNQPGEICIRGDQIMKGYLND 399
Cdd:PRK07529 359 vrivEGYGLTEATCVSSV--NPPDGE--RRIGSVGLRLPYQRVRVVilDDAGRYLrdCAVDEVGVLCIAGPNVFSGYLEA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 400 PEATSRTIDkEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAF 479
Cdd:PRK07529 435 AHNKGLWLE-DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAY 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 306440447 480 VVKSEKSQATEDEIKQYISKQVifYKRI---KRVFFIEAIPKAPSGKILRKNLKE 531
Cdd:PRK07529 514 VQLKPGASATEAELLAFARDHI--AERAavpKHVRILDALPKTAVGKIFKPALRR 566
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
47-533 |
1.53e-60 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 208.83 E-value: 1.53e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 47 GDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLI 126
Cdd:PRK06087 47 GASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFF 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 127 TQAcyYEKVKDFARE-----SDVK----VMCVDS-APD-GCLHFSELTQADENEAPQVDISPDDVVALPYSSGTTGLPKG 195
Cdd:PRK06087 127 APT--LFKQTRPVDLilplqNQLPqlqqIVGVDKlAPAtSSLSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 196 VMLTHKGLITSVAQQVDGDNPNlyfhSEDVILCVLPMFH----IYALNSIMLCGLRVgapiLIMPKFEIGSLLGLIEKYK 271
Cdd:PRK06087 205 VMLTHNNILASERAYCARLNLT----WQDVFMMPAPLGHatgfLHGVTAPFLIGARS----VLLDIFTPDACLALLEQQR 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 272 VSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELedTVRAKFPQARLGQGYGMTEAGPVLAMCLAfakEPFD 351
Cdd:PRK06087 277 CTCMLGATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKV--ARECQQRGIKLLSVYGSTESSPHAVVNLD---DPLS 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 352 IKPGACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIVD 431
Cdd:PRK06087 352 RFMHTDGYAAAGVEIKVVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 432 RLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVV--KSEKSQATEDEIKQYISKQVIFYKRIKR 509
Cdd:PRK06087 431 RKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVlkAPHHSLTLEEVVAFFSRKRVAKYKYPEH 510
|
490 500
....*....|....*....|....*...
gi 306440447 510 VFFIEAIPKAPSGKI----LRKNLKEKL 533
Cdd:PRK06087 511 IVVIDKLPRTASGKIqkflLRKDIMRRL 538
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
40-536 |
1.30e-59 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 205.11 E-value: 1.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 40 CLINGANGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKA 119
Cdd:PRK07514 19 PFIETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 120 SRAKLLITQACYYEKVKDFARESDVK-VMCVDSAPDGCLhfSELTQADENEAPQVDISPDDVVALPYSSGTTGLPKGVML 198
Cdd:PRK07514 99 AEPALVVCDPANFAWLSKIAAAAGAPhVETLDADGTGSL--LEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKGAML 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 199 THKGLITSVAQQVDgdnpnlY--FHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVSIAp 276
Cdd:PRK07514 177 SHGNLLSNALTLVD------YwrFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLALMPRATVMMG- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 277 vVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLgkeLEDTVRAkFpQARLGQG----YGMTEAGpvlaMclaFAKEPFDI 352
Cdd:PRK07514 250 -VPTFYTRLLQEPRLTREAAAHMRLFISGSAPL---LAETHRE-F-QERTGHAilerYGMTETN----M---NTSNPYDG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 353 K--PGACGTVVRNAEMKIVDPETGASLPRNQPGEICIRGDQIMKGYLNDPEATS---------RT-----IDKEGWLHtg 416
Cdd:PRK07514 317 ErrAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAeefradgffITgdlgkIDERGYVH-- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 417 digyiddddelfIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQY 496
Cdd:PRK07514 395 ------------IVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDEAAILAA 462
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 306440447 497 ISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEKLAGI 536
Cdd:PRK07514 463 LKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQYADL 502
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
23-529 |
1.35e-59 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 204.48 E-value: 1.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 23 PLHSYVLENLSNHSSKPCLINGanGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIIT 102
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDG--DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 103 AANPFSTPAELAKHAKASRAKLLItqacyyekVKDFARESDVKVMCVDSAPDGclhfseltqadeneapqvdispDDVVA 182
Cdd:cd05920 94 LALPSHRRSELSAFCAHAEAVAYI--------VPDRHAGFDHRALARELAESI----------------------PEVAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 183 LPYSSGTTGLPKGVMLTHKGLITSV--AQQVDGdnpnlyFHSEDVILCVLPMFHIYALNSI-MLCGLRVGAPILIMPKFE 259
Cdd:cd05920 144 FLLSGGTTGTPKLIPRTHNDYAYNVraSAEVCG------LDQDTVYLAVLPAAHNFPLACPgVLGTLLAGGRVVLAPDPS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 260 IGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFpQARLGQGYGMTEAgpvl 339
Cdd:cd05920 218 PDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVL-GCTLQQVFGMAEG---- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 340 AMCLAFAKEPFDIKPGACG-TVVRNAEMKIVDPEtGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDI 418
Cdd:cd05920 293 LLNYTRLDDPDEVIIHTQGrPMSPDDEIRVVDEE-GNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 419 GYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEdEIKQYIS 498
Cdd:cd05920 372 VRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAA-QLRRFLR 450
|
490 500 510
....*....|....*....|....*....|..
gi 306440447 499 KQVIF-YKRIKRVFFIEAIPKAPSGKILRKNL 529
Cdd:cd05920 451 ERGLAaYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
51-529 |
5.76e-59 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 201.91 E-value: 5.76e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQAC 130
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 131 YYEKVKDfaresdvkvmcvdsapdgCLHFSELTQADENE-APQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLITSVAq 209
Cdd:TIGR01923 81 LEEKDFQ------------------ADSLDRIEAAGRYEtSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAV- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 210 qvdGDNPNLYFHSEDVILCVLPMFHIYALNSIMLCgLRVGAPILIMPKFeiGSLLGLIEKYKVSIAPVVPPVMMSIAKSp 289
Cdd:TIGR01923 142 ---GSKENLGFTEDDNWLLSLPLYHISGLSILFRW-LIEGATLRIVDKF--NQLLEMIANERVTHISLVPTQLNRLLDE- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 290 dldKHDLSSLRMIKSGGAPLGKELEDTVRAK-FPqarLGQGYGMTEagpvlaMC---LAFAKEPFDIKPGAcGTVVRNAE 365
Cdd:TIGR01923 215 ---GGHNENLRKILLGGSAIPAPLIEEAQQYgLP---IYLSYGMTE------TCsqvTTATPEMLHARPDV-GRPLAGRE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 366 MKI-VDPETGAslprnqpGEICIRGDQIMKGYLNDPEATSrTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQV 444
Cdd:TIGR01923 282 IKIkVDNKEGH-------GEIMVKGANLMKGYLYQGELTP-AFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENI 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 445 APAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVV-KSEKSQAtedEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGK 523
Cdd:TIGR01923 354 YPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIVsESDISQA---KLIAYLTEKLAKYKVPIAFEKLDELPYNASGK 430
|
....*.
gi 306440447 524 ILRKNL 529
Cdd:TIGR01923 431 ILRNQL 436
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
50-526 |
9.04e-59 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 201.90 E-value: 9.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITqa 129
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 130 cyyekvkdfareSDvkvmcvdsapdgclhfseltqadeneapqvdisPDDVVALPYSSGTTGLPKGVMLTHKGLITSVaq 209
Cdd:cd05914 86 ------------SD---------------------------------EDDVALINYTSGTTGNSKGVMLTYRNIVSNV-- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 210 qvDGDNPNLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEiGSLLGLIEKYKVS--IAPVVPPVMMSIAK 287
Cdd:cd05914 119 --DGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIP-SAKIIALAFAQVTptLGVPVPLVIEKIFK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 288 SPDLDKHDLS-----------------------------SLRMIKSGGAPLGKELEDTVR-AKFPQArlgQGYGMTEAGP 337
Cdd:cd05914 196 MDIIPKLTLKkfkfklakkinnrkirklafkkvheafggNIKEFVIGGAKINPDVEEFLRtIGFPYT---IGYGMTETAP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 338 VLAmclafAKEPFDIKPGACGTVVRNAEMKIVDPEtgaslPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGD 417
Cdd:cd05914 273 IIS-----YSPPNRIRLGSAGKVIDGVEVRIDSPD-----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGD 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 418 IGYIDDDDELFIVDRLKELI-KYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEV---PVAFVVKSEKSQATEDEI 493
Cdd:cd05914 343 LGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAyidPDFLDVKALKQRNIIDAI 422
|
490 500 510
....*....|....*....|....*....|....*...
gi 306440447 494 KQY----ISKQVIFYKRIKRVFFI-EAIPKAPSGKILR 526
Cdd:cd05914 423 KWEvrdkVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
61-530 |
1.34e-58 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 201.51 E-value: 1.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 61 RVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASH----RGAIITAANPFSTPAELAKHAKASRAKLLITQACYYEKVK 136
Cdd:cd05922 5 AAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYaggrLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 137 DFARESDVKVMCVDSapdgclhfsELTQADENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLIT---SVAQQVDg 213
Cdd:cd05922 85 DALPASPDPGTVLDA---------DGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLAnarSIAEYLG- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 214 dnpnlyFHSEDVILCVLPMFHIYALnSIMLCGLRVGAPILIMPKFEIG-SLLGLIEKYKVSIAPVVPPvMMSIAKSPDLD 292
Cdd:cd05922 155 ------ITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDGVLDdAFWEDLREHGATGLAGVPS-TYAMLTRLGFD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 293 KHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEAGPVLAMCLAfakEPFDIKPGACGTVVRNAEMKIVDPE 372
Cdd:cd05922 227 PAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPP---ERILEKPGSIGLAIPGGEFEILDDD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 373 tGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEAL 452
Cdd:cd05922 304 -GTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAA 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 306440447 453 LIAHPEISDAAVVGLkDEDAGEVPVAFVVKSEKSQAteDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLK 530
Cdd:cd05922 383 ARSIGLIIEAAAVGL-PDPLGEKLALFVTAPDKIDP--KDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
39-532 |
4.40e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 201.29 E-value: 4.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 39 PCLINGANGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAK 118
Cdd:PRK08276 1 PAVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 119 ASRAKLLITQACYYEKVKDFARES--DVKV-MCVDSAPDGCLHFSELTqadeneAPQVDISPDDVVA---LPYSSGTTGL 192
Cdd:PRK08276 81 DSGAKVLIVSAALADTAAELAAELpaGVPLlLVVAGPVPGFRSYEEAL------AAQPDTPIADETAgadMLYSSGTTGR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 193 PKGVM--LTHKGLITSVAQQVDGDNPNLYFHSEDVILCVLPMFHIYALNSIMLCgLRVGAPILIMPKFEIGSLLGLIEKY 270
Cdd:PRK08276 155 PKGIKrpLPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFGMSA-LALGGTVVVMEKFDAEEALALIERY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 271 KVSIAPVVPPVMMSIAKSPD--LDKHDLSSLRMIKSGGAP------------LGKELEDTvrakfpqarlgqgYGMTEAG 336
Cdd:PRK08276 234 RVTHSQLVPTMFVRMLKLPEevRARYDVSSLRVAIHAAAPcpvevkramidwWGPIIHEY-------------YASSEGG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 337 pvlAMCLAFAKEPFDiKPGACGTVVrNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTG 416
Cdd:PRK08276 301 ---GVTVITSEDWLA-HPGSVGKAV-LGEVRILD-EDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 417 DIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAfVVK----SEKSQATEDE 492
Cdd:PRK08276 375 DVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA-VVQpadgADAGDALAAE 453
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 306440447 493 IKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEK 532
Cdd:PRK08276 454 LIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDR 493
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
50-531 |
5.93e-57 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 198.14 E-value: 5.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQA 129
Cdd:TIGR02262 31 LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 130 CYYEKVKDFARESD--VKVMCVDSAPDGCLHFSELTQADENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLITSv 207
Cdd:TIGR02262 111 ALLPVIKAALGKSPhlEHRVVVGRPEAGEVQLAELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWT- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 208 AQQVDGdnPNLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEI-GSLLGLIEKYKVSIAPVVPPVMMSIA 286
Cdd:TIGR02262 190 AELYAR--NTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERPTpDAVFDRLRRHQPTIFYGVPTLYAAML 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 287 KSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLgQGYGMTEAGPVLamclaFAKEPFDIKPGACGTVVRNAEM 366
Cdd:TIGR02262 268 ADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIV-DGIGSTEMLHIF-----LSNLPGDVRYGTSGKPVPGYRL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 367 KIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEgWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAP 446
Cdd:TIGR02262 342 RLVG-DGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQGE-WTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSP 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 447 AELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILR 526
Cdd:TIGR02262 420 FEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQR 499
|
....*
gi 306440447 527 KNLKE 531
Cdd:TIGR02262 500 FKLRE 504
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
47-534 |
1.23e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 198.25 E-value: 1.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 47 GDV-YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLL 125
Cdd:PRK08162 40 GDRrRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 126 ITQACYYEKVKDFARESDVKVMCV----DSAPDGCLHFSE------LTQADENEAPQVdisPDD---VVALPYSSGTTGL 192
Cdd:PRK08162 120 IVDTEFAEVAREALALLPGPKPLVidvdDPEYPGGRFIGAldyeafLASGDPDFAWTL---PADewdAIALNYTSGTTGN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 193 PKGVMLTHKG-LITSVAQQVDGDNPNlyfHSedVILCVLPMFH---------IYALNSIMLCgLRvgapilimpKFEIGS 262
Cdd:PRK08162 197 PKGVVYHHRGaYLNALSNILAWGMPK---HP--VYLWTLPMFHcngwcfpwtVAARAGTNVC-LR---------KVDPKL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 263 LLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLS-SLRMIKSGGAPLGKELEDTVRAKFpqaRLGQGYGMTEA-GPVlA 340
Cdd:PRK08162 262 IFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDhPVHAMVAGAAPPAAVIAKMEEIGF---DLTHVYGLTETyGPA-T 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 341 MClafAKEP-FDIKPGAcgtvvRNAEMK--------------IVDPETGASLPRNQP--GEICIRGDQIMKGYLNDPEAT 403
Cdd:PRK08162 338 VC---AWQPeWDALPLD-----ERAQLKarqgvryplqegvtVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKAT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 404 SRTIdKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKS 483
Cdd:PRK08162 410 EEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELK 488
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 306440447 484 EKSQATEDEIKQYISKQVIFYKRIKRVFFIEaIPKAPSGKI----LRKNLKEKLA 534
Cdd:PRK08162 489 DGASATEEEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIqkfvLREQAKSLKA 542
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
47-531 |
1.51e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 198.04 E-value: 1.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 47 GDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLI 126
Cdd:PRK06164 33 DRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 127 TQACYyeKVKDFAR-------ESD-----VKVMCVDS----APDGCLHFSELTQAD--ENEAPQVDISPDDVVALPYS-S 187
Cdd:PRK06164 113 VWPGF--KGIDFAAilaavppDALpplraIAVVDDAAdatpAPAPGARVQLFALPDpaPPAAAGERAADPDAGALLFTtS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 188 GTTGLPKGVM-----LTHKGLITSVAQQVDGDnpnlyfhseDVILCVLPMFHIYALNSImLCGLRVGAPILIMPKFEIGS 262
Cdd:PRK06164 191 GTTSGPKLVLhrqatLLRHARAIARAYGYDPG---------AVLLAALPFCGVFGFSTL-LGALAGGAPLVCEPVFDAAR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 263 LLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKhDLSSLRMIKSGG-APLGKELEDTVRAK-FPQARLgqgYGMTEagpVLA 340
Cdd:PRK06164 261 TARALRRHRVTHTFGNDEMLRRILDTAGERA-DFPSARLFGFASfAPALGELAALARARgVPLTGL---YGSSE---VQA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 341 MCLAF-AKEPFDIKPGACGTVVR-NAEMKIVDPETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDI 418
Cdd:PRK06164 334 LVALQpATDPVSVRIEGGGRPASpEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 419 GYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLkDEDAGEVPVAFVVKSEKSQATEDEIKQYIS 498
Cdd:PRK06164 414 GYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA-TRDGKTVPVAFVIPTDGASPDEAGLMAACR 492
|
490 500 510
....*....|....*....|....*....|....*.
gi 306440447 499 KQVIFYKRIKRVFFIEAIPKAPSG---KILRKNLKE 531
Cdd:PRK06164 493 EALAGFKVPARVQVVEAFPVTESAngaKIQKHRLRE 528
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
51-531 |
2.61e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 197.46 E-value: 2.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQAC 130
Cdd:PRK07788 76 TYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 131 YYEKVKDFARESD---VKVMCVDSAP---DGCLHFSELTQADENEAPQVDISPDDVVALpySSGTTGLPKGVMLTHKGLI 204
Cdd:PRK07788 156 FTDLLSALPPDLGrlrAWGGNPDDDEpsgSTDETLDDLIAGSSTAPLPKPPKPGGIVIL--TSGTTGTPKGAPRPEPSPL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 205 TSVAQQVDgdnpNLYFHSEDVILCVLPMFHIYALNSIMLcGLRVGAPILIMPKFEIGSLLGLIEKYKVSiAPVVPPVMMS 284
Cdd:PRK07788 234 APLAGLLS----RVPFRAGETTLLPAPMFHATGWAHLTL-AMALGSTVVLRRRFDPEATLEDIAKHKAT-ALVVVPVMLS 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 285 -IAKSPD--LDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQaRLGQGYGMTEAgpvlamclAFAK----EPFDIKPGAC 357
Cdd:PRK07788 308 rILDLGPevLAKYDTSSLKIIFVSGSALSPELATRALEAFGP-VLYNLYGSTEV--------AFATiatpEDLAEAPGTV 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 358 GTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPeaTSRTIDkeGWLHTGDIGYIDDDDELFIVDRLKELI 437
Cdd:PRK07788 379 GRPPKGVTVKILD-ENGNEVPRGVVGRIFVGNGFPFEGYTDGR--DKQIID--GLLSSGDVGYFDEDGLLFVDGRDDDMI 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 438 KYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIP 517
Cdd:PRK07788 454 VSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELP 533
|
490
....*....|....
gi 306440447 518 KAPSGKILRKNLKE 531
Cdd:PRK07788 534 RNPTGKVLKRELRE 547
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
38-531 |
1.53e-55 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 195.36 E-value: 1.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 38 KPCLIngANGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHA 117
Cdd:PRK06155 37 RPLLV--FGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHIL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 118 KASRAKLLITQACYYEKVK--DFARESDVKVMCVDSAPDGC----LHFSELTQADEnEAPQVDISPDDVVALPYSSGTTG 191
Cdd:PRK06155 115 RNSGARLLVVEAALLAALEaaDPGDLPLPAVWLLDAPASVSvpagWSTAPLPPLDA-PAPAAAVQPGDTAAILYTSGTTG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 192 LPKGVMLTHKGL----ITSVAQqvdgdnpnLYFHSEDVILCVLPMFHIYALNSIMLCGLrVGAPILIMPKFE-------- 259
Cdd:PRK06155 194 PSKGVCCPHAQFywwgRNSAED--------LEIGADDVLYTTLPLFHTNALNAFFQALL-AGATYVLEPRFSasgfwpav 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 260 ------IGSLLGLIekykVSIapvvppvMMSIAKSPDLDKHdlsSLRMIKSGGAPlgKELEDTVRAKFpQARLGQGYGMT 333
Cdd:PRK06155 265 rrhgatVTYLLGAM----VSI-------LLSQPARESDRAH---RVRVALGPGVP--AALHAAFRERF-GVDLLDGYGST 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 334 EAGPVLAMCLAfakepfDIKPGACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQ---IMKGYLNDPEATSRTIdKE 410
Cdd:PRK06155 328 ETNFVIAVTHG------SQRPGSMGRLAPGFEARVVD-EHDQELPDGEPGELLLRADEpfaFATGYFGMPEKTVEAW-RN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 411 GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAG-EVPVAFVVKsEKSQAT 489
Cdd:PRK06155 400 LWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEdEVMAAVVLR-DGTALE 478
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 306440447 490 EDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKE 531
Cdd:PRK06155 479 PVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLRE 520
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
45-524 |
1.92e-55 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 193.70 E-value: 1.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 45 ANGDVYTYADVELTARRVASGLNKIgIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKL 124
Cdd:cd05909 3 TLGTSLTYRKLLTGAIALARKLAKM-TKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 125 LITQACYYEK---VKDFARESDVKVMCVD------SAPDGCLHFSELTQADENE---APQVDISPDDVVALPYSSGTTGL 192
Cdd:cd05909 82 VLTSKQFIEKlklHHLFDVEYDARIVYLEdlrakiSKADKCKAFLAGKFPPKWLlriFGVAPVQPDDPAVILFTSGSEGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 193 PKGVMLTHKGLITSVAQQVDGDNPNlyfhSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPK-FEIGSLLGLIEKYK 271
Cdd:cd05909 162 PKGVVLSHKNLLANVEQITAIFDPN----PEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNpLDYKKIPELIYDKK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 272 VSIAPVVPPVMMSIAKSpdLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFpQARLGQGYGMTEAGPVLAMCLAFAkepfD 351
Cdd:cd05909 238 ATILLGTPTFLRGYARA--AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF-GIRILEGYGTTECSPVISVNTPQS----P 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 352 IKPGACGTVVRNAEMKIVDPETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFIVD 431
Cdd:cd05909 311 NKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 432 RLKELIKYKGFQVAPAELEALLIAH-PEISDAAVVGLKDEDAGEVPVAFVVKSEksqATEDEIKQYISK-QVIFYKRIKR 509
Cdd:cd05909 390 RLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTD---TDPSSLNDILKNaGISNLAKPSY 466
|
490
....*....|....*
gi 306440447 510 VFFIEAIPKAPSGKI 524
Cdd:cd05909 467 IHQVEEIPLLGTGKP 481
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
179-526 |
2.53e-55 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 189.02 E-value: 2.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 179 DVVALPYSSGTTGLPKGVMLTHKGLITSVAQQvdgdNPNLYFHSEDVILCVLPMFHIYALNsIMLCGLRVGAPILIMPKF 258
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQL----IHAMGLTEADVYLNMLPLFHIAGLN-LALATFHAGGANVVMEKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 259 EIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIksggapLGKELEDTVRA--KFPQARLGQGYGMTEAG 336
Cdd:cd17637 76 DPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHV------LGLDAPETIQRfeETTGATFWSLYGQTETS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 337 PVLAMClafakePFDIKPGACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIdKEGWLHTG 416
Cdd:cd17637 150 GLVTLS------PYRERPGSAGRPGPLVRVRIVD-DNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 417 DIGYIDDDDELFIVDRL--KELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIK 494
Cdd:cd17637 222 DLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADELI 301
|
330 340 350
....*....|....*....|....*....|..
gi 306440447 495 QYISKQVIFYKRIKRVFFIEAIPKAPSGKILR 526
Cdd:cd17637 302 EFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
52-531 |
5.15e-55 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 192.99 E-value: 5.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 52 YADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQACY 131
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHADL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 132 YEKVKDfARESDVKVMCVDS----------------APDGCLHFSE-LTQADENEAPQVDiSPDDVValpYSSGTTGLPK 194
Cdd:PRK12406 94 LHGLAS-ALPAGVTVLSVPTppeiaaayrispalltPPAGAIDWEGwLAQQEPYDGPPVP-QPQSMI---YTSGTTGHPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 195 GVMLT-----HKGLITSVAQQVDGDNPNLyfhsedVILCVLPMFHiYALNSIMLCGLRVGAPILIMPKFEIGSLLGLIEK 269
Cdd:PRK12406 169 GVRRAaptpeQAAAAEQMRALIYGLKPGI------RALLTGPLYH-SAPNAYGLRAGRLGGVLVLQPRFDPEELLQLIER 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 270 YKVSIAPVVPPVMMSIAKSPD--LDKHDLSSLRMIKSGGAPLGKELEdtvrakfpQARLG-------QGYGMTEAGPVla 340
Cdd:PRK12406 242 HRITHMHMVPTMFIRLLKLPEevRAKYDVSSLRHVIHAAAPCPADVK--------RAMIEwwgpviyEYYGSTESGAV-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 341 mclAFA-KEPFDIKPGACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMK-GYLNDPEAtSRTIDKEGWLHTGDI 418
Cdd:PRK12406 312 ---TFAtSEDALSHPGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEK-RAEIDRGGFITSGDV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 419 GYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYIS 498
Cdd:PRK12406 387 GYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQLK 466
|
490 500 510
....*....|....*....|....*....|...
gi 306440447 499 KQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKE 531
Cdd:PRK12406 467 ARLAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
48-526 |
5.72e-55 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 193.61 E-value: 5.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 48 DVYTYADVELTARRVASGLNKIGiQQGDVIMLFLPSSPEFVLAFLGASHRGAIitaANPFSTPAELAKHAKA------SR 121
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAI---AVPLPPPTPGRHAERLaailadAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 122 AKLLITQACYYEKVKDFARESDVK----VMCVDSAPDGclhfseltqaDENEAPQVDISPDDVVALPYSSGTTGLPKGVM 197
Cdd:cd05931 99 PRVVLTTAAALAAVRAFAASRPAAgtprLLVVDLLPDT----------SAADWPPPSPDPDDIAYLQYTSGSTGTPKGVV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 198 LTHKGLITSVAQQVDGdnpnLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEI----GSLLGLIEKYKVS 273
Cdd:cd05931 169 VTHRNLLANVRQIRRA----YGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAFlrrpLRWLRLISRYRAT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 274 IAPVvPP-------VMMSIAKSPDLDkhdLSSLRMIKSGGAPLgkeLEDTVRA--------KFPQARLGQGYGMTEA--- 335
Cdd:cd05931 245 ISAA-PNfaydlcvRRVRDEDLEGLD---LSSWRVALNGAEPV---RPATLRRfaeafapfGFRPEAFRPSYGLAEAtlf 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 336 --------GPVL----AMCLAFAKEPFDIKPGA------CGTVVRNAEMKIVDPETGASLPRNQPGEICIRGDQIMKGYL 397
Cdd:cd05931 318 vsggppgtGPVVlrvdRDALAGRAVAVAADDPAarelvsCGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYW 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 398 NDPEATSRT------IDKEGWLHTgdigyiddddELFIVDRLKELIKYKGFQVAPAELEA-LLIAHPEISDAAVVGLKDE 470
Cdd:cd05931 398 GRPEATAETfgalaaTDEGGWLRTgdlgf-lhdgELYITGRLKDLIIVRGRNHYPQDIEAtAEEAHPALRPGCVAAFSVP 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 306440447 471 DAGEVPVAFVVKSEKSQATED--EIKQYISKQVI--FYKRIKRVFFIE--AIPKAPSGKILR 526
Cdd:cd05931 477 DDGEERLVVVAEVERGADPADlaAIAAAIRAAVAreHGVAPADVVLVRpgSIPRTSSGKIQR 538
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
35-535 |
1.12e-54 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 192.21 E-value: 1.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 35 HSSKPCLINGANGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELA 114
Cdd:PRK13391 10 TPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 115 KHAKASRAKLLITQACYYEKVKDFARESDVKVMCV----DSAPDGCLHFSELTqADENEAPQVDISPDDvvALPYSSGTT 190
Cdd:PRK13391 90 YIVDDSGARALITSAAKLDVARALLKQCPGVRHRLvldgDGELEGFVGYAEAV-AGLPATPIADESLGT--DMLYSSGTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 191 GLPKGVM--LTHKGL-----ITSVAQqvdgdnpNLY-FHSEDVILCVLPMFHIYALNSIMLcGLRVGAPILIMPKFEIGS 262
Cdd:PRK13391 167 GRPKGIKrpLPEQPPdtplpLTAFLQ-------RLWgFRSDMVYLSPAPLYHSAPQRAVML-VIRLGGTVIVMEHFDAEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 263 LLGLIEKYKVSIAPVVPPVMMSIAKSPD--LDKHDLSSLRMIKSGGAPLGKEL-EDTVRAKFPQarLGQGYGMTEAGPVL 339
Cdd:PRK13391 239 YLALIEEYGVTHTQLVPTMFSRMLKLPEevRDKYDLSSLEVAIHAAAPCPPQVkEQMIDWWGPI--IHEYYAATEGLGFT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 340 AMclafAKEPFDIKPGACGTVVRnAEMKIVDpETGASLPRNQPGEICIRGDQIMKgYLNDPEATSRTIDKEG-WLHTGDI 418
Cdd:PRK13391 317 AC----DSEEWLAHPGTVGRAMF-GDLHILD-DDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 419 GYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATED---EIKQ 495
Cdd:PRK13391 390 GYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPAlaaELIA 469
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 306440447 496 YISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEKLAG 535
Cdd:PRK13391 470 FCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWG 509
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
46-529 |
6.96e-54 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 188.51 E-value: 6.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 46 NGDVYTYAdvELTAR--RVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPfSTPAELAKH-AKASRA 122
Cdd:cd05930 9 GDQSLTYA--ELDARanRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDP-SYPAERLAYiLEDSGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 123 KLLITQacyyekvkdfaresdvkvmcvdsapdgclhfseltqadeneapqvdisPDDVVALPYSSGTTGLPKGVMLTHKG 202
Cdd:cd05930 86 KLVLTD------------------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 203 LITsvaqQVDGDNPNLYFHSEDVILCVLPMFHIYALNSImLCGLRVGAPILIMPK---FEIGSLLGLIEKYKVSIAPVVP 279
Cdd:cd05930 118 LVN----LLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEI-FGALLAGATLVVLPEevrKDPEALADLLAEEGITVLHLTP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 280 PVMMSIAKSPDLDkhDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEAGpvlAMCLAF--AKEPFDIKPGAC 357
Cdd:cd05930 193 SLLRLLLQELELA--ALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEAT---VDATYYrvPPDDEEDGRVPI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 358 GTVVRNAEMKIVDPEtGASLPRNQPGEICIRGDQIMKGYLNDPEATS---------------RTIDKEGWLHtgdigyid 422
Cdd:cd05930 268 GRPIPNTRVYVLDEN-LRPVPPGVPGELYIGGAGLARGYLNRPELTAerfvpnpfgpgermyRTGDLVRWLP-------- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 423 dDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVI 502
Cdd:cd05930 339 -DGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLP 417
|
490 500
....*....|....*....|....*..
gi 306440447 503 FYKRIKRVFFIEAIPKAPSGKILRKNL 529
Cdd:cd05930 418 DYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
51-535 |
4.19e-52 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 186.03 E-value: 4.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQAC 130
Cdd:PRK13295 57 TYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 131 YyekvKDFARESDV-----------KVMCVDSAPDGCL--HFSELTQADENEAPQVDIS----PDDVVALPYSSGTTGLP 193
Cdd:PRK13295 137 F----RGFDHAAMArrlrpelpalrHVVVVGGDGADSFeaLLITPAWEQEPDAPAILARlrpgPDDVTQLIYTSGTTGEP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 194 KGVMLTHKGLITSVAQQVDgdnpNLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVS 273
Cdd:PRK13295 213 KGVMHTANTLMANIVPYAE----RLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAELIRTEGVT 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 274 IAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFpQARLGQGYGMTEAGPVLAMCLAfakEPFDIK 353
Cdd:PRK13295 289 FTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAAL-GAKIVSAWGMTENGAVTLTKLD---DPDERA 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 354 PGACGTVVRNAEMKIVDPEtGASLPRNQPGEICIRGDQIMKGYLNDPEATSrtIDKEGWLHTGDIGYIDDDDELFIVDRL 433
Cdd:PRK13295 365 STTDGCPLPGVEVRVVDAD-GAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG--TDADGWFDTGDLARIDADGYIRISGRS 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 434 KELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRI-KRVFF 512
Cdd:PRK13295 442 KDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLKAQKVAKQYIpERLVV 521
|
490 500
....*....|....*....|...
gi 306440447 513 IEAIPKAPSGKILRKNLKEKLAG 535
Cdd:PRK13295 522 RDALPRTPSGKIQKFRLREMLRG 544
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
50-532 |
4.92e-51 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 180.78 E-value: 4.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAAnpFST--PAELAKHAKASRAKLLIT 127
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPL--FSAfgPEAIRDRLENSEAKVLIT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 128 QACYYEKVkdfaresdvkvmcvdsapdgclhfseltqadeneapqvdiSPDDVVALPYSSGTTGLPKGVMLTHKGLIT-- 205
Cdd:cd05969 79 TEELYERT----------------------------------------DPEDPTLLHYTSGTTGTPKGVLHVHDAMIFyy 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 206 -SVAQQVDGDNPNLYFHSEDVILCVLPMFHIYA--LNsimlcglrvGAPILIMP-KFEIGSLLGLIEKYKVSI---APVV 278
Cdd:cd05969 119 fTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWApwLN---------GVTNVVYEgRFDAESWYGIIERVKVTVwytAPTA 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 279 PPVMMSIAKSPdLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFpQARLGQGYGMTEAGP-VLAMCLAFakepfDIKPGAC 357
Cdd:cd05969 190 IRMLMKEGDEL-ARKYDLSSLRFIHSVGEPLNPEAIRWGMEVF-GVPIHDTWWQTETGSiMIANYPCM-----PIKPGSM 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 358 GTVVRNAEMKIVDpETGASLPRNQPGEICIRGD--QIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFIVDRLKE 435
Cdd:cd05969 263 GKPLPGVKAAVVD-ENGNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSF-IDGWYLTGDLAYRDEDGYFWFVGRADD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 436 LIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATE---DEIKQYISKQVIFYKRIKRVFF 512
Cdd:cd05969 341 IIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDelkEEIINFVRQKLGAHVAPREIEF 420
|
490 500
....*....|....*....|
gi 306440447 513 IEAIPKAPSGKILRKNLKEK 532
Cdd:cd05969 421 VDNLPKTRSGKIMRRVLKAK 440
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
50-532 |
7.10e-51 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 182.31 E-value: 7.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQA 129
Cdd:cd05970 48 FTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 130 --CYYEKVKDFARES---DVKVMCVDSAPDGCLHFSELTQ--ADENEAPQVDISP--DDVVALPYSSGTTGLPKgvMLTH 200
Cdd:cd05970 128 edNIPEEIEKAAPECpskPKLVWVGDPVPEGWIDFRKLIKnaSPDFERPTANSYPcgEDILLVYFSSGTTGMPK--MVEH 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 201 K-----GLITSVA--QQVDGDNPNLYFHSEDVILCVLPMFHiyalnSIMLCGLRVGapILIMPKFEIGSLLGLIEKYKVS 273
Cdd:cd05970 206 DftyplGHIVTAKywQNVREGGLHLTVADTGWGKAVWGKIY-----GQWIAGAAVF--VYDYDKFDPKALLEKLSKYGVT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 274 iAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRaKFPQARLGQGYGMTEagpvlaMCLAFAKEP-FDI 352
Cdd:cd05970 279 -TFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFK-EKTGIKLMEGFGQTE------TTLTIATFPwMEP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 353 KPGACGTVVRNAEMKIVDPEtGASLPRNQPGEICIRGDQ-----IMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDEL 427
Cdd:cd05970 351 KPGSMGKPAPGYEIDLIDRE-GRSCEAGEEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 428 FIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKS---EKSQATEDEIKQYISKQVIFY 504
Cdd:cd05970 429 WFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAkgyEPSEELKKELQDHVKKVTAPY 508
|
490 500
....*....|....*....|....*...
gi 306440447 505 KRIKRVFFIEAIPKAPSGKILRKNLKEK 532
Cdd:cd05970 509 KYPRIVEFVDELPKTISGKIRRVEIRER 536
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
144-531 |
2.05e-49 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 177.18 E-value: 2.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 144 VKVMCVDSAPDGclhfseLTQADENEAPQVDISPDDVVA---LPYSSGTTGLPKGVMLTHKGLITSVAQQVDGdnPNLYF 220
Cdd:cd05929 94 CGLFTGGGALDG------LEDYEAAEGGSPETPIEDEAAgwkMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAA--ALGFG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 221 HSEDVI-LCVLPMFHIYALNSIMLcGLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPD--LDKHDLS 297
Cdd:cd05929 166 PGADSVyLSPAPLYHAAPFRWSMT-ALFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEavRNAYDLS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 298 SLRMIKSGGAPLGKELEDTVRAKFPQaRLGQGYGMTEAgpvLAMCLAFAKEPFDiKPGACGTVVRnAEMKIVDpETGASL 377
Cdd:cd05929 245 SLKRVIHAAAPCPPWVKEQWIDWGGP-IIWEYYGGTEG---QGLTIINGEEWLT-HPGSVGRAVL-GKVHILD-EDGNEV 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 378 PRNQPGEICIRGDQiMKGYLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHP 457
Cdd:cd05929 318 PPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHP 396
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 306440447 458 EISDAAVVGLKDEDAGEVPVAfVVKSEKS----QATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKE 531
Cdd:cd05929 397 KVLDAAVVGVPDEELGQRVHA-VVQPAPGadagTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
51-529 |
6.16e-49 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 176.16 E-value: 6.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYAdvELTAR--RVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLgASHR-GAIITAANPFSTPAELA---KHAKASRAKL 124
Cdd:cd05923 30 TYS--ELRARieAVAARLHARGLRPGQRVAVVLPNSVEAVIALL-ALHRlGAVPALINPRLKAAELAeliERGEMTAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 125 litqaCYYEKVKDFARESDVKVMCVDSAPDgclhFSELTQA-DENEAPQVDisPDDVVALPYSSGTTGLPKGVMLTHKGL 203
Cdd:cd05923 107 -----AVDAQVMDAIFQSGVRVLALSDLVG----LGEPESAgPLIEDPPRE--PEQPAFVFYTSGTTGLPKGAVIPQRAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 204 ITSV---AQQVdgdnpNLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPP 280
Cdd:cd05923 176 ESRVlfmSTQA-----GLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALKLIEQERVTSLFATPT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 281 VMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQgYGMTEAgpvlaMCLAFAKEPfdiKPGACGTV 360
Cdd:cd05923 251 HLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNI-YGTTEA-----MNSLYMRDA---RTGTEMRP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 361 VRNAEMKIVdpETGAS----LPRNQPGEICIR--GDQIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFIVDRLK 434
Cdd:cd05923 322 GFFSEVRIV--RIGGSpdeaLANGEEGELIVAaaADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 435 ELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSqATEDEIKQY-ISKQVIFYKRIKRVFFI 513
Cdd:cd05923 399 DMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGT-LSADELDQFcRASELADFKRPRRYFFL 477
|
490
....*....|....*.
gi 306440447 514 EAIPKAPSGKILRKNL 529
Cdd:cd05923 478 DELPKNAMNKVLRRQL 493
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
187-533 |
4.80e-48 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 169.43 E-value: 4.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 187 SGTTGLPKGVMLTHKGLITSVaqqvDGDNPNLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGL 266
Cdd:cd17630 9 SGSTGTPKAVVHTAANLLASA----AGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQALAEDLAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 267 IEKYKVSIapvVPPVMMSIAKSpDLDKHDLSSLRMIKSGGAPLGKELEDtvRAKFPQARLGQGYGMTEAGPVLAmclafA 346
Cdd:cd17630 85 PGVTHVSL---VPTQLQRLLDS-GQGPAALKSLRAVLLGGAPIPPELLE--RAADRGIPLYTTYGMTETASQVA-----T 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 347 KEPFDIKPGACGTVVRNAEMKIVDPetgaslprnqpGEICIRGDQIMKGYLNDPEATSRtiDKEGWLHTGDIGYIDDDDE 426
Cdd:cd17630 154 KRPDGFGRGGVGVLLPGRELRIVED-----------GEIWVGGASLAMGYLRGQLVPEF--NEDGWFTTKDLGELHADGR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 427 LFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKsqATEDEIKQYISKQVIFYKR 506
Cdd:cd17630 221 LTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP--ADPAELRAWLKDKLARFKL 298
|
330 340
....*....|....*....|....*..
gi 306440447 507 IKRVFFIEAIPKAPSGKILRKNLKEKL 533
Cdd:cd17630 299 PKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
17-531 |
5.84e-48 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 179.35 E-value: 5.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 17 YIPKNLPLHSYVLENLSNHSSKPCLINGANGDVyTYADVeLTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASH 96
Cdd:PRK08633 610 RKEALPPLAEAWIDTAKRNWSRLAVADSTGGEL-SYGKA-LTGALALARLLKRELKDEENVGILLPPSVAGALANLALLL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 97 RGAIITAANPFSTPAELAKHAKASRAKLLITQACYYEKVK----DFARESDVKVMCVD------SAPDGCLHF------- 159
Cdd:PRK08633 688 AGKVPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKnkgfDLELPENVKVIYLEdlkakiSKVDKLTALlaarllp 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 160 SELTQADENEapqvDISPDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQVDGDNPNlyfhSEDVILCVLPMFHIYALN 239
Cdd:PRK08633 768 ARLLKRLYGP----TFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLR----NDDVILSSLPFFHSFGLT 839
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 240 SIMLCGLRVGAPILIMPK----FEIGSLlglIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELED 315
Cdd:PRK08633 840 VTLWLPLLEGIKVVYHPDptdaLGIAKL---VAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVAD 916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 316 TVRAKFpQARLGQGYGMTEAGPVLAMCLAFAKEPFDI-----KPGACGTVVRNAEMKIVDPETGASLPRNQPGEICIRGD 390
Cdd:PRK08633 917 AFEEKF-GIRILEGYGATETSPVASVNLPDVLAADFKrqtgsKEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGP 995
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 391 QIMKGYLNDPEATS---RTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIA--HPEISDAAVV 465
Cdd:PRK08633 996 QVMKGYLGDPEKTAeviKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalGGEEVVFAVT 1075
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 466 GLKDEDAGEvpvAFVVKSEKSQATEDEIKQYISKQVI----FYKRIKRVffiEAIPKAPSGKILRKNLKE 531
Cdd:PRK08633 1076 AVPDEKKGE---KLVVLHTCGAEDVEELKRAIKESGLpnlwKPSRYFKV---EALPLLGSGKLDLKGLKE 1139
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
51-464 |
4.68e-47 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 168.98 E-value: 4.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYAdvELTAR--RVASGLNKI-GIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPfSTPAE-LAKHAKASRAKLLI 126
Cdd:TIGR01733 1 TYR--ELDERanRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDP-AYPAErLAFILEDAGARLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 127 TQACYYEKvkdfARESDVKVMCVDSapdgcLHFSELTQADENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLITS 206
Cdd:TIGR01733 78 TDSALASR----LAGLVLPVILLDP-----LELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 207 VAqqvdgDNPNLY-FHSEDVILCVLPMFHIYALNSIMLCgLRVGAPILIMP----KFEIGSLLGLIEKYKVSIAPVVPPV 281
Cdd:TIGR01733 149 LA-----WLARRYgLDPDDRVLQFASLSFDASVEEIFGA-LLAGATLVVPPedeeRDDAALLAALIAEHPVTVLNLTPSL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 282 MMSIAkspDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEAgPVLAMCLAF-AKEPFDIKPGACGTV 360
Cdd:TIGR01733 223 LALLA---AALPPALASLRLVILGGEALTPALVDRWRARGPGARLINLYGPTET-TVWSTATLVdPDDAPRESPVPIGRP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 361 VRNAEMKIVDPEtGASLPRNQPGEICIRGDQIMKGYLNDPEATS-----------------RTIDKEGWLHtgdigyidd 423
Cdd:TIGR01733 299 LANTRLYVLDDD-LRPVPVGVVGELYIGGPGVARGYLNRPELTAerfvpdpfaggdgarlyRTGDLVRYLP--------- 368
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 306440447 424 DDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAV 464
Cdd:TIGR01733 369 DGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
46-529 |
6.71e-47 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 169.74 E-value: 6.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 46 NGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLL 125
Cdd:cd05945 13 GGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 126 ITqacyyekvkdfaresdvkvmcvdsapdgclhfseltqadeneapqvdiSPDDVVALPYSSGTTGLPKGVMLTHKGLIT 205
Cdd:cd05945 93 IA------------------------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNLVS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 206 SVAQqVDGDNPnlyFHSEDVILCVLP------MFHIYalnsimlCGLRVGAPILIMPKFEIGSLLGL---IEKYKVSIAP 276
Cdd:cd05945 125 FTNW-MLSDFP---LGPGDVFLNQAPfsfdlsVMDLY-------PALASGATLVPVPRDATADPKQLfrfLAEHGITVWV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 277 VVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEA-GPVLAMclAFAKEPFD-IKP 354
Cdd:cd05945 194 STPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEAtVAVTYI--EVTPEVLDgYDR 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 355 GACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATSR---TIDKEGWLHTGDIGYIDDDDELFIVD 431
Cdd:cd05945 272 LPIGYAKPGAKLVILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAaffPDEGQRAYRTGDLVRLEADGLLFYRG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 432 RLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVV-KSEKSQATEDEIKQYISKQVIFYKRIKRV 510
Cdd:cd05945 351 RLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVpKPGAEAGLTKAIKAELAERLPPYMIPRRF 430
|
490
....*....|....*....
gi 306440447 511 FFIEAIPKAPSGKILRKNL 529
Cdd:cd05945 431 VYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
51-533 |
1.34e-46 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 170.93 E-value: 1.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELA---KHAKASRAKL--- 124
Cdd:cd05906 41 SYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPNarlRKLRHIWQLLgsp 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 125 -LITQAcyyEKVKDFARESDVKVMCVDSapdgcLHFSELTQADENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGL 203
Cdd:cd05906 121 vVLTDA---ELVAEFAGLETLSGLPGIR-----VLSIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 204 ITSVAqqvdGDNPNLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGS----LLGLIEKYKVSIApVVP 279
Cdd:cd05906 193 LARSA----GKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPTEEILAdplrWLDLIDRYRVTIT-WAP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 280 PVMMSI----AKSPDLDKHDLSSLRMIKSGGAP--------LGKELEdtvRAKFPQARLGQGYGMTEAGPVLAMCLAFAK 347
Cdd:cd05906 268 NFAFALlndlLEEIEDGTWDLSSLRYLVNAGEAvvaktirrLLRLLE---PYGLPPDAIRPAFGMTETCSGVIYSRSFPT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 348 EPFDIKP--GACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGdIGYIDDDD 425
Cdd:cd05906 345 YDHSQALefVSLGRPIPGVSMRIVD-DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTG-DLGFLDNG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 426 ELFIVDRLKELIKYKGFQVAPAELEALLIAHPEI--SDAAVVGLKDEDAG-EVPVAFVVKSEKSQATEDEIKQYISKQVI 502
Cdd:cd05906 423 NLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVepSFTAAFAVRDPGAEtEELAIFFVPEYDLQDALSETLRAIRSVVS 502
|
490 500 510
....*....|....*....|....*....|....*
gi 306440447 503 FYKRIKRVFFI----EAIPKAPSGKILRKNLKEKL 533
Cdd:cd05906 503 REVGVSPAYLIplpkEEIPKTSLGKIQRSKLKAAF 537
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
46-530 |
2.59e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 168.80 E-value: 2.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 46 NGDVYTYADVELTARRVASGLNKIGIQQGDVIMLfLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLL 125
Cdd:PRK07638 23 NDRVLTYKDWFESVCKVANWLNEKESKNKTIAIL-LENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 126 ITQACYYEKVkdfareSDVKVMCVDSapdgclhfSELTQADENEAP---QVDISPDDVVALPYSSGTTGLPKGVMLTHKG 202
Cdd:PRK07638 102 VTERYKLNDL------PDEEGRVIEI--------DEWKRMIEKYLPtyaPIENVQNAPFYMGFTSGSTGKPKAFLRAQQS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 203 LITSVAQQVDgdnpNLYFHSEDVILCVLPMFHiyalnSIMLCG----LRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVV 278
Cdd:PRK07638 168 WLHSFDCNVH----DFHMKREDSVLIAGTLVH-----SLFLYGaistLYVGQTVHLMRKFIPNQVLDKLETENISVMYTV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 279 PPVMMSIAKSPDLDKHDLSslrmIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEagpvLAMCLAFAKEPFDIKPGACG 358
Cdd:PRK07638 239 PTMLESLYKENRVIENKMK----IISSGAKWEAEAKEKIKNIFPYAKLYEFYGASE----LSFVTALVDEESERRPNSVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 359 TVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDpEATSRTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIK 438
Cdd:PRK07638 311 RPFHNVQVRICN-EAGEEVQKGEIGTVYVKSPQFFMGYIIG-GVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMIL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 439 YKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVvkseKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPK 518
Cdd:PRK07638 389 FGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII----KGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPY 464
|
490
....*....|..
gi 306440447 519 APSGKILRKNLK 530
Cdd:PRK07638 465 TNSGKIARMEAK 476
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
50-481 |
3.89e-46 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 169.70 E-value: 3.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQ--GDVIMLFLPSSPEFVLAFLgashrgaiitAANPFStpaelakhakasraklLIT 127
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISEL----------ACYAYS----------------LVT 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 128 QACY----YEKVKDFARESDVKVMCVDsapDG--CLHFSEL-TQADENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTH 200
Cdd:cd05927 60 VPLYdtlgPEAIEYILNHAEISIVFCD---AGvkVYSLEEFeKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 201 KGLITSVAQQVDGDNPNLYFHSEDVILCVLPMFHIYALNSIMLCgLRVGAPIlimpKFEIGSLLGLIEKYKV---SIAPV 277
Cdd:cd05927 137 GNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALF-LYHGAKI----GFYSGDIRLLLDDIKAlkpTVFPG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 278 VPPV--------MMSIAKSPDLDK--------HDLSSL---------------------------RMIKSGGAPLGKELE 314
Cdd:cd05927 212 VPRVlnriydkiFNKVQAKGPLKRklfnfalnYKLAELrsgvvraspfwdklvfnkikqalggnvRLMLTGSAPLSPEVL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 315 DTVRAKFpQARLGQGYGMTEagpvlamCLA--FAKEPFDIKPGACGTVVRNAEMKIVD-PETG-ASLPRNQPGEICIRGD 390
Cdd:cd05927 292 EFLRVAL-GCPVLEGYGQTE-------CTAgaTLTLPGDTSVGHVGGPLPCAEVKLVDvPEMNyDAKDPNPRGEVCIRGP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 391 QIMKGYLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEALLIAHPEISDAAVVGlkd 469
Cdd:cd05927 364 NVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFVYG--- 440
|
490
....*....|...
gi 306440447 470 eDAGEV-PVAFVV 481
Cdd:cd05927 441 -DSLKSfLVAIVV 452
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
177-530 |
6.43e-46 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 164.58 E-value: 6.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 177 PDDVVALPYSSGTTGLPKGVMLTHKGLitsVAQQVDGdNPNLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMP 256
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNE---VYNAWML-ALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 257 ------KFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDldKHDLSSLRMIKSGGAPLGKELedtvRAKFpQARLG--- 327
Cdd:cd05944 77 pagyrnPGLFDNFWKLVERYRITSLSTVPTVYAALLQVPV--NADISSLRFAMSGAAPLPVEL----RARF-EDATGlpv 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 328 -QGYGMTEAGPVLAmcLAFAKEPfdIKPGACGTVVRNAEMKIV--DPETGASLP--RNQPGEICIRGDQIMKGYLNDPEA 402
Cdd:cd05944 150 vEGYGLTEATCLVA--VNPPDGP--KRPGSVGLRLPYARVRIKvlDGVGRLLRDcaPDEVGEICVAGPGVFGGYLYTEGN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 403 TSRTIDkEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVK 482
Cdd:cd05944 226 KNAFVA-DGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQL 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 306440447 483 SEKSQATEDEIKQYISKQVIFYKRI-KRVFFIEAIPKAPSGKILRKNLK 530
Cdd:cd05944 305 KPGAVVEEEELLAWARDHVPERAAVpKHIEVLEELPVTAVGKVFKPALR 353
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
18-532 |
7.33e-46 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 168.41 E-value: 7.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 18 IPKNLPLHSYVLENLSN------HSSKPCL--INGANGDV-YTYADVELTARRVASGLNKI-GIQQGDVIMLFLPSSPEF 87
Cdd:cd05928 1 VPEYFNFASDVLDQWADkekagkRPPNPALwwVNGKGDEVkWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 88 VLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQACYYEKVKDFARES---DVKVMCVDSAPDGCLHFSELTQ 164
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECpslKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 165 ADENEAPQVDISPDDVVALPYSSGTTGLPKgvMLTHKGLITSVAQQVDGdNPNLYFHSEDVILCVLPMFHIYALNSIMLC 244
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPK--MAEHSHSSLGLGLKVNG-RYWLDLTASDIMWNTSDTGWIKSAWSSLFE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 245 GLRVGAPILI--MPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSpDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKfP 322
Cdd:cd05928 238 PWIQGACVFVhhLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQ-DLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQ-T 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 323 QARLGQGYGMTEAGpvlAMCLAFAKEpfDIKPGACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQ-----IMKGYL 397
Cdd:cd05928 316 GLDIYEGYGQTETG---LICANFKGM--KIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIRVKPirpfgLFSGYV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 398 NDPEATSRTIDKEGWLhTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPV 477
Cdd:cd05928 390 DNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVK 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 478 AFVV-----KSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEK 532
Cdd:cd05928 469 AFVVlapqfLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDK 528
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
47-529 |
8.06e-46 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 167.38 E-value: 8.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 47 GDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLI 126
Cdd:cd12117 20 DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 127 TQacyyEKVKDFARESDVKVMCVDSAPDGclhfseltqadENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLITS 206
Cdd:cd12117 100 TD----RSLAGRAGGLEVAVVIDEALDAG-----------PAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 207 VAqqvdgdNPN-LYFHSEDVILCVLP------MFHIYA--LNsimlcglrvGAPILIMPK---FEIGSLLGLIEKYKVSI 274
Cdd:cd12117 165 VK------NTNyVTLGPDDRVLQTSPlafdasTFEIWGalLN---------GARLVLAPKgtlLDPDALGALIAEEGVTV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 275 APVVPPVMMSIAkspDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEaGPVLAMCLAFAKEPFDIKP 354
Cdd:cd12117 230 LWLTAALFNQLA---DEDPECFAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTE-NTTFTTSHVVTELDEVAGS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 355 GACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATS---------------RTIDKEGWLhtgdig 419
Cdd:cd12117 306 IPIGRPIANTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGYLNRPALTAerfvadpfgpgerlyRTGDLARWL------ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 420 yidDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKsqATEDEIKQYISK 499
Cdd:cd12117 379 ---PDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGA--LDAAELRAFLRE 453
|
490 500 510
....*....|....*....|....*....|
gi 306440447 500 QVIFYKRIKRVFFIEAIPKAPSGKILRKNL 529
Cdd:cd12117 454 RLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
47-529 |
1.33e-45 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 167.14 E-value: 1.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 47 GDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPfSTPAE-LAKHAKASRAKLL 125
Cdd:cd17651 18 GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDP-AYPAErLAFMLADAGPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 126 ITQAcyyekvkDFARESDVkvmcvDSAPDGCLHFSELTQADENEaPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLIT 205
Cdd:cd17651 97 LTHP-------ALAGELAV-----ELVAVTLLDQPGAAAGADAE-PDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLAN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 206 SVAQQ-----VDGDNPNLYFHSedvilcvlPMFHiYALNSIM--LCGlrvGAPILIMP---KFEIGSLLGLIEKYKVSIA 275
Cdd:cd17651 164 LVAWQarassLGPGARTLQFAG--------LGFD-VSVQEIFstLCA---GATLVLPPeevRTDPPALAAWLDEQRISRV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 276 PVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGkeLEDTVRAKF---PQARLGQGYGMTEAGPVLAMCLAFAKEPFDI 352
Cdd:cd17651 232 FLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLV--LTEDLREFCaglPGLRLHNHYGPTETHVVTALSLPGDPAAWPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 353 KPgACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATS---------------RTIDKEGWLhtgd 417
Cdd:cd17651 310 PP-PIGRPIDNTRVYVLD-AALRPVPPGVPGELYIGGAGLARGYLNRPELTAerfvpdpfvpgarmyRTGDLARWL---- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 418 igyidDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYI 497
Cdd:cd17651 384 -----PDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAAL 458
|
490 500 510
....*....|....*....|....*....|..
gi 306440447 498 SKQVIFYKRIKRVFFIEAIPKAPSGKILRKNL 529
Cdd:cd17651 459 ATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
50-466 |
2.35e-45 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 166.00 E-value: 2.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLItqa 129
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 130 cyyekvkdfaresdvkvmcvdsapdgclhfseltqadeneapqVDISPDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQ 209
Cdd:cd17640 83 -------------------------------------------VENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRS 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 210 QVDGDNPnlyfHSEDVILCVLPMFHIY---ALNSIMLCGLrvgapilIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIA 286
Cdd:cd17640 120 LSDIVPP----QPGDRFLSILPIWHSYersAEYFIFACGC-------SQAYTSIRTLKDDLKRVKPHYIVSVPRLWESLY 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 287 KSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRA---------KFPQA---RLGQGYGMTEAGPVLAmclafAKEPFDIKP 354
Cdd:cd17640 189 SGIQKQVSKSSPIKQFLFLFFLSGGIFKFGISGggalpphvdTFFEAigiEVLNGYGLTETSPVVS-----ARRLKCNVR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 355 GACGTVVRNAEMKIVDPETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIVDRLK 434
Cdd:cd17640 264 GSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAK 343
|
410 420 430
....*....|....*....|....*....|...
gi 306440447 435 ELIKYK-GFQVAPAELEALLIAHPEISDAAVVG 466
Cdd:cd17640 344 DTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
46-530 |
3.02e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 165.55 E-value: 3.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 46 NGDVYTYADVELTARRVASGLNKIGiqqgDVIMLFLPSsPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLL 125
Cdd:PRK07787 22 GGRVLSRSDLAGAATAVAERVAGAR----RVAVLATPT-LATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAW 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 126 ITQAcyyekvkdfaresdvkvmcvDSAPDGCLHFS-ELTQADENEAPQVDisPDDVVALPYSSGTTGLPKGVMLTHKgli 204
Cdd:PRK07787 97 LGPA--------------------PDDPAGLPHVPvRLHARSWHRYPEPD--PDAPALIVYTSGTTGPPKGVVLSRR--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 205 tSVAQQVDGDNPNLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEI----------GSLL-Gliekykvs 273
Cdd:PRK07787 152 -AIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPeayaqalsegGTLYfG-------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 274 iapvVPPVMMSIAKSPDLDKHdLSSLRMIKSGGAPLGKELEDTVRAKFPQaRLGQGYGMTEAgpvLAMCLAFAK-EPfdi 352
Cdd:PRK07787 223 ----VPTVWSRIAADPEAARA-LRGARLLVSGSAALPVPVFDRLAALTGH-RPVERYGMTET---LITLSTRADgER--- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 353 KPGACGTVVRNAEMKIVDpETGASLPRNQP--GEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIV 430
Cdd:PRK07787 291 RPGWVGLPLAGVETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 431 DRLK-ELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEksQATEDEIKQYISKQVIFYKRIKR 509
Cdd:PRK07787 370 GREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGAD--DVAADELIDFVAQQLSVHKRPRE 447
|
490 500
....*....|....*....|.
gi 306440447 510 VFFIEAIPKAPSGKILRKNLK 530
Cdd:PRK07787 448 VRFVDALPRNAMGKVLKKQLL 468
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
60-530 |
3.43e-45 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 167.28 E-value: 3.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 60 RRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANpFSTPAELAKHA-KASRAKLLIT-QAC--YYEKV 135
Cdd:PLN02860 43 LSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLN-YRWSFEEAKSAmLLVRPVMLVTdETCssWYEEL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 136 KDFARES-DVKVMCVDSAPDGCLHFSELTQADE-----NEAPQVDIS--PDDVVALPYSSGTTGLPKGVMLTHKGLIT-S 206
Cdd:PLN02860 122 QNDRLPSlMWQVFLESPSSSVFIFLNSFLTTEMlkqraLGTTELDYAwaPDDAVLICFTSGTTGRPKGVTISHSALIVqS 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 207 VAQ-QVDGdnpnlyFHSEDVILCVLPMFHIYALNSIMlCGLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPVM--- 282
Cdd:PLN02860 202 LAKiAIVG------YGEDDVYLHTAPLCHIGGLSSAL-AMLMVGACHVLLPKFDAKAALQAIKQHNVTSMITVPAMMadl 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 283 MSIAKSPDLDkHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEA----------GPVLAMCLAFAKEPFDI 352
Cdd:PLN02860 275 ISLTRKSMTW-KVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEAcssltfmtlhDPTLESPKQTLQTVNQT 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 353 KP-------GAC-GTVVRNAEMKIVDPETGASlprnqpGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDIGYIDDD 424
Cdd:PLN02860 354 KSssvhqpqGVCvGKPAPHVELKIGLDESSRV------GRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKA 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 425 DELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFV--------VKSEKS------QATE 490
Cdd:PLN02860 428 GNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVrlrdgwiwSDNEKEnakknlTLSS 507
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 306440447 491 DEIKQYISKQVIFYKRIKRVFFI--EAIPKAPSGKILRKNLK 530
Cdd:PLN02860 508 ETLRHHCREKNLSRFKIPKLFVQwrKPFPLTTTGKIRRDEVR 549
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
51-535 |
3.65e-45 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 166.85 E-value: 3.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQ-- 128
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDlt 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 129 --------ACYYEKVKDFARESDVKVMCVDSAPDGCLHFSELTQADENEAPQvDISPDDVVALPYSSGTTGLPKGVMLTH 200
Cdd:PRK06018 121 fvpilekiADKLPSVERYVVLTDAAHMPQTTLKNAVAYEEWIAEADGDFAWK-TFDENTAAGMCYTSGTTGDPKGVLYSH 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 201 KG--LITSVAQQVDGdnpnLYFHSEDVILCVLPMFHIYALnsimlcGLRVGAPI----LIMP--KFEIGSLLGLIEKYKV 272
Cdd:PRK06018 200 RSnvLHALMANNGDA----LGTSAADTMLPVVPLFHANSW------GIAFSAPSmgtkLVMPgaKLDGASVYELLDTEKV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 273 SIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARlgQGYGMTEAGPVLAMCLAfaKEPFDI 352
Cdd:PRK06018 270 TFTAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVR--HAWGMTEMSPLGTLAAL--KPPFSK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 353 KPGACGTVVR--------NAEMKIVDPEtGASLPR--NQPGEICIRGDQIMKGYLndpEATSRTIDKEGWLHTGDIGYID 422
Cdd:PRK06018 346 LPGDARLDVLqkqgyppfGVEMKITDDA-GKELPWdgKTFGRLKVRGPAVAAAYY---RVDGEILDDDGFFDTGDVATID 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 423 DDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVI 502
Cdd:PRK06018 422 AYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMDGKIA 501
|
490 500 510
....*....|....*....|....*....|...
gi 306440447 503 FYKRIKRVFFIEAIPKAPSGKILRKNLKEKLAG 535
Cdd:PRK06018 502 KWWMPDDVAFVDAIPHTATGKILKTALREQFKD 534
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
48-530 |
6.93e-45 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 167.49 E-value: 6.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 48 DVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIIT------AANPFSTPAElakHAKAsr 121
Cdd:cd05967 81 RTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSvvfggfAAKELASRID---DAKP-- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 122 aKLLITQAC---------YYEKVKDFARESDVK-----------VMCVDSAPDGCLHFSELTQADEnEAPQVDISPDDVV 181
Cdd:cd05967 156 -KLIVTASCgiepgkvvpYKPLLDKALELSGHKphhvlvlnrpqVPADLTKPGRDLDWSELLAKAE-PVDCVPVAATDPL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 182 ALPYSSGTTGLPKGVMLTHKG----LITSVAQQVDGDNPNLYFHSEDV-------ILCVLPMFHiyALNSIMLCGLRVGA 250
Cdd:cd05967 234 YILYTSGTTGKPKGVVRDNGGhavaLNWSMRNIYGIKPGDVWWAASDVgwvvghsYIVYGPLLH--GATTVLYEGKPVGT 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 251 PilimpkfEIGSLLGLIEKYKVSIAPVVPPVMMSIAKS-PDLD---KHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARL 326
Cdd:cd05967 312 P-------DPGAFWRVIEKYQVNALFTAPTAIRAIRKEdPDGKyikKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVI 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 327 GQgYGMTEAG-PVLAMCLAFakEPFDIKPGACGTVVRNAEMKIVDpETGASLPRNQPGEICIRG--------------DQ 391
Cdd:cd05967 385 DH-WWQTETGwPITANPVGL--EPLPIKAGSPGKPVPGYQVQVLD-EDGEPVGPNELGNIVIKLplppgclltlwkndER 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 392 IMKGYLNDPEATSRT-----IDKEGWLhtgdigyiddddelFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVG 466
Cdd:cd05967 461 FKKLYLSKFPGYYDTgdagyKDEDGYL--------------FIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVG 526
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 467 LKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVifYKRI------KRVFFIEAIPKAPSGKILRKNLK 530
Cdd:cd05967 527 VRDELKGQVPLGLVVLKEGVKITAEELEKELVALV--REQIgpvaafRLVIFVKRLPKTRSGKILRRTLR 594
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
50-530 |
8.74e-45 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 166.22 E-value: 8.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITaanP-FST--PAELAKHAKASRAKLLI 126
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVG---PlFEAfmEEAVRDRLEDSEAKVLI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 127 TQACYYEKVKdFARESDVK-VMCVD---SAPDGCLHFSELTQADENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKG 202
Cdd:PRK04319 151 TTPALLERKP-ADDLPSLKhVLLVGedvEEGPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 203 LIT--SVAQQVdgdnpnLYFHSEDVILC------VLPMfhIYALNSIMLCGLrvgAPILIMPKFEIGSLLGLIEKYKVSI 274
Cdd:PRK04319 230 MLQhyQTGKYV------LDLHEDDVYWCtadpgwVTGT--SYGIFAPWLNGA---TNVIDGGRFSPERWYRILEDYKVTV 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 275 ---APVVPPVMMSIAksPDL-DKHDLSSLRMIKSGGAPLGKELedtVRakFPQARLGQ----GYGMTEAGpvlamCLAFA 346
Cdd:PRK04319 299 wytAPTAIRMLMGAG--DDLvKKYDLSSLRHILSVGEPLNPEV---VR--WGMKVFGLpihdNWWMTETG-----GIMIA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 347 KEP-FDIKPGACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGD--QIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDD 423
Cdd:PRK04319 367 NYPaMDIKPGSMGKPLPGIEAAIVD-DQGNELPPNRMGNLAIKKGwpSMMRGIWNNPEKYESYF-AGDWYVSGDSAYMDE 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 424 DDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATED---EIKQYISKQ 500
Cdd:PRK04319 445 DGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSEElkeEIRGFVKKG 524
|
490 500 510
....*....|....*....|....*....|
gi 306440447 501 VIFYKRIKRVFFIEAIPKAPSGKILRKNLK 530
Cdd:PRK04319 525 LGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
185-526 |
2.24e-44 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 159.49 E-value: 2.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 185 YSSGTTGLPKGVMLTHKGLITSVAQQVDGdnpnLYFHSEDVILCVLPMFHIYALNSIMLcGLRVGAPILIMPKFEIGSLL 264
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDL----FNISGEDAILAPGPLSHSLFLYGAIS-ALYLGGTFIGQRKFNPKSWI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 265 GLIEKYKVSIAPVVPPVMMSIAKSpdlDKHDlSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEAGPVLAMCLA 344
Cdd:cd17633 82 RKINQYNATVIYLVPTMLQALART---LEPE-SKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 345 FAKepfdiKPGACGTVVRNAEMKIVDPETGASlprnqpGEICIRGDQIMKGYLndpeaTSRTIDKEGWLHTGDIGYIDDD 424
Cdd:cd17633 158 ESR-----PPNSVGRPFPNVEIEIRNADGGEI------GKIFVKSEMVFSGYV-----RGGFSNPDGWMSVGDIGYVDEE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 425 DELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVvksEKSQATEDEIKQYISKQVIFY 504
Cdd:cd17633 222 GYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALY---SGDKLTYKQLKRFLKQKLSRY 298
|
330 340
....*....|....*....|..
gi 306440447 505 KRIKRVFFIEAIPKAPSGKILR 526
Cdd:cd17633 299 EIPKKIIFVDSLPYTSSGKIAR 320
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
25-530 |
3.29e-44 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 165.36 E-value: 3.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 25 HSYVLENLSNHSSKPCLI-NGANGDV--YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAII 101
Cdd:cd05968 64 EQLLDKWLADTRTRPALRwEGEDGTSrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 102 TAAnpFS--TPAELAKHAKASRAKLLITQACYYEK-----VKDFARESDVKVMCVDS--------APDGCLHFSELTQAD 166
Cdd:cd05968 144 VPI--FSgfGKEAAATRLQDAEAKALITADGFTRRgrevnLKEEADKACAQCPTVEKvvvvrhlgNDFTPAKGRDLSYDE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 167 ENEAPQVDIS---PDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQ----QVDGDNPNLYFHSEDVILCVLPmFHIYAln 239
Cdd:cd05968 222 EKETAGDGAErteSEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQdmyfQFDLKPGDLLTWFTDLGWMMGP-WLIFG-- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 240 simlcGLRVGAPILI---MPKF-EIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPD--LDKHDLSSLRMIKSGGAPLGKE- 312
Cdd:cd05968 299 -----GLILGATMVLydgAPDHpKADRLWRMVEDHEITHLGLSPTLIRALKPRGDapVNAHDLSSLRVLGSTGEPWNPEp 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 313 ----LEDTVRAKFPQARLGQGygmTE-AGPVLamCLAFAKEpfdIKPGACGTVVRNAEMKIVDpETGASLpRNQPGEICI 387
Cdd:cd05968 374 wnwlFETVGKGRNPIINYSGG---TEiSGGIL--GNVLIKP---IKPSSFNGPVPGMKADVLD-ESGKPA-RPEVGELVL 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 388 RGDQI--MKGYLNDPEAT-----SRTIDKegWLHTGDIGYIDDDDeLFIVDRLKELIKYKGFQVAPAELEALLIAHPEIS 460
Cdd:cd05968 444 LAPWPgmTRGFWRDEDRYletywSRFDNV--WVHGDFAYYDEEGY-FYILGRSDDTINVAGKRVGPAEIESVLNAHPAVL 520
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 306440447 461 DAAVVGLKDEDAGEVPVAFVVKSE---KSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLK 530
Cdd:cd05968 521 ESAAIGVPHPVKGEAIVCFVVLKPgvtPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
37-535 |
8.67e-44 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 162.75 E-value: 8.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 37 SKPCLINGANGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKH 116
Cdd:PRK05852 31 EAPALVVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 117 AKASRAKLLITQAcyyEKVKDFARES------DVKVMCVDSAPDGCLhfseLTQADENEAPQVDIS------PDDVVALp 184
Cdd:PRK05852 111 SQAAGARVVLIDA---DGPHDRAEPTtrwwplTVNVGGDSGPSGGTL----SVHLDAATEPTPATStpeglrPDDAMIM- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 185 YSSGTTGLPKGVMLTHKGLITSVAQQVDGdnpnLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILiMP---KFEIG 261
Cdd:PRK05852 183 FTGGTTGLPKMVPWTHANIASSVRAIITG----YRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVL-LPargRFSAH 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 262 SLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDL--SSLRMIKSGGAPLGKELEDTVRAKFpQARLGQGYGMTEAGPVL 339
Cdd:PRK05852 258 TFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRkpAALRFIRSCSAPLTAETAQALQTEF-AAPVVCAFGMTEATHQV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 340 AmCLAFAKEPFDIKPGAC-GTVVRN--AEMKIVDPEtGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIdKEGWLHTG 416
Cdd:PRK05852 337 T-TTQIEGIGQTENPVVStGLVGRStgAQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 417 DIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQY 496
Cdd:PRK05852 414 DLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEELVQF 493
|
490 500 510
....*....|....*....|....*....|....*....
gi 306440447 497 ISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEKLAG 535
Cdd:PRK05852 494 CRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQFGH 532
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
51-529 |
1.25e-43 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 161.67 E-value: 1.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQAc 130
Cdd:cd17646 25 TYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLTTA- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 131 yyekvkdfaRESDVKVmcVDSAPDGCLHfsELTQADENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQ 210
Cdd:cd17646 104 ---------DLAARLP--AGGDVALLGD--EALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 211 VDGdnpnLYFHSEDVILCVLPM-FHIyALNSIMLcGLRVGAPILIMP---KFEIGSLLGLIEKYKVSIAPVVPPVMMSIA 286
Cdd:cd17646 171 QDE----YPLGPGDRVLQKTPLsFDV-SVWELFW-PLVAGARLVVARpggHRDPAYLAALIREHGVTTCHFVPSMLRVFL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 287 KSPDLDKHDlsSLRMIKSGGAPLGKELEDTVRAKFPqARLGQGYGMTEAGPVLAMCLAFAKEPFDIKPgaCGTVVRNAEM 366
Cdd:cd17646 245 AEPAAGSCA--SLRRVFCSGEALPPELAARFLALPG-AELHNLYGPTEAAIDVTHWPVRGPAETPSVP--IGRPVPNTRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 367 KIVDPEtGASLPRNQPGEICIRGDQIMKGYLNDPEATS---------------RTIDKEGWLHtgdigyiddDDELFIVD 431
Cdd:cd17646 320 YVLDDA-LRPVPVGVPGELYLGGVQLARGYLGRPALTAerfvpdpfgpgsrmyRTGDLARWRP---------DGALEFLG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 432 RLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKS-EKSQATEDEIKQYISKQVIFYKRIKRV 510
Cdd:cd17646 390 RSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAaGAAGPDTAALRAHLAERLPEYMVPAAF 469
|
490
....*....|....*....
gi 306440447 511 FFIEAIPKAPSGKILRKNL 529
Cdd:cd17646 470 VVLDALPLTANGKLDRAAL 488
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
19-535 |
1.29e-43 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 166.57 E-value: 1.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 19 PKNLPLHSYVLENLSNHSSKPCLINGanGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRG 98
Cdd:COG1020 473 PADATLHELFEAQAARTPDAVAVVFG--DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAG 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 99 AiitaA----NPfSTPAE-LAKHAKASRAKLLITQacyyEKVKDFARESDVKVMCVDSApdgclhfsELTQADEnEAPQV 173
Cdd:COG1020 551 A----AyvplDP-AYPAErLAYMLEDAGARLVLTQ----SALAARLPELGVPVLALDAL--------ALAAEPA-TNPPV 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 174 DISPDDVVALPYSSGTTGLPKGVMLTHKGLitsvAQQVDGDNPNLYFHSEDVILcvlpMFHiyALN---SI--MLCGLRV 248
Cdd:COG1020 613 PVTPDDLAYVIYTSGSTGRPKGVMVEHRAL----VNLLAWMQRRYGLGPGDRVL----QFA--SLSfdaSVweIFGALLS 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 249 GAPILIMPKFEIGS---LLGLIEKYKVSIAPVVPPVMMSIAkspDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQAR 325
Cdd:COG1020 683 GATLVLAPPEARRDpaaLAELLARHRVTVLNLTPSLLRALL---DAAPEALPSLRLVLVGGEALPPELVRRWRARLPGAR 759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 326 LGQGYGMTEAGpVLAMCLAFAKEPFDIKPGACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATS- 404
Cdd:COG1020 760 LVNLYGPTETT-VDSTYYEVTPPDADGGSVPIGRPIANTRVYVLD-AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAe 837
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 405 ---------------RTIDKEGWLHTGdigyiddddELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKD 469
Cdd:COG1020 838 rfvadpfgfpgarlyRTGDLARWLPDG---------NLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVARED 908
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 306440447 470 EDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEKLAG 535
Cdd:COG1020 909 APGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAA 974
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
50-526 |
2.11e-43 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 159.99 E-value: 2.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAI----ITAanpFSTPAeLAKHAKASRAKLL 125
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVyqplFTA---FGPKA-IEHRLRTSGARLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 126 ITQACYYEKVkdfarESDVKVMCvdsapdgclhfseltqadeneapqvdispddvvalpYSSGTTGLPKGVMLTHKGLIT 205
Cdd:cd05973 77 VTDAANRHKL-----DSDPFVMM------------------------------------FTSGTTGLPKGVPVPLRALAA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 206 SVAQQVDGdnpnLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAP-ILIMPKFEIGSLLGLIEKYKVSIAPVVPPVM-M 283
Cdd:cd05973 116 FGAYLRDA----VDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPtILLEGGFSVESTWRVIERLGVTNLAGSPTAYrL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 284 SIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAkfpqaRLG----QGYGMTEAGPVLAMCLAFAKEpfdIKPGACGT 359
Cdd:cd05973 192 LMAAGAEVPARPKGRLRRVSSAGEPLTPEVIRWFDA-----ALGvpihDHYGQTELGMVLANHHALEHP---VHAGSAGR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 360 VVRNAEMKIVDpETGASLPRNQPGEICI--RGDQIM--KGYLNDPEATsrtIDKeGWLHTGDIGYIDDDDELFIVDRLKE 435
Cdd:cd05973 264 AMPGWRVAVLD-DDGDELGPGEPGRLAIdiANSPLMwfRGYQLPDTPA---IDG-GYYLTGDTVEFDPDGSFSFIGRADD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 436 LIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKS---EKSQATEDEIKQYISKQVIFYKRIKRVFF 512
Cdd:cd05973 339 VITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRgghEGTPALADELQLHVKKRLSAHAYPRTIHF 418
|
490
....*....|....
gi 306440447 513 IEAIPKAPSGKILR 526
Cdd:cd05973 419 VDELPKTPSGKIQR 432
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
47-523 |
3.02e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 161.21 E-value: 3.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 47 GD-VYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLL 125
Cdd:PRK07798 25 GDrRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 126 ITQACYYEKVKD-FARESDVKVMCV---DSAPD---GCLHFSELTQADENEAPQVDISPDDVVALpYSSGTTGLPKGVML 198
Cdd:PRK07798 105 VYEREFAPRVAEvLPRLPKLRTLVVvedGSGNDllpGAVDYEDALAAGSPERDFGERSPDDLYLL-YTGGTTGMPKGVMW 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 199 THKGLITSVAQQVD---GDNP-NLYFHSEDV-------ILCVLPMFHIYALNSIM---LCGLRVgaPILIMPKFEIGSLL 264
Cdd:PRK07798 184 RQEDIFRVLLGGRDfatGEPIeDEEELAKRAaagpgmrRFPAPPLMHGAGQWAAFaalFSGQTV--VLLPDVRFDADEVW 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 265 GLIEKYKVSIAPVVPPVMmsiAKsPDLD------KHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEAGpv 338
Cdd:PRK07798 262 RTIEREKVNVITIVGDAM---AR-PLLDaleargPYDLSSLFAIASGGALFSPSVKEALLELLPNVVLTDSIGSSETG-- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 339 lAMCLAFAKEpfDIKPGACGTVVRNAEMKIVDPETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRT---IDKEGWLHT 415
Cdd:PRK07798 336 -FGGSGTVAK--GAVHTGGPRFTIGPRTVVLDEDGNPVEPGSGEIGWIARRGHIPLGYYKDPEKTAETfptIDGVRYAIP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 416 GDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQ 495
Cdd:PRK07798 413 GDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRA 492
|
490 500
....*....|....*....|....*...
gi 306440447 496 YISKQVIFYKRIKRVFFIEAIPKAPSGK 523
Cdd:PRK07798 493 HCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
179-526 |
7.14e-43 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 155.88 E-value: 7.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 179 DVVALPYSSGTTGLPKGVMLTHKGLITSVAQ-QVDGDNpnlyFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPK 257
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDIlQKEGLN----WVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 258 FEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAplgKELEDTVR--AKFPQARLGQGYGMTEA 335
Cdd:cd17635 78 TTYKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGS---RAIAADVRfiEATGLTNTAQVYGLSET 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 336 GPVLamCLAFAKEPFDIkpGACGTVVRNAEMKIVDPEtGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIdKEGWLHT 415
Cdd:cd17635 155 GTAL--CLPTDDDSIEI--NAVGRPYPGVDVYLAATD-GIAGPSASFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 416 GDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSE-KSQATEDEIK 494
Cdd:cd17635 229 GDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAeLDENAIRALK 308
|
330 340 350
....*....|....*....|....*....|..
gi 306440447 495 QYISKQVIFYKRIKRVFFIEAIPKAPSGKILR 526
Cdd:cd17635 309 HTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
51-485 |
9.64e-43 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 159.30 E-value: 9.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGaiITAANPFSTPAELA-KHAkasrakllitqa 129
Cdd:cd17639 7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN--IPIVTVYATLGEDAlIHS------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 130 cyyekvkdfARESDVKVMCVDSapdgclhfseltqadeneapqvdiSPDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQ 209
Cdd:cd17639 73 ---------LNETECSAIFTDG------------------------KPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAG 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 210 QvdGDNPNLYFHSEDVILCVLPMFHIYALNSIMLC---GLRVG--APILIMPKFEIGSLlGLIEKYKVSIAPVVPPVMMS 284
Cdd:cd17639 120 L--GDRVPELLGPDDRYLAYLPLAHIFELAAENVClyrGGTIGygSPRTLTDKSKRGCK-GDLTEFKPTLMVGVPAIWDT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 285 IAK---------------------------------SPDLDKHDLSS--------LRMIKSGGAPLGKELEDTVRAKFpq 323
Cdd:cd17639 197 IRKgvlaklnpmgglkrtlfwtayqsklkalkegpgTPLLDELVFKKvraalggrLRYMLSGGAPLSADTQEFLNIVL-- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 324 ARLGQGYGMTEAgpvlaMCLAFAKEPFDIKPGACGTVVRNAEMKIVD-PETGASLPRNQP-GEICIRGDQIMKGYLNDPE 401
Cdd:cd17639 275 CPVIQGYGLTET-----CAGGTVQDPGDLETGRVGPPLPCCEIKLVDwEEGGYSTDKPPPrGEILIRGPNVFKGYYKNPE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 402 ATSRTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYK-GFQVAPAELEALLIAHPEISDAAVVGLKDEDAgevPVAFV 480
Cdd:cd17639 350 KTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPDKSY---PVAIV 426
|
....*
gi 306440447 481 VKSEK 485
Cdd:cd17639 427 VPNEK 431
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
51-532 |
1.44e-42 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 159.54 E-value: 1.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANP-FSTPAeLAKHAKASRAKLLITQA 129
Cdd:PRK13382 70 TWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTsFAGPA-LAEVVTREGVDTVIYDE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 130 CYYEKV-KDFA-RESDVKVMCVDSAPDGCLHfSELTQADENEAPQVDISPDDVVALpySSGTTGLPKGVMLTHKGLItSV 207
Cdd:PRK13382 149 EFSATVdRALAdCPQATRIVAWTDEDHDLTV-EVLIAAHAGQRPEPTGRKGRVILL--TSGTTGTPKGARRSGPGGI-GT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 208 AQQVDGDNPnlyFHSEDVILCVLPMFHIYALNSIMLCGLrVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAK 287
Cdd:PRK13382 225 LKAILDRTP---WRAEEPTVIVAPMFHAWGFSQLVLAAS-LACTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 288 SPD--LDKHDLSSLRMIKSGGAPLGKeleDTVRA---KFPQArLGQGYGMTEAGpvlamcLAFAKEPFDIK--PGACGTV 360
Cdd:PRK13382 301 LPAevRNRYSGRSLRFAAASGSRMRP---DVVIAfmdQFGDV-IYNNYNATEAG------MIATATPADLRaaPDTAGRP 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 361 VRNAEMKIVDPEtGASLPRNQPGEICIRGDQIMKGYlnDPEATSRTIDkeGWLHTGDIGYIDDDDELFIVDRLKELIKYK 440
Cdd:PRK13382 371 AEGTEIRILDQD-FREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFHD--GFMASGDVGYLDENGRLFVVGRDDEMIVSG 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 441 GFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAP 520
Cdd:PRK13382 446 GENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGA 525
|
490
....*....|..
gi 306440447 521 SGKILRKNLKEK 532
Cdd:PRK13382 526 TGKILRRELQAR 537
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
178-522 |
3.90e-41 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 150.92 E-value: 3.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 178 DDVVALpYSSGTTGLPKGVMLTHKGLIT-----SVAQQVDgdnpnlyfhSEDVILCVLPMFHIYALNSiMLCGLRVGAPI 252
Cdd:cd17636 1 DPVLAI-YTAAFSGRPNGALLSHQALLAqalvlAVLQAID---------EGTVFLNSGPLFHIGTLMF-TLATFHAGGTN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 253 LIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRmiKSGGAPLGKEL--EDTVrakfPQARLGQGY 330
Cdd:cd17636 70 VFVRRVDAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLR--SSPAAPEWNDMatVDTS----PWGRKPGGY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 331 GMTEAGPVLAMcLAFAKEPFdikpGACGTVVRNAEMKIVDPEtGASLPRNQPGEICIRGDQIMKGYLNDPEATS-RTIDk 409
Cdd:cd17636 144 GQTEVMGLATF-AALGGGAI----GGAGRPSPLVQVRILDED-GREVPDGEVGEIVARGPTVMAGYWNRPEVNArRTRG- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 410 eGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQAT 489
Cdd:cd17636 217 -GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVT 295
|
330 340 350
....*....|....*....|....*....|...
gi 306440447 490 EDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSG 522
Cdd:cd17636 296 EAELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
31-536 |
9.08e-41 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 155.41 E-value: 9.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 31 NLSNHSSKPCLI----NGANGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFL-----GASHrgAII 101
Cdd:cd05966 62 HLKERGDKVAIIwegdEPDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLacariGAVH--SVV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 102 TAAnpFStPAELAKHAKASRAKLLITQACYY--------EKVKDFARESDVKVMCV-------DSAP-----DGCLHfsE 161
Cdd:cd05966 140 FAG--FS-AESLADRINDAQCKLVITADGGYrggkviplKEIVDEALEKCPSVEKVlvvkrtgGEVPmtegrDLWWH--D 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 162 LTQADENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQVDgdnpnlY---FHSEDVILCVLPMF----H 234
Cdd:cd05966 215 LMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFK------YvfdYHPDDIYWCTADIGwitgH 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 235 IYALNSIMLCG----LRVGAPIliMPKFeiGSLLGLIEKYKVSIAPVVPPVMMSIAKSPD--LDKHDLSSLRMIKSGGAP 308
Cdd:cd05966 289 SYIVYGPLANGattvMFEGTPT--YPDP--GRYWDIVEKHKVTIFYTAPTAIRALMKFGDewVKKHDLSSLRVLGSVGEP 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 309 ------------LGKE---LEDTvrakfpqarlgqgYGMTEAGPVLAMCLAFAkepFDIKPGACGTVVRNAEMKIVDPEt 373
Cdd:cd05966 365 inpeawmwyyevIGKErcpIVDT-------------WWQTETGGIMITPLPGA---TPLKPGSATRPFFGIEPAILDEE- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 374 GASLPRNQPGEICIR----GdqIMKGYLNDPEATSRT----------------IDKEGWLhtgdigyiddddelFIVDRL 433
Cdd:cd05966 428 GNEVEGEVEGYLVIKrpwpG--MARTIYGDHERYEDTyfskfpgyyftgdgarRDEDGYY--------------WITGRV 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 434 KELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVV---KSEKSQATEDEIKQYISKQVIFYKRIKRV 510
Cdd:cd05966 492 DDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTlkdGEEPSDELRKELRKHVRKEIGPIATPDKI 571
|
570 580
....*....|....*....|....*.
gi 306440447 511 FFIEAIPKAPSGKILRKNLKEKLAGI 536
Cdd:cd05966 572 QFVPGLPKTRSGKIMRRILRKIAAGE 597
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
50-525 |
2.96e-40 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 153.89 E-value: 2.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQA 129
Cdd:cd17634 85 ISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITAD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 130 CYYE--------KVKDFARESDV----KVMCVD---SAPDGC----LHFSELTQADENEAPQVDISPDDVVALPYSSGTT 190
Cdd:cd17634 165 GGVRagrsvplkKNVDDALNPNVtsveHVIVLKrtgSDIDWQegrdLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 191 GLPKGVMLTHKGLITSVAQqvdgDNPNLY-FHSEDVILCVLP----MFHIYALNSIMLCGLRV----GAPILIMPkfeiG 261
Cdd:cd17634 245 GKPKGVLHTTGGYLVYAAT----TMKYVFdYGPGDIYWCTADvgwvTGHSYLLYGPLACGATTllyeGVPNWPTP----A 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 262 SLLGLIEKYKVSIAPVVPPVMMSIAKSPD--LDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQAR--LGQGYGMTEAGP 337
Cdd:cd17634 317 RMWQVVDKHGVNILYTAPTAIRALMAAGDdaIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGKEKcpVVDTWWQTETGG 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 338 VLAMCLAFAKEpfdIKPGACGTVVRNAEMKIVDPEtGASLPRNQPGEICIrGDQI---MKGYLNDPEATSRT-------- 406
Cdd:cd17634 397 FMITPLPGAIE---LKAGSATRPVFGVQPAVVDNE-GHPQPGGTEGNLVI-TDPWpgqTRTLFGDHERFEQTyfstfkgm 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 407 --------IDKEGWLhtgdigyiddddelFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVA 478
Cdd:cd17634 472 yfsgdgarRDEDGYY--------------WITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYA 537
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 306440447 479 FVVKS---EKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKIL 525
Cdd:cd17634 538 YVVLNhgvEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
38-530 |
1.47e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 147.85 E-value: 1.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 38 KPCLINGANGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHA 117
Cdd:PRK13390 13 RPAVIVAETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 118 KASRAKLLITQACYYEKVKDFARESDVKVmCVDSAPDGclhFSELTQADENEAPQVDISPDDVVALpYSSGTTGLPKGVM 197
Cdd:PRK13390 93 GDSGARVLVASAALDGLAAKVGADLPLRL-SFGGEIDG---FGSFEAALAGAGPRLTEQPCGAVML-YSSGTTGFPKGIQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 198 --LTHKGL------ITSVAQQVDGdnpnlyFHSEDVILCVLPMFHIYALNsimLCGL--RVGAPILIMPKFEIGSLLGLI 267
Cdd:PRK13390 168 pdLPGRDVdapgdpIVAIARAFYD------ISESDIYYSSAPIYHAAPLR---WCSMvhALGGTVVLAKRFDAQATLGHV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 268 EKYKVSIAPVVPPVMMSIAKSPD--LDKHDLSSLRMIKSGGAPLGKELEDTVrAKFPQARLGQGYGMTEagpvlAMCLAF 345
Cdd:PRK13390 239 ERYRITVTQMVPTMFVRLLKLDAdvRTRYDVSSLRAVIHAAAPCPVDVKHAM-IDWLGPIVYEYYSSTE-----AHGMTF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 346 AKEP-FDIKPGACGTVVRnAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATSR----------------TID 408
Cdd:PRK13390 313 IDSPdWLAHPGSVGRSVL-GDLHICD-DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAaqhpahpfwttvgdlgSVD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 409 KEGWlhtgdigyiddddeLFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQA 488
Cdd:PRK13390 391 EDGY--------------LYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRG 456
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 306440447 489 TED---EIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLK 530
Cdd:PRK13390 457 SDElarELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
38-529 |
1.47e-37 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 144.34 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 38 KPCLINGAngDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAK-H 116
Cdd:cd12114 3 ATAVICGD--GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAiL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 117 AKASrAKLLITqacyyEKVKDFARESDVKVMCVDSAPdgclhfseltQADENEAPQVDISPDDVVALPYSSGTTGLPKGV 196
Cdd:cd12114 81 ADAG-ARLVLT-----DGPDAQLDVAVFDVLILDLDA----------LAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 197 MLTHKGLITSVAQ-----QVDGDnpnlyfhseDVILCV------LPMFHIYALnsimlcgLRVGAPILIMPKFEIG---S 262
Cdd:cd12114 145 MISHRAALNTILDinrrfAVGPD---------DRVLALsslsfdLSVYDIFGA-------LSAGATLVLPDEARRRdpaH 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 263 LLGLIEKYKVSIAPVVPPVM-MSIAKSPDLDKHdLSSLRMIKSGGAPLGKELEDTVRAKFPQAR---LGqgyGMTEAGpV 338
Cdd:cd12114 209 WAELIERHGVTLWNSVPALLeMLLDVLEAAQAL-LPSLRLVLLSGDWIPLDLPARLRALAPDARlisLG---GATEAS-I 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 339 LAMCLAFAKEPFDIKPGACGTVVRNAEMKIVDPEtGASLPRNQPGEICIRGDQIMKGYLNDPEATSRT----IDKEGWLH 414
Cdd:cd12114 284 WSIYHPIDEVPPDWRSIPYGRPLANQRYRVLDPR-GRDCPDWVPGELWIGGRGVALGYLGDPELTAARfvthPDGERLYR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 415 TGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLkDEDAGEVPVAFVV-KSEKSQATEDEI 493
Cdd:cd12114 363 TGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVpDNDGTPIAPDAL 441
|
490 500 510
....*....|....*....|....*....|....*.
gi 306440447 494 KQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNL 529
Cdd:cd12114 442 RAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
61-536 |
2.07e-37 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 145.55 E-value: 2.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 61 RVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIItaaNPFSTP------AELAKHAKAsraKLLITqacyYEK 134
Cdd:PLN03102 51 RLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVL---NPINTRldatsiAAILRHAKP---KILFV----DRS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 135 VKDFARESDVKVMCVDSAPDGCLHFseltqADENEAPQVDISPD---------------------------DVVALPYSS 187
Cdd:PLN03102 121 FEPLAREVLHLLSSEDSNLNLPVIF-----IHEIDFPKRPSSEEldyecliqrgeptpslvarmfriqdehDPISLNYTS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 188 GTTGLPKGVMLTHKGLITSVAQQVDGDNPNLYfhseDVILCVLPMFH---------IYALNSIMLCGLRVGAPilimpkf 258
Cdd:PLN03102 196 GTTADPKGVVISHRGAYLSTLSAIIGWEMGTC----PVYLWTLPMFHcngwtftwgTAARGGTSVCMRHVTAP------- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 259 eigSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRakfpqaRLG----QGYGMTE 334
Cdd:PLN03102 265 ---EIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQ------RLGfqvmHAYGLTE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 335 A-GPVLaMCL---AFAKEP----FDIKPGACGTVVRNAEMKIVDPETGASLPRNQP--GEICIRGDQIMKGYLNDPEATS 404
Cdd:PLN03102 336 AtGPVL-FCEwqdEWNRLPenqqMELKARQGVSILGLADVDVKNKETQESVPRDGKtmGEIVIKGSSIMKGYLKNPKATS 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 405 RTIdKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSE 484
Cdd:PLN03102 415 EAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEK 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 306440447 485 KSQATEDEIKQYISKQ--VIFYKR--------IKRVFFIEAIPKAPSGKILRKNLKEKLAGI 536
Cdd:PLN03102 494 GETTKEDRVDKLVTRErdLIEYCRenlphfmcPRKVVFLQELPKNGNGKILKPKLRDIAKGL 555
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
47-535 |
5.66e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 143.69 E-value: 5.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 47 GDV--YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELA---KHAK--- 118
Cdd:PRK07008 35 GDIhrYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAyivNHAEdry 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 119 ----ASRAKLLITQACYYEKVKDFARESDVKVMCVDSAPDGClhFSEL--TQADENEAPQVDisPDDVVALPYSSGTTGL 192
Cdd:PRK07008 115 vlfdLTFLPLVDALAPQCPNVKGWVAMTDAAHLPAGSTPLLC--YETLvgAQDGDYDWPRFD--ENQASSLCYTSGTTGN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 193 PKGVMLTHKgliTSVAQQVDGDNPN-LYFHSEDVILCVLPMFHIYALN---SIMLCGLRVgapILIMPKFEIGSLLGLIE 268
Cdd:PRK07008 191 PKGALYSHR---STVLHAYGAALPDaMGLSARDAVLPVVPMFHVNAWGlpySAPLTGAKL---VLPGPDLDGKSLYELIE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 269 KYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFpQARLGQGYGMTEAGPVLAMCLAFAKE 348
Cdd:PRK07008 265 AERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEY-GVEVIHAWGMTEMSPLGTLCKLKWKH 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 349 ---PFDIKPGAC---GTVVRNAEMKIVDPEtGASLPRNQP--GEICIRGDQIMKGYL-NDpeaTSRTIDkeGWLHTGDIG 419
Cdd:PRK07008 344 sqlPLDEQRKLLekqGRVIYGVDMKIVGDD-GRELPWDGKafGDLQVRGPWVIDRYFrGD---ASPLVD--GWFPTGDVA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 420 YIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISK 499
Cdd:PRK07008 418 TIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEG 497
|
490 500 510
....*....|....*....|....*....|....*.
gi 306440447 500 QVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEKLAG 535
Cdd:PRK07008 498 KVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFRD 533
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
81-531 |
7.69e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 143.28 E-value: 7.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 81 LPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQACYYEKVKDfaRESDVKVMCVDSAPdgclHFS 160
Cdd:PRK07867 61 LDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDG--LDPGVRVINVDSPA----WAD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 161 ELTQADENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLIT---SVAQQVdGDNPnlyfhsEDVILCVLPMFHIya 237
Cdd:PRK07867 135 ELAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASagvMLAQRF-GLGP------DDVCYVSMPLFHS-- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 238 lNSIMLC---GLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVV-PPVMMSIAKSPDLDKHDlSSLRMIksggapLGKEL 313
Cdd:PRK07867 206 -NAVMAGwavALAAGASIALRRKFSASGFLPDVRRYGATYANYVgKPLSYVLATPERPDDAD-NPLRIV------YGNEG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 314 EDTVRAKFpQARLG----QGYGMTEAGpvlamcLAFAKEPfDIKPGACGTVVrnAEMKIVDPETGASLPRNQP------- 382
Cdd:PRK07867 278 APGDIARF-ARRFGcvvvDGFGSTEGG------VAITRTP-DTPPGALGPLP--PGVAIVDPDTGTECPPAEDadgrlln 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 383 -----GEIC-IRGDQIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAH 456
Cdd:PRK07867 348 adeaiGELVnTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRY 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 457 PEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYIS-------KQVIFYKRIkrvffIEAIPKAPSGKILRKNL 529
Cdd:PRK07867 427 PDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAaqpdlgpKQWPSYVRV-----CAELPRTATFKVLKRQL 501
|
..
gi 306440447 530 KE 531
Cdd:PRK07867 502 SA 503
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
176-523 |
1.09e-36 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 139.44 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 176 SPDDVVALpYSSGTTGLPKGVMLTHKGLITSVAQQVDGDNPNlYFHSED-----------VILCVLPMFHIYALNSIMLC 244
Cdd:cd05924 2 SADDLYIL-YTGGTTGMPKGVMWRQEDIFRMLMGGADFGTGE-FTPSEDahkaaaaaagtVMFPAPPLMHGTGSWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 245 GLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMmsiAKsPDLDK------HDLSSLRMIKSGGAPLGKELEDTVR 318
Cdd:cd05924 80 LLGGQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDAM---AR-PLIDAlrdagpYDLSSLFAISSGGALLSPEVKQGLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 319 AKFPQARLGQGYGMTEAGpvlAMCLAFAKEpfdiKPGACGTVVRNAEMKIV-DPETGASLP-RNQPGEICIRGdQIMKGY 396
Cdd:cd05924 156 ELVPNITLVDAFGSSETG---FTGSGHSAG----SGPETGPFTRANPDTVVlDDDGRVVPPgSGGVGWIARRG-HIPLGY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 397 LNDPEATSRT---IDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAG 473
Cdd:cd05924 228 YGDEAKTAETfpeVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWG 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 306440447 474 EVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGK 523
Cdd:cd05924 308 QEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
46-530 |
9.10e-36 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 139.04 E-value: 9.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 46 NGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLL 125
Cdd:cd17649 9 GDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 126 ITQAcyyekvkdfaresdvkvmcvdsapdgclhfseltqadeneapqvdisPDDVVALPYSSGTTGLPKGVMLTHKGLIT 205
Cdd:cd17649 89 LTHH-----------------------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 206 SVaqQVDGDNPNLyfHSEDVILCVLPM-FHIYAlnSIMLCGLRVGAPILIMPKFEIGS---LLGLIEKYKVSIAPVVPPV 281
Cdd:cd17649 122 HC--QATAERYGL--TPGDRELQFASFnFDGAH--EQLLPPLICGACVVLRPDELWASadeLAEMVRELGVTVLDLPPAY 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 282 MMSIAKspDLDKHDLS---SLRMIKSGGAPLGKELedtVRAKFPQA-RLGQGYGMTEAgpvLAMCLAFAKEPFDIKPGA- 356
Cdd:cd17649 196 LQQLAE--EADRTGDGrppSLRLYIFGGEALSPEL---LRRWLKAPvRLFNAYGPTEA---TVTPLVWKCEAGAARAGAs 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 357 --CGTVVRNAEMKIVDPEtGASLPRNQPGEICIRGDQIMKGYLNDPEAT-SRTID----KEG--WLHTGDIGYIDDDDEL 427
Cdd:cd17649 268 mpIGRPLGGRSAYILDAD-LNPVPVGVTGELYIGGEGLARGYLGRPELTaERFVPdpfgAPGsrLYRTGDLARWRDDGVI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 428 FIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLkDEDAGEVPVAFVV--KSEKSQATEDEIKQYISKQVIFYK 505
Cdd:cd17649 347 EYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVlrAAAAQPELRAQLRTALRASLPDYM 425
|
490 500
....*....|....*....|....*
gi 306440447 506 RIKRVFFIEAIPKAPSGKILRKNLK 530
Cdd:cd17649 426 VPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
46-529 |
1.25e-35 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 138.96 E-value: 1.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 46 NGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPfSTPAE-LAKHAKASRAKL 124
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDP-DYPADrLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 125 LITQAcyyekvkdfAREsdvkvmcvDSAPDGCLHFSELTQADEN--EAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKG 202
Cdd:cd12116 88 VLTDD---------ALP--------DRLPAGLPVLLLALAAAAAapAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 203 LI---TSVAQQvdgdnpnLYFHSEDVILCVL-PMFHIYALNsiMLCGLRVGAPILIMPK---FEIGSLLGLIEKYKVSIA 275
Cdd:cd12116 151 LVnflHSMRER-------LGLGPGDRLLAVTtYAFDISLLE--LLLPLLAGARVVIAPRetqRDPEALARLIEAHSITVM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 276 PVVPPVMMSIAKSpdlDKHDLSSLRMIKSGGA---PLGKELEDTVRakfpqaRLGQGYGMTEAGP-VLAMCLAFAKEPFD 351
Cdd:cd12116 222 QATPATWRMLLDA---GWQGRAGLTALCGGEAlppDLAARLLSRVG------SLWNLYGPTETTIwSTAARVTAAAGPIP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 352 IkpgacGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATS----------------RTIDKEGWLht 415
Cdd:cd12116 293 I-----GRPLANTQVYVLD-AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAerfvpdpfagpgsrlyRTGDLVRRR-- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 416 gdigyidDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVgLKDEDAGEVPVAFVVKSEKSQATEDEIKQ 495
Cdd:cd12116 365 -------ADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVV-VREDGGDRRLVAYVVLKAGAAPDAAALRA 436
|
490 500 510
....*....|....*....|....*....|....
gi 306440447 496 YISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNL 529
Cdd:cd12116 437 HLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
47-532 |
1.78e-35 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 139.10 E-value: 1.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 47 GDV-YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLL 125
Cdd:cd05915 21 EVHrTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 126 ITQACYYEkvkdFARESDVKVMCVDSAPDGCLHFSE----LTQADENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHK 201
Cdd:cd05915 101 LFDPNLLP----LVEAIRGELKTVQHFVVMDEKAPEgylaYEEALGEEADPVRVPERAACGMAYTTGTTGLPKGVVYSHR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 202 GLITSVAQQvdGDNPNLYFHSEDVILCVLPMFH---------IYALNSIMLCGLRVGAPILIMPKfeigsllglIEKYKV 272
Cdd:cd05915 177 ALVLHSLAA--SLVDGTALSEKDVVLPVVPMFHvnawclpyaATLVGAKQVLPGPRLDPASLVEL---------FDGEGV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 273 SIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTvrAKFPQARLGQGYGMTEAGPVLAMCLAFAK----- 347
Cdd:cd05915 246 TFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSAAPRSLIAR--FERMGVEVRQGYGLTETSPVVVQNFVKSHlesls 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 348 EPFDIKPGACGTVVRNAE-MKIVDPETgASLPRNQPG--EICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDIGYIDDD 424
Cdd:cd05915 324 EEEKLTLKAKTGLPIPLVrLRVADEEG-RPVPKDGKAlgEVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 425 DELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFvVKSEKSQATEDEIKQYISKQVIFY 504
Cdd:cd05915 403 GYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAV-VVPRGEKPTPEELNEHLLKAGFAK 481
|
490 500
....*....|....*....|....*....
gi 306440447 505 KRI-KRVFFIEAIPKAPSGKIlRKNLKEK 532
Cdd:cd05915 482 WQLpDAYVFAEEIPRTSAGKF-LKRALRE 509
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-531 |
2.06e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 142.22 E-value: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 3 PQEEFIFRSKLPDiYIPKNLPLHSYVLENLSNHSSKPCLINGanGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLP 82
Cdd:PRK12467 494 ERARELVRWNAPA-TEYAPDCVHQLIEAQARQHPERPALVFG--EQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 83 SSPEFVLAFLGASHRGAIITAANPfSTPAE-LAKHAKASRAKLLITQAcyyEKVKDFARESDVKVMCVDSAPDGCLHFSE 161
Cdd:PRK12467 571 RSIEMVVGLLAVLKAGGAYVPLDP-EYPQDrLAYMLDDSGVRLLLTQS---HLLAQLPVPAGLRSLCLDEPADLLCGYSG 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 162 LTqadeneaPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLitsvAQQVDGDNPNLYFHSEDVILcvlpMFHIYA--LN 239
Cdd:PRK12467 647 HN-------PEVALDPDNLAYVIYTSGSTGQPKGVAISHGAL----ANYVCVIAERLQLAADDSML----MVSTFAfdLG 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 240 SIMLCG-LRVGAPILIMPK---FEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKhdLSSLRMIKSGGAPLGKELED 315
Cdd:PRK12467 712 VTELFGaLASGATLHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVAL--PRPQRALVCGGEALQVDLLA 789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 316 TVRAKFPQARLGQGYGMTEAgPVLAMCLAFAKEPFDIKPGACGTVVRNAEMKIVDPETgASLPRNQPGEICIRGDQIMKG 395
Cdd:PRK12467 790 RVRALGPGARLINHYGPTET-TVGVSTYELSDEERDFGNVPIGQPLANLGLYILDHYL-NPVPVGVVGELYIGGAGLARG 867
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 396 YLNDPEATSRTI-------DKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLk 468
Cdd:PRK12467 868 YHRRPALTAERFvpdpfgaDGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQ- 946
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 306440447 469 DEDAGEVPVAFVV-----KSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKE 531
Cdd:PRK12467 947 PGDAGLQLVAYLVpaavaDGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
50-535 |
2.32e-35 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 138.97 E-value: 2.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAF-----LGA-------SHRGAIITAANPFSTPAELAkha 117
Cdd:PRK10946 49 FSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFfallkLGVapvnalfSHQRSELNAYASQIEPALLI--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 118 kASRAKLLITQACYYEKVKDFARESDVKVMCVDSAPdgclhfSELTQADENEAPQVDISP---DDVVALPYSSGTTGLPK 194
Cdd:PRK10946 126 -ADRQHALFSDDDFLNTLVAEHSSLRVVLLLNDDGE------HSLDDAINHPAEDFTATPspaDEVAFFQLSGGSTGTPK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 195 GVMLTHKGLITSVAQQVD--GDNPNLYFhsedviLCVLPMFHIYALNSIMLCG-LRVGAPILIMPKFEIGSLLGLIEKYK 271
Cdd:PRK10946 199 LIPRTHNDYYYSVRRSVEicGFTPQTRY------LCALPAAHNYPMSSPGALGvFLAGGTVVLAPDPSATLCFPLIEKHQ 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 272 VSIAPVVPP-VMMSIAKSPDLD-KHDLSSLRMIKSGGAPLGkeleDTVRAKFPQ---ARLGQGYGMTEaGPVLAMCL--- 343
Cdd:PRK10946 273 VNVTALVPPaVSLWLQAIAEGGsRAQLASLKLLQVGGARLS----ETLARRIPAelgCQLQQVFGMAE-GLVNYTRLdds 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 344 ---AFAKEPFDIKPgacgtvvrNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDIGY 420
Cdd:PRK10946 348 derIFTTQGRPMSP--------DDEVWVAD-ADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVS 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 421 IDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATedEIKQYISKQ 500
Cdd:PRK10946 419 IDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAV--QLRRFLREQ 496
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 306440447 501 -VIFYKRIKRVFFIEAIPKAPSGKI----LRKNLKEKLAG 535
Cdd:PRK10946 497 gIAEFKLPDRVECVDSLPLTAVGKVdkkqLRQWLASRASA 536
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
49-529 |
1.02e-34 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 138.16 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 49 VYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAAnpFSTpaeLAKHAKASR-----AK 123
Cdd:PRK10524 84 TYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVV--FGG---FASHSLAARiddakPV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 124 LLIT--------QACYYEKVKDFA-RESDVK---VMCVDSapdGCLHFSELTQADENEAPQVDISPDDVVA--------- 182
Cdd:PRK10524 159 LIVSadagsrggKVVPYKPLLDEAiALAQHKprhVLLVDR---GLAPMARVAGRDVDYATLRAQHLGARVPvewlesnep 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 183 --LPYSSGTTGLPKGVMLTHKG----LITSVAQQVDGDNPNLYFHSEDVILCVLPMFHIYA-----LNSIMLCGLrvgaP 251
Cdd:PRK10524 236 syILYTSGTTGKPKGVQRDTGGyavaLATSMDTIFGGKAGETFFCASDIGWVVGHSYIVYApllagMATIMYEGL----P 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 252 ILIMPkfeiGSLLGLIEKYKVSIAPVVPPVMMSIAKSPD--LDKHDLSSLRMIKSGGAPLgkeleDTVRAKFPQARLGQ- 328
Cdd:PRK10524 312 TRPDA----GIWWRIVEKYKVNRMFSAPTAIRVLKKQDPalLRKHDLSSLRALFLAGEPL-----DEPTASWISEALGVp 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 329 ---GYGMTEAG-PVLAMCLAFAKEPfdIKPGACGTVVRNAEMKIVDPETGASLPRNQPGEICIRG--------------D 390
Cdd:PRK10524 383 vidNYWQTETGwPILAIARGVEDRP--TRLGSPGVPMYGYNVKLLNEVTGEPCGPNEKGVLVIEGplppgcmqtvwgddD 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 391 QIMKGY--LNDPEATSR----TIDKEGWLhtgdigyiddddelFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAV 464
Cdd:PRK10524 461 RFVKTYwsLFGRQVYSTfdwgIRDADGYY--------------FILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAV 526
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 306440447 465 VGLKDEDAGEVPVAFVV--------KSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNL 529
Cdd:PRK10524 527 VGVKDALKGQVAVAFVVpkdsdslaDREARLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLRRAI 599
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
35-532 |
2.15e-34 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 136.90 E-value: 2.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 35 HSSKPCLINGANGdvYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAAN---PFSTPA 111
Cdd:PLN02479 33 HPTRKSVVHGSVR--YTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNirlNAPTIA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 112 ELAKHakaSRAKLLITQACYYEKVKDFAR------ESDVK-----VMCVDSAPDGCLHFSELTQADENEA------PQVD 174
Cdd:PLN02479 111 FLLEH---SKSEVVMVDQEFFTLAEEALKilaekkKSSFKpplliVIGDPTCDPKSLQYALGKGAIEYEKfletgdPEFA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 175 ISPD----DVVALPYSSGTTGLPKGVMLTHKGlitsvAQQVDGDNPNLYFHSED-VILCVLPMFH----IYALNSIMLCG 245
Cdd:PLN02479 188 WKPPadewQSIALGYTSGTTASPKGVVLHHRG-----AYLMALSNALIWGMNEGaVYLWTLPMFHcngwCFTWTLAALCG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 246 LRVgapilIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHdLSSLRMIK---SGGAPLGKELEDTVRAKFp 322
Cdd:PLN02479 263 TNI-----CLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETI-LPLPRVVHvmtAGAAPPPSVLFAMSEKGF- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 323 qaRLGQGYGMTEA-GPVlAMClAFAKEpFDIKPGA------CGTVVRNAEMK---IVDPETGASLPRNQP--GEICIRGD 390
Cdd:PLN02479 336 --RVTHTYGLSETyGPS-TVC-AWKPE-WDSLPPEeqarlnARQGVRYIGLEgldVVDTKTMKPVPADGKtmGEIVMRGN 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 391 QIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDE 470
Cdd:PLN02479 411 MVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDE 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 306440447 471 DAGEVPVAFV-----VKSEKSQATEDEIKQYISKQVIFYKRIKRVFFiEAIPKAPSGKILRKNLKEK 532
Cdd:PLN02479 490 RWGESPCAFVtlkpgVDKSDEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAK 555
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
24-450 |
5.39e-34 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 136.38 E-value: 5.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 24 LHSYVLENLSNHSSKPCL-----INGANGDvY---TYADVElTARR-VASGLNKIGIQQGDVIMLFLPSSPEFVL----- 89
Cdd:PLN02736 46 LHDNFVYAVETFRDYKYLgtrirVDGTVGE-YkwmTYGEAG-TARTaIGSGLVQHGIPKGACVGLYFINRPEWLIvdhac 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 90 -AF----------LGASHRGAIITAAN---PFSTPAELAKH----AKASRAKLLITQACYYEKVKDFARESDVKVMCvds 151
Cdd:PLN02736 124 sAYsyvsvplydtLGPDAVKFIVNHAEvaaIFCVPQTLNTLlsclSEIPSVRLIVVVGGADEPLPSLPSGTGVEIVT--- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 152 apdgclhFSEL-TQADENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLITSVAqqvdGDNPNLYFHSEDVILCVL 230
Cdd:PLN02736 201 -------YSKLlAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVA----GSSLSTKFYPSDVHISYL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 231 PMFHIYA-LNSIML--CGLRVGapilimpkFEIGSLLGL---IEKYKVSIAPVVPPVMMSI------------------- 285
Cdd:PLN02736 270 PLAHIYErVNQIVMlhYGVAVG--------FYQGDNLKLmddLAALRPTIFCSVPRLYNRIydgitnavkesgglkerlf 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 286 -----AK----------SPDLDKHDLSSL--------RMIKSGGAPLGKELEDTVRAKFpQARLGQGYGMTEAGpvlamC 342
Cdd:PLN02736 342 naaynAKkqalengknpSPMWDRLVFNKIkaklggrvRFMSSGASPLSPDVMEFLRICF-GGRVLEGYGMTETS-----C 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 343 LAFAKEPFDIKPGACGTVVRNAEMKIVD-PETGASlPRNQP---GEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDI 418
Cdd:PLN02736 416 VISGMDEGDNLSGHVGSPNPACEVKLVDvPEMNYT-SEDQPyprGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDI 494
|
490 500 510
....*....|....*....|....*....|...
gi 306440447 419 GYIDDDDELFIVDRLKELIKY-KGFQVAPAELE 450
Cdd:PLN02736 495 GLWLPGGRLKIIDRKKNIFKLaQGEYIAPEKIE 527
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
50-531 |
7.46e-34 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 133.08 E-value: 7.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELakhakasRAKLLITQA 129
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDL-------RDRVDRGGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 130 CYyekvkdfaresdvkvmcvdsapdgclhfselTQADENEAPqvdispDDVVALPYSSGTTGLPKGVMLTHKGLITsvaq 209
Cdd:cd05974 74 VY-------------------------------AAVDENTHA------DDPMLLYFTSGTTSKPKLVEHTHRSYPV---- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 210 qvdGDNPNLYF---HSEDVILCVL-PMFHIYALnSIMLCGLRVGAPILIM--PKFEIGSLLGLIEKYKVSIApVVPPVMM 283
Cdd:cd05974 113 ---GHLSTMYWiglKPGDVHWNISsPGWAKHAW-SCFFAPWNAGATVFLFnyARFDAKRVLAALVRYGVTTL-CAPPTVW 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 284 SIAKSPDLDKHDLSsLRMIKSGGAPLGKELEDTVRAKFPQArLGQGYGMTEAgpvlaMCLAFAKEPFDIKPGACGTVVRN 363
Cdd:cd05974 188 RMLIQQDLASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLT-IRDGYGQTET-----TALVGNSPGQPVKAGSMGRPLPG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 364 AEMKIVDPETGASlprnQPGEICI-----RGDQIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFIVDRLKELIK 438
Cdd:cd05974 261 YRVALLDPDGAPA----TEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 439 YKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVV---KSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEa 515
Cdd:cd05974 336 SSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlraGYEPSPETALEIFRFSRERLAPYKRIRRLEFAE- 414
|
490
....*....|....*.
gi 306440447 516 IPKAPSGKILRKNLKE 531
Cdd:cd05974 415 LPKTISGKIRRVELRR 430
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
51-531 |
1.04e-33 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 133.61 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGashrgaIItaanpfstpaelakhaKASRAKLLITQAC 130
Cdd:cd17655 24 TYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILG------IL----------------KAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 131 YYEKVKDFARESDVKVMCVDSAPDGCLHFSEL--------TQADENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKG 202
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQPPIAFIGLidlldedtIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 203 LItsvaQQVDGDNpNLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGS---LLGLIEKYKVSIAPVVP 279
Cdd:cd17655 162 VV----NLVEWAN-KVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDgqaLTQYIRQNRITIIDLTP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 280 PVMMSIAKSpdlDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQAR-LGQGYGMTEAgPVLAMclAFAKEPFDIKPGA-- 356
Cdd:cd17655 237 AHLKLLDAA---DDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPtITNAYGPTET-TVDAS--IYQYEPETDQQVSvp 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 357 CGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATS---------------RTIDKEGWLhtgdigyi 421
Cdd:cd17655 311 IGKPLGNTRIYILD-QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAekfvddpfvpgermyRTGDLARWL-------- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 422 dDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVkSEKSQATEDeIKQYISKQV 501
Cdd:cd17655 382 -PDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV-SEKELPVAQ-LREFLAREL 458
|
490 500 510
....*....|....*....|....*....|..
gi 306440447 502 IFYkrIKRVFFI--EAIPKAPSGKILRKNLKE 531
Cdd:cd17655 459 PDY--MIPSYFIklDEIPLTPNGKVDRKALPE 488
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
19-536 |
1.06e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 133.93 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 19 PKNLPLHSYVLENLSNHSSKPCLINGAngDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRG 98
Cdd:PRK12316 508 PLQRGVHRLFEEQVERTPEAPALAFGE--ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAG 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 99 AIITAANPfSTPAE-LAKHAKASRAKLLITQACYYEKVkDFAREsdVKVMCVDSApdgclhfSELTQADENEAPQVDISP 177
Cdd:PRK12316 586 GAYVPLDP-EYPAErLAYMLEDSGVQLLLSQSHLGRKL-PLAAG--VQVLDLDRP-------AAWLEGYSEENPGTELNP 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 178 DDVVALPYSSGTTGLPKGVMLTHKGLITSV--AQQVDGdnpnlyFHSEDVILCVLPMfhIYALNSIMLCG-LRVGAPILI 254
Cdd:PRK12316 655 ENLAYVIYTSGSTGKPKGAGNRHRALSNRLcwMQQAYG------LGVGDTVLQKTPF--SFDVSVWEFFWpLMSGARLVV 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 255 MPK---FEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDkhDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYG 331
Cdd:PRK12316 727 AAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA--SCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYG 804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 332 MTEAGpVLAMCLAFAKEPFDIKPgaCGTVVRNAEMKIVDPETGAsLPRNQPGEICIRGDQIMKGYLNDPEAT------SR 405
Cdd:PRK12316 805 PTEAA-IDVTHWTCVEEGGDSVP--IGRPIANLACYILDANLEP-VPVGVLGELYLAGRGLARGYHGRPGLTaerfvpSP 880
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 406 TIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKdedaGEVPVAFVVKSEK 485
Cdd:PRK12316 881 FVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLESE 956
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 306440447 486 SQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEKLAGI 536
Cdd:PRK12316 957 GGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASV 1007
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
48-526 |
2.19e-32 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 130.90 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 48 DVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIiTAANPFSTP--------AELAKHAKA 119
Cdd:PRK09192 48 EALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLV-PVPLPLPMGfggresyiAQLRGMLAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 120 SRAKLLItqacYYEKVKDFARESdvkvmcVDSAPdGCLHFSeLTQADENEAPQVD---ISPDDVVALPYSSGTTGLPKGV 196
Cdd:PRK09192 127 AQPAAII----TPDELLPWVNEA------THGNP-LLHVLS-HAWFKALPEADVAlprPTPDDIAYLQYSSGSTRFPRGV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 197 MLTHKGLITsvaqqvdgdnpNLYFHSEDVIL------CV--LPMFH----IYALNSIMLCGLRVGapILIMPKFEIGSL- 263
Cdd:PRK09192 195 IITHRALMA-----------NLRAISHDGLKvrpgdrCVswLPFYHdmglVGFLLTPVATQLSVD--YLPTRDFARRPLq 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 264 -LGLIEKYKVSIApVVPPVMMSI----AKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQ-----GYGMT 333
Cdd:PRK09192 262 wLDLISRNRGTIS-YSPPFGYELcarrVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAGFDDkafmpSYGLA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 334 EAgpVLAMCLA---------------FAKEPFDIKPGA----------CGTVVRNAEMKIVDpETGASLPRNQPGEICIR 388
Cdd:PRK09192 341 EA--TLAVSFSplgsgivveevdrdrLEYQGKAVAPGAetrrvrtfvnCGKALPGHEIEIRN-EAGMPLPERVVGHICVR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 389 GDQIMKGYLNDPEaTSRTIDKEGWLHTgDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEI--SDAAVVG 466
Cdd:PRK09192 418 GPSLMSGYFRDEE-SQDVLAADGWLDT-GDLGYLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFS 495
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 306440447 467 LkDEDAGEVPVAFV----VKSEKSQATEDEIKQyiskqvifykRIKRVFFIE---------AIPKAPSGKILR 526
Cdd:PRK09192 496 I-AQENGEKIVLLVqcriSDEERRGQLIHALAA----------LVRSEFGVEaavelvpphSLPRTSSGKLSR 557
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
46-529 |
2.41e-32 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 128.96 E-value: 2.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 46 NGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAI---ITAANPfstPAELAKHAKASRA 122
Cdd:cd17643 9 EDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAyvpIDPAYP---VERIAFILADSGP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 123 KLLITQacyyekvkdfaresdvkvmcvdsapdgclhfseltqadeneapqvdisPDDVVALPYSSGTTGLPKGVMLTHKG 202
Cdd:cd17643 86 SLLLTD------------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHAN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 203 LITSVAQQvdgdNPNLYFHSEDVILcvlpMFHIYALN-SI--MLCGLRVGAPILIMPKFEIGS---LLGLIEKYKVSIAP 276
Cdd:cd17643 118 VLALFAAT----QRWFGFNEDDVWT----LFHSYAFDfSVweIWGALLHGGRLVVVPYEVARSpedFARLLRDEGVTVLN 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 277 VVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLgkeLEDTVRAKF-----PQARLGQGYGMTEAG-----PVLAMCLAFA 346
Cdd:cd17643 190 QTPSAFYQLVEAADRDGRDPLALRYVIFGGEAL---EAAMLRPWAgrfglDRPQLVNMYGITETTvhvtfRPLDAADLPA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 347 KEPFDIKPGACGTVVRnaemkIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATSR-------TIDKEGWLHTGDIG 419
Cdd:cd17643 267 AAASPIGRPLPGLRVY-----VLD-ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLA 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 420 YIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISK 499
Cdd:cd17643 341 RRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKE 420
|
490 500 510
....*....|....*....|....*....|
gi 306440447 500 QVIFYKRIKRVFFIEAIPKAPSGKILRKNL 529
Cdd:cd17643 421 LLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
24-534 |
6.63e-32 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 128.43 E-value: 6.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 24 LHSYVLENLSNHSSKPClINGANGDVyTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITA 103
Cdd:cd05918 1 VHDLIEERARSQPDAPA-VCAWDGSL-TYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 104 ANPfSTPAElakhakasRAKLLItqacyyekvkdfaRESDVKVMCVDSapdgclhfseltqadeneapqvdisPDDVVAL 183
Cdd:cd05918 79 LDP-SHPLQ--------RLQEIL-------------QDTGAKVVLTSS-------------------------PSDAAYV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 184 PYSSGTTGLPKGVMLTHKGLITSVAQQvdgdNPNLYFHSEDVILCvlpmFHIYALN-SIM--LCGLRVGAPILIMPKFE- 259
Cdd:cd05918 112 IFTSGSTGKPKGVVIEHRALSTSALAH----GRALGLTSESRVLQ----FASYTFDvSILeiFTTLAAGGCLCIPSEEDr 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 260 IGSLLGLIEKYKVSIAPVVPpvmmSIAKSpdLDKHDLSSLRMIKSGGAPLGKEledtVRAKF-PQARLGQGYGMTEAgpv 338
Cdd:cd05918 184 LNDLAGFINRLRVTWAFLTP----SVARL--LDPEDVPSLRTLVLGGEALTQS----DVDTWaDRVRLINAYGPAEC--- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 339 lAMCLAFAKEPFDIKPGACGTVVrNAEMKIVDPETGASL-PRNQPGEICIRGDQIMKGYLNDPEATSRT-IDKEGWLHTG 416
Cdd:cd05918 251 -TIAATVSPVVPSTDPRNIGRPL-GATCWVVDPDNHDRLvPIGAVGELLIEGPILARGYLNDPEKTAAAfIEDPAWLKQE 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 417 DIGYI------------DDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGL-KDEDAGEVP--VAFVV 481
Cdd:cd05918 329 GSGRGrrlyrtgdlvryNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVvKPKDGSSSPqlVAFVV 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 482 KSEKSQATEDEIKQYISKQVIFYKRIKRV-----------------FFIEAIPKAPSGKILRKNLKEKLA 534
Cdd:cd05918 409 LDGSSSGSGDGDSLFLEPSDEFRALVAELrsklrqrlpsymvpsvfLPLSHLPLTASGKIDRRALRELAE 478
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
44-534 |
8.23e-32 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 131.06 E-value: 8.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 44 GANGDVYTYADVELTARRVASGLNKIGiQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPfstPAELAKHAKA---- 119
Cdd:PRK05691 35 PGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYP---PESARRHHQErlls 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 120 ----SRAKLLITQACYYE---KVKDFARESDVKVMCVDSAPDGClhfseltqADENEAPQVDisPDDVVALPYSSGTTGL 192
Cdd:PRK05691 111 iiadAEPRLLLTVADLRDsllQMEELAAANAPELLCVDTLDPAL--------AEAWQEPALQ--PDDIAFLQYTSGSTAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 193 PKGVMLTHKGLITsvaqqvdgdNPNLYFHS-------EDVILCVLPMFHIYALNSIMLCGLRVGAPILIM-PKFEIGS-- 262
Cdd:PRK05691 181 PKGVQVSHGNLVA---------NEQLIRHGfgidlnpDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMsPAYFLERpl 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 263 -LLGLIEKYKVSIA--PVVPPVMMS--IAKSPdLDKHDLSSLRMIKSGGAPLGKELEDTVRAKF------PQARLGQgYG 331
Cdd:PRK05691 252 rWLEAISEYGGTISggPDFAYRLCSerVSESA-LERLDLSRWRVAYSGSEPIRQDSLERFAEKFaacgfdPDSFFAS-YG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 332 MTEAG------------PVLAM-CLAFAKEpfDIKPGA------CGTVVRNAEMKIVDPETGASLPRNQPGEICIRGDQI 392
Cdd:PRK05691 330 LAEATlfvsggrrgqgiPALELdAEALARN--RAEPGTgsvlmsCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 393 MKGYLNDPEATSRTI---DKEGWLHTgDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAH-PEISDAAVVGLK 468
Cdd:PRK05691 408 AHGYWRNPEASAKTFvehDGRTWLRT-GDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREvEVVRKGRVAAFA 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 306440447 469 DEDAGE--VPVAF-----VVKSEKSQATEDEIKQYISKqvIFYKRIKRVFFIE--AIPKAPSGKILRKNLKEKLA 534
Cdd:PRK05691 487 VNHQGEegIGIAAeisrsVQKILPPQALIKSIRQAVAE--ACQEAPSVVLLLNpgALPKTSSGKLQRSACRLRLA 559
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
50-531 |
8.35e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 128.99 E-value: 8.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDV-IMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQ 128
Cdd:PRK13388 27 WTWREVLAEAAARAAALIALADPDRPLhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 129 ACYYEKVKDFAReSDVKVMCVDSApdgclHFSELTQADENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLITSVA 208
Cdd:PRK13388 107 AEHRPLLDGLDL-PGVRVLDVDTP-----AYAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 209 QQVDGDNpnlyFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKS 288
Cdd:PRK13388 181 ALTERFG----LTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSASGFLDDVRRYGATYFNYVGKPLAYILAT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 289 PDLDKHDLSSLRmiksggAPLGKELEDTVRAKFPQ---ARLGQGYGMTEAGpvlamcLAFAKEPfDIKPGACGtvvRNAE 365
Cdd:PRK13388 257 PERPDDADNPLR------VAFGNEASPRDIAEFSRrfgCQVEDGYGSSEGA------VIVVREP-GTPPGSIG---RGAP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 366 -MKIVDPETGASLPRNQ-------------PGEICIR-GDQIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFIV 430
Cdd:PRK13388 321 gVAIYNPETLTECAVARfdahgallnadeaIGELVNTaGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGWIYFA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 431 DRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQ----VIFYKR 506
Cdd:PRK13388 400 GRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFAAFLAAQpdlgTKAWPR 479
|
490 500
....*....|....*....|....*
gi 306440447 507 IKRVffIEAIPKAPSGKILRKNLKE 531
Cdd:PRK13388 480 YVRI--AADLPSTATNKVLKRELIA 502
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
19-529 |
2.33e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 129.69 E-value: 2.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 19 PKNLPLHSYVLENLSNHSSKPCLIngANGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRG 98
Cdd:PRK12316 2000 PRGPGVHQRIAEQAARAPEAIAVV--FGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAG 2077
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 99 AIITAANPfSTPAE-LAKHAKASRAKLLITQACYYEKVKDFAresdvKVMCVDSAPDGCLhfseltQADENEAPQVDISP 177
Cdd:PRK12316 2078 GAYVPLDP-NYPAErLAYMLEDSGAALLLTQRHLLERLPLPA-----GVARLPLDRDAEW------ADYPDTAPAVQLAG 2145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 178 DDVVALPYSSGTTGLPKGVMLTHKGLI-----TSVAQQVDGDNPNLYFHSedvilcvlpmFHIYALNSIMLCGLRVGAPI 252
Cdd:PRK12316 2146 ENLAYVIYTSGSTGLPKGVAVSHGALVahcqaAGERYELSPADCELQFMS----------FSFDGAHEQWFHPLLNGARV 2215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 253 LIMPK--FEIGSLLGLIEKYKVSIApVVPPVMM-SIAKSPDLDKHDLSsLRMIKSGGAPLGKELEDTVRAKFPQARLGQG 329
Cdd:PRK12316 2216 LIRDDelWDPEQLYDEMERHGVTIL-DFPPVYLqQLAEHAERDGRPPA-VRVYCFGGEAVPAASLRLAWEALRPVYLFNG 2293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 330 YGMTEAGPVLAMCLAFAKEPFDIKPGACGTVVRNAEMKIVDPETGAsLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDK 409
Cdd:PRK12316 2294 YGPTEAVVTPLLWKCRPQDPCGAAYVPIGRALGNRRAYILDADLNL-LAPGMAGELYLGGEGLARGYLNRPGLTAERFVP 2372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 410 EGWLH-------TGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLkDEDAGEVPVAFVVK 482
Cdd:PRK12316 2373 DPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVP 2451
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 306440447 483 SEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNL 529
Cdd:PRK12316 2452 DDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
174-523 |
3.80e-31 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 126.85 E-value: 3.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 174 DISPDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQVDGDNPNlyfhSEDVILCVLPMFHIYALNSIMLCGLRVGAPIL 253
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPK----EDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 254 -----IMPKfeigSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQ 328
Cdd:PRK06334 255 faynpLYPK----KIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQ 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 329 GYGMTEAGPVLAmcLAFAKEPfdiKPGAC-GTVVRNAEMKIVDPETGASLPRNQPGEICIRGDQIMKGYL-NDPEATSRT 406
Cdd:PRK06334 331 GYGTTECSPVIT--INTVNSP---KHESCvGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSLFSGYLgEDFGQGFVE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 407 IDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAH---PEISDAA---VVGLKDEDagEVPVAFV 480
Cdd:PRK06334 406 LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGfgqNAADHAGplvVCGLPGEK--VRLCLFT 483
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 306440447 481 VKSEKSQATEDEIKQYISKQVIfykRIKRVFFIEAIPKAPSGK 523
Cdd:PRK06334 484 TFPTSISEVNDILKNSKTSSIL---KISYHHQVESIPMLGTGK 523
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
48-530 |
1.25e-30 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 126.68 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 48 DVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLIT 127
Cdd:PRK06060 29 DVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 128 QAcyyeKVKDFARESDVkvmcVDSAPdgclHFSELTQADENEAPQVdiSPDDVVALPYSSGTTGLPKGVMLTHKGLITSV 207
Cdd:PRK06060 109 SD----ALRDRFQPSRV----AEAAE----LMSEAARVAPGGYEPM--GGDALAYATYTSGTTGPPKAAIHRHADPLTFV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 208 AQQVdgdNPNLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMP---KFEIGSLLGliEKYKVSIAPVVPPVMMS 284
Cdd:PRK06060 175 DAMC---RKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSapvTPEAAAILS--ARFGPSVLYGVPNFFAR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 285 I--AKSPDldkhDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEAGPVLAmclafAKEPFDIKPGACGTVVR 362
Cdd:PRK06060 250 VidSCSPD----SFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFV-----SNRVDEWRLGTLGRVLP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 363 NAEMKIVDPETGASLPRNQpGEICIRGDQIMKGYLNDPEAtsrTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGF 442
Cdd:PRK06060 321 PYEIRVVAPDGTTAGPGVE-GDLWVRGPAIAKGYWNRPDS---PVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 443 QVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATED---EIKQYISKQVIFYKRIKRVFFIEAIPKA 519
Cdd:PRK06060 397 NVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSvmrDLHRGLLNRLSAFKVPHRFAVVDRLPRT 476
|
490
....*....|.
gi 306440447 520 PSGKILRKNLK 530
Cdd:PRK06060 477 PNGKLVRGALR 487
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
51-466 |
2.31e-30 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 125.16 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQ--GDVIMLFlpSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLI-- 126
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERfhGVGILGF--NSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVve 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 127 --TQACYYEKVKDFARESDVKVMCVDSAP---DGCLHFSE-LTQADENEAPQVD-----ISPDDVVALPYSSGTTGLPKG 195
Cdd:cd05933 88 nqKQLQKILQIQDKLPHLKAIIQYKEPLKekePNLYSWDEfMELGRSIPDEQLDaiissQKPNQCCTLIYTSGTTGMPKG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 196 VMLTHKGLI---TSVAQQVDGDNPNlyfHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEI-GSLLGLIEKYK 271
Cdd:cd05933 168 VMLSHDNITwtaKAASQHMDLRPAT---VGQESVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQPDALkGTLVKTLREVR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 272 VSIAPVVPPV---------------------MMSIAKSPDLD---------------KHDLSSLRMIK------------ 303
Cdd:cd05933 245 PTAFMGVPRVwekiqekmkavgaksgtlkrkIASWAKGVGLEtnlklmggespsplfYRLAKKLVFKKvrkalgldrcqk 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 304 --SGGAPLGKELEDTVRAKfpQARLGQGYGMTE-AGPVlAMCLafakePFDIKPGACGTVVRNAEMKIVDPETgaslprN 380
Cdd:cd05933 325 ffTGAAPISRETLEFFLSL--NIPIMELYGMSEtSGPH-TISN-----PQAYRLLSCGKALPGCKTKIHNPDA------D 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 381 QPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQ-VAPAELEALLIAH-PE 458
Cdd:cd05933 391 GIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGEnVPPVPIEDAVKKElPI 470
|
....*...
gi 306440447 459 ISDAAVVG 466
Cdd:cd05933 471 ISNAMLIG 478
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
51-529 |
2.49e-30 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 123.35 E-value: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPfSTPAE-LAKHAKASRAKLLITQa 129
Cdd:cd17650 14 TYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDP-DYPAErLQYMLEDSGAKLLLTQ- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 130 cyyekvkdfaresdvkvmcvdsapdgclhfseltqadeneapqvdisPDDVVALPYSSGTTGLPKGVMLTHKglitSVAQ 209
Cdd:cd17650 92 -----------------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHR----NVAH 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 210 QVDGDNPNLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMP---KFEIGSLLGLIEKYKVSIAPVVPPVMMSIA 286
Cdd:cd17650 121 AAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPdevKLDPAALYDLILKSRITLMESTPALIRPVM 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 287 KSPDLDKHDLSSLRMIKSGGaplgkeleDTVRAKFPQ---ARLGQG------YGMTEAgpvlAMCLAFAKEPFDIKPGA- 356
Cdd:cd17650 201 AYVYRNGLDLSAMRLLIVGS--------DGCKAQDFKtlaARFGQGmriinsYGVTEA----TIDSTYYEEGRDPLGDSa 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 357 ---CGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATS---------------RTIDKEGWLhtgdi 418
Cdd:cd17650 269 nvpIGRPLPNTAMYVLD-ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAerfvenpfapgermyRTGDLARWR----- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 419 gyidDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQAteDEIKQYIS 498
Cdd:cd17650 343 ----ADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNT--AELRAFLA 416
|
490 500 510
....*....|....*....|....*....|.
gi 306440447 499 KQVIFYKRIKRVFFIEAIPKAPSGKILRKNL 529
Cdd:cd17650 417 KELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
177-535 |
3.26e-30 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 123.75 E-value: 3.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 177 PDDVVALPYSSGTTGLPKGVMLTHKGLIT---SVAQQVDGDnpnlyfhSEDVILCVLPMFHIYALNSIMLCGLRVGAPIL 253
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHnmfAILNSTEWK-------TKDRILSWMPLTHDMGLIAFHLAPLIAGMNQY 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 254 IMPK--FEIGSLLGL--IEKYKVSIapVVPP-----VMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQA 324
Cdd:cd05908 178 LMPTrlFIRRPILWLkkASEHKATI--VSSPnfgykYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKY 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 325 RLGQG-----YGMTEAGpvLAMCLAFAKEPF-------------------DIKPGACGTVVR------NAEMKIVDpETG 374
Cdd:cd05908 256 GLKRNailpvYGLAEAS--VGASLPKAQSPFktitlgrrhvthgepepevDKKDSECLTFVEvgkpidETDIRICD-EDN 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 375 ASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGdIGYIDDDDELFIVDRLKELIKYKGFQVAPAELE--AL 452
Cdd:cd05908 333 KILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTG-DLGFIRNGRLVITGREKDIIFVNGQNVYPHDIEriAE 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 453 LIAHPEISDAAVVGLKDEDAGEVPV-AFVVKSEKsqatEDEIKQYISK-QVIFYKR----IKRVFFIEAIPKAPSGKILR 526
Cdd:cd05908 412 ELEGVELGRVVACGVNNSNTRNEEIfCFIEHRKS----EDDFYPLGKKiKKHLNKRggwqINEVLPIRRIPKTTSGKVKR 487
|
....*....
gi 306440447 527 KNLKEKLAG 535
Cdd:cd05908 488 YELAQRYQS 496
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
51-529 |
3.55e-30 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 122.81 E-value: 3.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAI---ITAANPfstPAELAKHAKASRAKLLIT 127
Cdd:cd12115 26 TYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAyvpLDPAYP---PERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 128 QacyyekvkdfaresdvkvmcvdsapdgclhfseltqadeneapqvdisPDDVVALPYSSGTTGLPKGVMLTHKGLITSV 207
Cdd:cd12115 103 D------------------------------------------------PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 208 aqQVDGDNpnlyfHSEDVILCVLpmfhiyALNSI--------MLCGLRVGAPILImpkfeIGSLLGLIE---KYKVSIAP 276
Cdd:cd12115 135 --QWAAAA-----FSAEELAGVL------ASTSIcfdlsvfeLFGPLATGGKVVL-----ADNVLALPDlpaAAEVTLIN 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 277 VVPPVMMSiakspdLDKHDL--SSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEAG--PVLAMCLAFAKEPFDI 352
Cdd:cd12115 197 TVPSAAAE------LLRHDAlpASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTtySTVAPVPPGASGEVSI 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 353 kpgacGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATS---------------RTIDKEGWLhtgd 417
Cdd:cd12115 271 -----GRPLANTQAYVLD-RALQPVPLGVPGELYIGGAGVARGYLGRPGLTAerflpdpfgpgarlyRTGDLVRWR---- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 418 igyidDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYI 497
Cdd:cd12115 341 -----PDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHL 415
|
490 500 510
....*....|....*....|....*....|..
gi 306440447 498 SKQVIFYKRIKRVFFIEAIPKAPSGKILRKNL 529
Cdd:cd12115 416 GTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
51-529 |
4.47e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 123.57 E-value: 4.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITaanPFSTPAELAKHAKASRAKLLITQAC 130
Cdd:PRK13383 62 SYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVV---PISTEFRSDALAAALRAHHISTVVA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 131 YYEKVKDFARESDvKVMCVDSAPDGclhfseltqADENEAPQVDISPDDVVALpySSGTTGLPKGVMLTHKgLITSVAQQ 210
Cdd:PRK13383 139 DNEFAERIAGADD-AVAVIDPATAG---------AEESGGRPAVAAPGRIVLL--TSGTTGKPKGVPRAPQ-LRSAVGVW 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 211 VD-GDNPNLYFHSEdvILCVLPMFHIYALNSIMLCgLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSP 289
Cdd:PRK13383 206 VTiLDRTRLRTGSR--ISVAMPMFHGLGLGMLMLT-IALGGTVLTHRHFDAEAALAQASLHRADAFTAVPVVLARILELP 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 290 DL--DKHDLSSLRMIKSGGaplgKELEDTVRAKFPQAR---LGQGYGMTEAGpvlamcLAFAKEPFDIK--PGACGTVVR 362
Cdd:PRK13383 283 PRvrARNPLPQLRVVMSSG----DRLDPTLGQRFMDTYgdiLYNGYGSTEVG------IGALATPADLRdaPETVGKPVA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 363 NAEMKIVDPETGASLPRnQPGEICIRGDQIMKGYLNDpeATSRTIDkeGWLHTGDIGYIDDDDELFIVDRLKELIKYKGF 442
Cdd:PRK13383 353 GCPVRILDRNNRPVGPR-VTGRIFVGGELAGTRYTDG--GGKAVVD--GMTSTGDMGYLDNAGRLFIVGREDDMIISGGE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 443 QVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSG 522
Cdd:PRK13383 428 NVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTG 507
|
....*..
gi 306440447 523 KILRKNL 529
Cdd:PRK13383 508 KVLRKEL 514
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
47-531 |
3.18e-29 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 123.35 E-value: 3.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 47 GDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPfSTPAE-LAKHAKASRAKLL 125
Cdd:PRK05691 1154 GGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDP-DYPAErLAYMLADSGVELL 1232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 126 ITQACYYEKVkdfARESDVKVMCVDSapdgcLHFSELTqadeNEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLit 205
Cdd:PRK05691 1233 LTQSHLLERL---PQAEGVSAIALDS-----LHLDSWP----SQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAAL-- 1298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 206 svAQQVDGDNPNLYFHSEDVILCVLPM-FHIyalnSIMLC--GLRVGAPILIMPKFE---IGSLLGLIEKYKVSIAPVVP 279
Cdd:PRK05691 1299 --AERLQWMQATYALDDSDVLMQKAPIsFDV----SVWECfwPLITGCRLVLAGPGEhrdPQRIAELVQQYGVTTLHFVP 1372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 280 PVMMSIAKSPDLdkHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEAGPVLA--MCLAFAKEPFDIkpgac 357
Cdd:PRK05691 1373 PLLQLFIDEPLA--AACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVThwQCQAEDGERSPI----- 1445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 358 GTVVRNAEMKIVDPETgASLPRNQPGEICIRGDQIMKGYLNDPEATS----------------RTIDKEGWLHTGDigyi 421
Cdd:PRK05691 1446 GRPLGNVLCRVLDAEL-NLLPPGVAGELCIGGAGLARGYLGRPALTAerfvpdplgedgarlyRTGDRARWNADGA---- 1520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 422 ddddeLFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVgLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQV 501
Cdd:PRK05691 1521 -----LEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGEAGQEAEAERLKAALAAEL 1594
|
490 500 510
....*....|....*....|....*....|
gi 306440447 502 IFYKRIKRVFFIEAIPKAPSGKILRKNLKE 531
Cdd:PRK05691 1595 PEYMVPAQLIRLDQMPLGPSGKLDRRALPE 1624
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
51-529 |
7.86e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 122.19 E-value: 7.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQAC 130
Cdd:PRK12467 1601 TYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSH 1680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 131 YYEKVkdfaresdvkvmcvdSAPDGcLHFSELTQADE------NEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLI 204
Cdd:PRK12467 1681 LQARL---------------PLPDG-LRSLVLDQEDDwlegysDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALV 1744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 205 -----TSVAQQVDGDNPNLYFHSEDVILCVLPMFHiyalnsimlcGLRVGAPILIMPkFEI----GSLLGLIEKYKVSIA 275
Cdd:PRK12467 1745 nrlcaTQEAYQLSAADVVLQFTSFAFDVSVWELFW----------PLINGARLVIAP-PGAhrdpEQLIQLIERQQVTTL 1813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 276 PVVPPVMMSIAKSPDLDKHDLSsLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEAG--PVLAMCLAFAKEPFDIK 353
Cdd:PRK12467 1814 HFVPSMLQQLLQMDEQVEHPLS-LRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAvdVTHWTCRRKDLEGRDSV 1892
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 354 PgaCGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATS----------------RTIDKEGWlhtgd 417
Cdd:PRK12467 1893 P--IGQPIANLSTYILD-ASLNPVPIGVAGELYLGGVGLARGYLNRPALTAerfvadpfgtvgsrlyRTGDLARY----- 1964
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 418 igyiDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGlKDEDAGEVPVAFVV--------KSEKSQAT 489
Cdd:PRK12467 1965 ----RADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA-QDGANGKQLVAYVVptdpglvdDDEAQVAL 2039
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 306440447 490 EDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNL 529
Cdd:PRK12467 2040 RAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
51-529 |
1.23e-28 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 118.12 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPfSTPAE-LAKHAKASRAKLLITQa 129
Cdd:cd17652 14 TYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDP-AYPAErIAYMLADARPALLLTT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 130 cyyekvkdfaresdvkvmcvdsapdgclhfseltqadeneapqvdisPDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQ 209
Cdd:cd17652 92 -----------------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 210 QVDGDNPN-----LYFHSedvilcvlPMFHIYALNSIMlcGLRVGAPILIMPKFEIGS---LLGLIEKYKVSIAPVVPPV 281
Cdd:cd17652 125 QIAAFDVGpgsrvLQFAS--------PSFDASVWELLM--ALLAGATLVLAPAEELLPgepLADLLREHRITHVTLPPAA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 282 MMSIakSPDldkhDLSSLRMIKSGGAPLGKELedtVRAKFPQARLGQGYGMTEA--GPVLAMCLAFAKEPfdikpgACGT 359
Cdd:cd17652 195 LAAL--PPD----DLPDLRTLVVAGEACPAEL---VDRWAPGRRMINAYGPTETtvCATMAGPLPGGGVP------PIGR 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 360 VVRNAEMKIVDPETgASLPRNQPGEICIRGDQIMKGYLNDPEATS----------------RTIDKEGWLhtgdigyidD 423
Cdd:cd17652 260 PVPGTRVYVLDARL-RPVPPGVPGELYIAGAGLARGYLNRPGLTAerfvadpfgapgsrmyRTGDLARWR---------A 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 424 DDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIF 503
Cdd:cd17652 330 DGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPG 409
|
490 500
....*....|....*....|....*.
gi 306440447 504 YKRIKRVFFIEAIPKAPSGKILRKNL 529
Cdd:cd17652 410 YMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
46-531 |
2.32e-28 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 117.41 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 46 NGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPfSTPAELAKHA-KASRAKL 124
Cdd:cd17653 19 LGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDA-KLPSARIQAIlRTSGATL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 125 LITQAcyyekvkdfaresdvkvmcvdsapdgclhfseltqadeneapqvdiSPDDVVALPYSSGTTGLPKGVMLTHKGlI 204
Cdd:cd17653 98 LLTTD----------------------------------------------SPDDLAYIIFTSGSTGIPKGVMVPHRG-V 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 205 TSVAQQVdGDNPNLYFHSEdvilcVLPMFHI---YALNSIMLCGLRVGAPILIMPKFEIGSLLGliekyKVSIAPVVPPV 281
Cdd:cd17653 131 LNYVSQP-PARLDVGPGSR-----VAQVLSIafdACIGEIFSTLCNGGTLVLADPSDPFAHVAR-----TVDALMSTPSI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 282 MMSIakSPDldkhDLSSLRMIKSGGAPLGKELedtVRAKFPQARLGQGYGMTEAgpvlaMCLAFAKEPFDIKPGACGTVV 361
Cdd:cd17653 200 LSTL--SPQ----DFPNLKTIFLGGEAVPPSL---LDRWSPGRRLYNAYGPTEC-----TISSTMTELLPGQPVTIGKPI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 362 RNAEMKIVDPETGASlPRNQPGEICIRGDQIMKGYLNDPEATSR----TIDKEGWLH--TGDIGYIDDDDELFIVDRLKE 435
Cdd:cd17653 266 PNSTCYILDADLQPV-PEGVVGEICISGVQVARGYLGNPALTASkfvpDPFWPGSRMyrTGDYGRWTEDGGLEFLGREDN 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 436 LIKYKGFQVA-PAELEALLIAHPEISDAAVVGLKDedageVPVAFVVKSEksqATEDEIKQYISKQVIFYKRIKRVFFIE 514
Cdd:cd17653 345 QVKVRGFRINlEEIEEVVLQSQPEVTQAAAIVVNG-----RLVAFVTPET---VDVDGLRSELAKHLPSYAVPDRIIALD 416
|
490
....*....|....*..
gi 306440447 515 AIPKAPSGKILRKNLKE 531
Cdd:cd17653 417 SFPLTANGKVDRKALRE 433
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
51-528 |
3.05e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 118.56 E-value: 3.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAAnPFSTP-AELAKHAKASR-------A 122
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTML-HQPTPrTDLAVWAEDTLrvigmigA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 123 KLLITQACYyEKVKDFARESDVKVmcvdsapdgcLHFSELTQADEneAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKG 202
Cdd:PRK07768 110 KAVVVGEPF-LAAAPVLEEKGIRV----------LTVADLLAADP--IDPVETGEDDLALMQLTSGSTGSPKAVQITHGN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 203 LITSVAQQVDGdnpnLYFHSE-DVILCVLPMFH----IYALNSIMLCGLRVgapILIMP-KFEIGSLL--GLIEKYKVSI 274
Cdd:PRK07768 177 LYANAEAMFVA----AEFDVEtDVMVSWLPLFHdmgmVGFLTVPMYFGAEL---VKVTPmDFLRDPLLwaELISKYRGTM 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 275 --AP-----VVPPVMMSIAKSPDLDkhdLSSLRMIKSGGAPLGKE-LEDTVRA----KFPQARLGQGYGMTEA------- 335
Cdd:PRK07768 250 taAPnfayaLLARRLRRQAKPGAFD---LSSLRFALNGAEPIDPAdVEDLLDAgarfGLRPEAILPAYGMAEAtlavsfs 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 336 ----GPVL---------AMCLAFAKEPFDIKPGAC-GTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLnDPE 401
Cdd:PRK07768 327 pcgaGLVVdevdadllaALRRAVPATKGNTRRLATlGPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYL-TMD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 402 ATSRTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELE--ALLIAHPEISDAAVVGLkdeDAGEVPVAF 479
Cdd:PRK07768 405 GFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIEraAARVEGVRPGNAVAVRL---DAGHSREGF 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 306440447 480 VVKSE-KSQATEDEIKQyISKQV---IFYK---RIKRVFFIEA--IPKAPSGKILRKN 528
Cdd:PRK07768 482 AVAVEsNAFEDPAEVRR-IRHQVaheVVAEvgvRPRNVVVLGPgsIPKTPSGKLRRAN 538
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
50-492 |
7.51e-28 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 116.80 E-value: 7.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKllitqA 129
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK-----A 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 130 CYYEKVKDF-ARESDVK---VMCVDSAPDGCLHFSELTQADENEAPQVDIS---PDDVVALPYSSGTTGLPKGVMLTHKG 202
Cdd:cd05932 82 LFVGKLDDWkAMAPGVPeglISISLPPPSAANCQYQWDDLIAQHPPLEERPtrfPEQLATLIYTSGTTGQPKGVMLTFGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 203 LITSVAQQVD--GDNPNlyfhseDVILCVLPMFHIYALNSIMLCGLRVGA-------------------PIL------IM 255
Cdd:cd05932 162 FAWAAQAGIEhiGTEEN------DRMLSYLPLAHVTERVFVEGGSLYGGVlvafaesldtfvedvqrarPTLffsvprLW 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 256 PKFEIGsLLGLIEKYKVSIAPVVPpVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRakfpqaRLG----QGYG 331
Cdd:cd05932 236 TKFQQG-VQDKIPQQKLNLLLKIP-VVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALLEWYR------SLGlnilEAYG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 332 MTEAGPVLAMClafakEPFDIKPGACGTVVRNAEMKIVDPetgaslprnqpGEICIRGDQIMKGYLNDPEATSRTIDKEG 411
Cdd:cd05932 308 MTENFAYSHLN-----YPGRDKIGTVGNAGPGVEVRISED-----------GEILVRSPALMMGYYKDPEATAEAFTADG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 412 WLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEALLIAHPEISDAAVVGlkdedAG-EVPVAFVVKSEKSQAT 489
Cdd:cd05932 372 FLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIG-----SGlPAPLALVVLSEEARLR 446
|
...
gi 306440447 490 EDE 492
Cdd:cd05932 447 ADA 449
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
49-466 |
1.05e-27 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 117.14 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 49 VYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELA---KHAKASRA--- 122
Cdd:cd17641 11 EFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAyllNYTGARVViae 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 123 ------KLL--------ITQACYYEKvKDFARESDVKVMcvdSAPDgclhFSELTQADENEAPQV------DISPDDVVA 182
Cdd:cd17641 91 deeqvdKLLeiadripsVRYVIYCDP-RGMRKYDDPRLI---SFED----VVALGRALDRRDPGLyerevaAGKGEDVAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 183 LPYSSGTTGLPKGVMLTHKGLITSVA--QQVDGDNPNlyfhseDVILCVLP----MFHIYALNSIMLCGLRVGAP----- 251
Cdd:cd17641 163 LCTTSGTTGKPKLAMLSHGNFLGHCAayLAADPLGPG------DEYVSVLPlpwiGEQMYSVGQALVCGFIVNFPeepet 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 252 ------------ILIMPK-----------------------FEIGSLLGL-IEKYKVSIAPVVPPVMMS------IAKSP 289
Cdd:cd17641 237 mmedlreigptfVLLPPRvwegiaadvrarmmdatpfkrfmFELGMKLGLrALDRGKRGRPVSLWLRLAswladaLLFRP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 290 DLDKHDLSSLRMIKSGGAPLGKELEDTVRAKfpQARLGQGYGMTEAgpvlaMCLAFAKEPFDIKPGACGTVVRNAEMKIv 369
Cdd:cd17641 317 LRDRLGFSRLRSAATGGAALGPDTFRFFHAI--GVPLKQLYGQTEL-----AGAYTVHRDGDVDPDTVGVPFPGTEVRI- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 370 dpetgaslprNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIK-YKGFQVAPAE 448
Cdd:cd17641 389 ----------DEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTtSDGTRFSPQF 458
|
490
....*....|....*...
gi 306440447 449 LEALLIAHPEISDAAVVG 466
Cdd:cd17641 459 IENKLKFSPYIAEAVVLG 476
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
19-536 |
1.07e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 118.52 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 19 PKNLPLHSYVLENLSNHSSKPCLINGanGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRG 98
Cdd:PRK12316 4548 PATRCVHQLVAERARMTPDAVAVVFD--EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAG 4625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 99 AIITAANPFSTPAELAKHAKASRAKLLITQACYYEKVkdfaresdvkvmcvdSAPDGcLHFSELTQADE-----NEAPQV 173
Cdd:PRK12316 4626 GAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRL---------------PIPDG-LASLALDRDEDwegfpAHDPAV 4689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 174 DISPDDVVALPYSSGTTGLPKGVMLTHKGLI-----TSVAQQVDGDNPNLYFHSEDVILCVLPMFHiyalnsimlcGLRV 248
Cdd:PRK12316 4690 RLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVnhlhaTGERYELTPDDRVLQFMSFSFDGSHEGLYH----------PLIN 4759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 249 GAPILIMPK--FEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKhDLSSLRMIKSGGAPLGKELEDTVRAKFPQARL 326
Cdd:PRK12316 4760 GASVVIRDDslWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDG-EPPSLRVYCFGGEAVAQASYDLAWRALKPVYL 4838
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 327 GQGYGMTEAG--PVLAMCLAFAKEPFDIKPgaCGTVVRNAEMKIVDPEtGASLPRNQPGEICIRGDQIMKGYLNDPEATS 404
Cdd:PRK12316 4839 FNGYGPTETTvtVLLWKARDGDACGAAYMP--IGTPLGNRSGYVLDGQ-LNPLPVGVAGELYLGGEGVARGYLERPALTA 4915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 405 -RTI----DKEG--WLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGlKDEDAGEVPV 477
Cdd:PRK12316 4916 eRFVpdpfGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIA-QEGAVGKQLV 4994
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 306440447 478 AFVVKSEKSQATEDE--------IKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEKLAGI 536
Cdd:PRK12316 4995 GYVVPQDPALADADEaqaelrdeLKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASL 5061
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-529 |
2.89e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 117.18 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 3 PQEEFIFRSKLP--DIYiPKNLPLHSYVLENLSNHSSKPCLINGanGDVYTYADVELTARRVASGLNKIGIQQGDVIMLF 80
Cdd:PRK12467 3075 HERRQVLHAWNAtaAAY-PSERLVHQLIEAQVARTPEAPALVFG--DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVA 3151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 81 LPSSPEFVLAFLGASHRGAIITAANPfSTPAE-LAKHAKASRAKLLITQACYYEKVkdfARESDVKVMCVDSApdgclhf 159
Cdd:PRK12467 3152 VERSVEMIVALLAVLKAGGAYVPLDP-EYPRErLAYMIEDSGVKLLLTQAHLLEQL---PAPAGDTALTLDRL------- 3220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 160 SELTQADENeaPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLI--TSVAQQ---VDGDNPNLYFHSEDVILCVLPMFh 234
Cdd:PRK12467 3221 DLNGYSENN--PSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALAnhLCWIAEayeLDANDRVLLFMSFSFDGAQERFL- 3297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 235 iyalnSIMLCG--LRVGAPILIMPKfeigSLLGLIEKYKVSIAPVVPPVMMSIAKspDLDKHDLSSLRMIKSGGAPLGKE 312
Cdd:PRK12467 3298 -----WTLICGgcLVVRDNDLWDPE----ELWQAIHAHRISIACFPPAYLQQFAE--DAGGADCASLDIYVFGGEAVPPA 3366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 313 LEDTVRAKFPQARLGQGYGMTEAG--PVLAMClafakePFDIKPGAC----GTVVRNAEMKIVDpETGASLPRNQPGEIC 386
Cdd:PRK12467 3367 AFEQVKRKLKPRGLTNGYGPTEAVvtVTLWKC------GGDAVCEAPyapiGRPVAGRSIYVLD-GQLNPVPVGVAGELY 3439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 387 IRGDQIMKGYLNDPEATS----------------RTID-----KEGwlhtgdigyiddddelfIVD---RLKELIKYKGF 442
Cdd:PRK12467 3440 IGGVGLARGYHQRPSLTAerfvadpfsgsggrlyRTGDlaryrADG-----------------VIEylgRIDHQVKIRGF 3502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 443 QVAPAELEALLIAHPEISDAAVVGlKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSG 522
Cdd:PRK12467 3503 RIELGEIEARLLQHPSVREAVVLA-RDGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNG 3581
|
....*..
gi 306440447 523 KILRKNL 529
Cdd:PRK12467 3582 KVDRKAL 3588
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
46-457 |
6.06e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 115.07 E-value: 6.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 46 NGDVY-TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIitAANPFSTPAELA-KHA-KASRA 122
Cdd:PTZ00216 117 NETRYiTYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMV--AATVYANLGEDAlAYAlRETEC 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 123 KLLItqaCYYEKVKDFARESDVKVM------CVDSAPD-----GC--LHFSELTQADENEAPQVDISP----DDVVALPY 185
Cdd:PTZ00216 195 KAIV---CNGKNVPNLLRLMKSGGMpnttiiYLDSLPAsvdteGCrlVAWTDVVAKGHSAGSHHPLNIpennDDLALIMY 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 186 SSGTTGLPKGVMLTHKGLITSVAQQVDGDNPNLYFHSEDVILCV-LPMFHI--YALNSIML---CGLRVGAPILIMPKFE 259
Cdd:PTZ00216 272 TSGTTGDPKGVMHTHGSLTAGILALEDRLNDLIGPPEEDETYCSyLPLAHImeFGVTNIFLargALIGFGSPRTLTDTFA 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 260 I--GSLlgliEKYKVSIAPVVPPVMMSI-----AKSPD--------LDKHDLSSLRMIK--------------------- 303
Cdd:PTZ00216 352 RphGDL----TEFRPVFLIGVPRIFDTIkkaveAKLPPvgslkrrvFDHAYQSRLRALKegkdtpywnekvfsapravlg 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 304 -------SGGAPLGKELEDTVRAKFpqARLGQGYGMTEAgpvlaMCLAFAKEPFDIKPGACGTVVRNAEMKIVDPE---- 372
Cdd:PTZ00216 428 grvramlSGGGPLSAATQEFVNVVF--GMVIQGWGLTET-----VCCGGIQRTGDLEPNAVGQLLKGVEMKLLDTEeykh 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 373 TGASLPRnqpGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIK-YKGFQVAPAELEA 451
Cdd:PTZ00216 501 TDTPEPR---GEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKnCLGEYIALEALEA 577
|
....*.
gi 306440447 452 LLIAHP 457
Cdd:PTZ00216 578 LYGQNE 583
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
52-535 |
6.56e-27 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 114.34 E-value: 6.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 52 YADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASR-AKLLITQAC 130
Cdd:PRK05857 44 YRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDpAAALVAPGS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 131 YYEKVKDFARESDVKVMCVDSAPDGCLHFSELTQAdeNEAPQVDISPDDVVALPYSSGTTGLPKGVMLTH---------- 200
Cdd:PRK05857 124 KMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAA--SLAGNADQGSEDPLAMIFTSGTTGEPKAVLLANrtffavpdil 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 201 --KGL--ITSVaqqvdgDNPNLYfhsedvilCVLPMFHIYALNSIMLCGLRVGapILIMPKFEIGSLLGLIEKYKVSIAP 276
Cdd:PRK05857 202 qkEGLnwVTWV------VGETTY--------SPLPATHIGGLWWILTCLMHGG--LCVTGGENTTSLLEILTTNAVATTC 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 277 VVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAplgKELEDTVRakFPQA---RLGQGYGMTEAGpVLAMCLAFAKEPFD-I 352
Cdd:PRK05857 266 LVPTLLSKLVSELKSANATVPSLRLVGYGGS---RAIAADVR--FIEAtgvRTAQVYGLSETG-CTALCLPTDDGSIVkI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 353 KPGACGTVVRNAEMKIV-----DPETGASLPRNQPGEICIRGDQIMKGYLNDPEATsRTIDKEGWLHTGDIGYIDDDDEL 427
Cdd:PRK05857 340 EAGAVGRPYPGVDVYLAatdgiGPTAPGAGPSASFGTLWIKSPANMLGYWNNPERT-AEVLIDGWVNTGDLLERREDGFF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 428 FIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGE-VPVAFVVKSEKSQATEDEIKQYISKQvifYKR 506
Cdd:PRK05857 419 YIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGAlVGLAVVASAELDESAARALKHTIAAR---FRR 495
|
490 500 510
....*....|....*....|....*....|....*.
gi 306440447 507 ----IKR---VFFIEAIPKAPSGKILRKNLKEKLAG 535
Cdd:PRK05857 496 esepMARpstIVIVTDIPRTQSGKVMRASLAAAATA 531
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
46-534 |
1.74e-26 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 112.27 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 46 NGDVYTYAdvELTAR--RVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPfSTPAELakhakasRAK 123
Cdd:PRK09029 25 NDEVLTWQ--QLCARidQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNP-QLPQPL-------LEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 124 LLITQACyyekvkDFAresdvkvmcvdSAPDGCLHFSELT---QADENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTH 200
Cdd:PRK09029 95 LLPSLTL------DFA-----------LVLEGENTFSALTslhLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 201 KGLITS---VAQQVDgdnpnlyFHSEDVILCVLPMFHIYALnSIMLCGLRVGApILIMPkfEIGSLLGLIEKykVSIAPV 277
Cdd:PRK09029 158 QAHLASaegVLSLMP-------FTAQDSWLLSLPLFHVSGQ-GIVWRWLYAGA-TLVVR--DKQPLEQALAG--CTHASL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 278 VPPVMMSIAKSPdldkHDLSSLRMIKSGGAPLGKELedTVRAKFPQARLGQGYGMTEAGPVLamclaFAKEPfDIKPGAc 357
Cdd:PRK09029 225 VPTQLWRLLDNR----SEPLSLKAVLLGGAAIPVEL--TEQAEQQGIRCWCGYGLTEMASTV-----CAKRA-DGLAGV- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 358 GTVVRNAEMKIVDpetgaslprnqpGEICIRGDQIMKGYLNDPEATSRTiDKEGWLHTGDIGYIDDDdELFIVDRLKELI 437
Cdd:PRK09029 292 GSPLPGREVKLVD------------GEIWLRGASLALGYWRQGQLVPLV-NDEGWFATRDRGEWQNG-ELTILGRLDNLF 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 438 KYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAfVVKSEkSQATEDEIKQYISKQVIFYKRIKRVFFIEAIP 517
Cdd:PRK09029 358 FSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVA-VVESD-SEAAVVNLAEWLQDKLARFQQPVAYYLLPPEL 435
|
490
....*....|....*..
gi 306440447 518 KAPSGKILRKNLKEKLA 534
Cdd:PRK09029 436 KNGGIKISRQALKEWVA 452
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
35-476 |
3.90e-26 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 112.28 E-value: 3.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 35 HSSKPCLINGanGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELA 114
Cdd:PRK08279 50 HPDRPALLFE--DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 115 kHA-KASRAKLLITQA-CY--YEKVKDFAREsDVKVMCVDSA----PDGCLHFSEL--TQADENEAPQVDISPDDVVALP 184
Cdd:PRK08279 128 -HSlNLVDAKHLIVGEeLVeaFEEARADLAR-PPRLWVAGGDtlddPEGYEDLAAAaaGAPTTNPASRSGVTAKDTAFYI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 185 YSSGTTGLPKGVMLTHKGLITSVAQQVDGDNPNlyfhSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLL 264
Cdd:PRK08279 206 YTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLT----PDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFW 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 265 GLIEKYKVSIAPVV----------PPvmmsiakSPDLDKHdlsSLRMIKsgGAPLGKELEDTVRAKFPQARLGQGYGMTE 334
Cdd:PRK08279 282 DDVRRYRATAFQYIgelcryllnqPP-------KPTDRDH---RLRLMI--GNGLRPDIWDEFQQRFGIPRILEFYAASE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 335 AGpvlamcLAFAKepFDIKPGACGTV----VRNAEMKIVDPETGASL----------PRNQPGEIC--IRGDQIMKGYlN 398
Cdd:PRK08279 350 GN------VGFIN--VFNFDGTVGRVplwlAHPYAIVKYDVDTGEPVrdadgrcikvKPGEVGLLIgrITDRGPFDGY-T 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 399 DPEATSRTI--D--KEG--WLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLkdeda 472
Cdd:PRK08279 421 DPEASEKKIlrDvfKKGdaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGV----- 495
|
....
gi 306440447 473 gEVP 476
Cdd:PRK08279 496 -EVP 498
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
16-527 |
4.97e-26 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 112.14 E-value: 4.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 16 IYIPKNLPLHSYVLENLSNHSSKPclingangdVYTYAD---------VELTARRVASGLNKIG--IQQ----GDVIMLF 80
Cdd:PRK12476 28 IALPPGTTLISLIERNIANVGDTV---------AYRYLDhshsaagcaVELTWTQLGVRLRAVGarLQQvagpGDRVAIL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 81 LPSSPEFVLAFLGASHRGAIitaANPFSTPaELAKHA-------KASRAKLLITQACYYEKVKDFARE----SDVKVMCV 149
Cdd:PRK12476 99 APQGIDYVAGFFAAIKAGTI---AVPLFAP-ELPGHAerldtalRDAEPTVVLTTTAAAEAVEGFLRNlprlRRPRVIAI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 150 DSAPDgclhfselTQADENEAPQVDIspDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQ---QVDGDNPNLyfHSedvi 226
Cdd:PRK12476 175 DAIPD--------SAGESFVPVELDT--DDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQmilSIDLLDRNT--HG---- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 227 LCVLPMFHIYALNSIMLCGLRVGAPILIMP------------KFEIGSLLGLIekykVSIAPV----------VPPvmms 284
Cdd:PRK12476 239 VSWLPLYHDMGLSMIGFPAVYGGHSTLMSPtafvrrpqrwikALSEGSRTGRV----VTAAPNfayewaaqrgLPA---- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 285 iakspDLDKHDLSSLRMIkSGGAPLGKELEDTVRAKF-----PQARLGQGYGMTEAGPVLAMcLAFAKEP----FD---- 351
Cdd:PRK12476 311 -----EGDDIDLSNVVLI-IGSEPVSIDAVTTFNKAFapyglPRTAFKPSYGIAEATLFVAT-IAPDAEPsvvyLDreql 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 352 -------IKPGA--------CGTVVRNAEMKIVDPETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTI--------- 407
Cdd:PRK12476 384 gagravrVAADApnavahvsCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrla 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 408 ---------DKEGWLHTgDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVA 478
Cdd:PRK12476 464 egshadgaaDDGTWLRT-GDLGVYLDGELYITGRIADLIVIDGRNHYPQDIEATVAEASPMVRRGYVTAFTVPAEDNERL 542
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 306440447 479 FVVKSEKSQATEDE-------IKQYISKQviFYKRIKRVFFIEA--IPKAPSGKILRK 527
Cdd:PRK12476 543 VIVAERAAGTSRADpapaidaIRAAVSRR--HGLAVADVRLVPAgaIPRTTSGKLARR 598
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
51-534 |
1.41e-25 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 111.60 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVeLTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANpFST-PAELAKHAKASRAKLLITQA 129
Cdd:PRK06814 660 TYRKL-LTGAFVLGRKLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMIN-FSAgIANILSACKAAQVKTVLTSR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 130 CYYEKVK----DFARESDVKVMCVDSAPDGclhfseLTQADENEA------PQVDI---SPDDVVALPYSSGTTGLPKGV 196
Cdd:PRK06814 738 AFIEKARlgplIEALEFGIRIIYLEDVRAQ------IGLADKIKGllagrfPLVYFcnrDPDDPAVILFTSGSEGTPKGV 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 197 MLTHKGLITSVAQ---QVDgdnpnlyFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPkfeigSLLglieKYKVs 273
Cdd:PRK06814 812 VLSHRNLLANRAQvaaRID-------FSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYP-----SPL----HYRI- 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 274 iapvVPPV---------------MMSIAKSPDldKHDLSSLRMIKSGGAPLGKELEDTVRAKFpQARLGQGYGMTEAGPV 338
Cdd:PRK06814 875 ----IPELiydtnatilfgtdtfLNGYARYAH--PYDFRSLRYVFAGAEKVKEETRQTWMEKF-GIRILEGYGVTETAPV 947
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 339 LAMclafaKEPFDIKPGACGTVVRNAEMKiVDPETGAslprNQPGEICIRGDQIMKGYLnDPEAtSRTID--KEGWLHTG 416
Cdd:PRK06814 948 IAL-----NTPMHNKAGTVGRLLPGIEYR-LEPVPGI----DEGGRLFVRGPNVMLGYL-RAEN-PGVLEppADGWYDTG 1015
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 417 DIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFvvkSEKSQATEDEIKQY 496
Cdd:PRK06814 1016 DIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERIILL---TTASDATRAAFLAH 1092
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 306440447 497 ISKQVIFYKRI-KRVFFIEAIPKAPSGKI----LRKNLKEKLA 534
Cdd:PRK06814 1093 AKAAGASELMVpAEIITIDEIPLLGTGKIdyvaVTKLAEEAAA 1135
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
47-473 |
3.04e-25 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 108.60 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 47 GDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLI 126
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 127 TQACYYekvkdfaresdvkvmcvdsapdgclhfseltqadeneapqvdispddvvalPYSSGTTGLPKGVMLTHKGLI-- 204
Cdd:cd05940 81 VDAALY---------------------------------------------------IYTSGTTGLPKAAIISHRRAWrg 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 205 TSVAQQVDGDNPnlyfhsEDVILCVLPMFHIYALnsiMLC---GLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPV 281
Cdd:cd05940 110 GAFFAGSGGALP------SDVLYTCLPLYHSTAL---IVGwsaCLASGATLVIRKKFSASNFWDDIRKYQATIFQYIGEL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 282 MMSIAKSPDLDKHDLSSLRMIKSGGapLGKELEDTVRAKFPQARLGQGYGMTEAGpvlamclaFAKEPFDIKPGACG--- 358
Cdd:cd05940 181 CRYLLNQPPKPTERKHKVRMIFGNG--LRPDIWEEFKERFGVPRIAEFYAATEGN--------SGFINFFGKPGAIGrnp 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 359 -TVVRNAEMKIV--DPETGASL----------PRNQPGE-IC-IRGDQIMKGYLnDPEATSRTI------DKEGWLHTGD 417
Cdd:cd05940 251 sLLRKVAPLALVkyDLESGEPIrdaegrcikvPRGEPGLlISrINPLEPFDGYT-DPAATEKKIlrdvfkKGDAWFNTGD 329
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 306440447 418 IGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAG 473
Cdd:cd05940 330 LMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTD 385
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
51-411 |
5.40e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 108.98 E-value: 5.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIitaANPFSTPAEL--AKHAK----ASRAK- 123
Cdd:PRK12582 82 TYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVP---AAPVSPAYSLmsHDHAKlkhlFDLVKp 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 124 --LLITQACYYEKVKDFARESDVKVMCVDSAPDG--CLHFSEL---TQADENEAPQVDISPDDVVALPYSSGTTGLPKGV 196
Cdd:PRK12582 159 rvVFAQSGAPFARALAALDLLDVTVVHVTGPGEGiaSIAFADLaatPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 197 MLTHkGLITSVAQQVDGDNPNLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILI-----MPkfeigsllGLIEKYK 271
Cdd:PRK12582 239 INTQ-RMMCANIAMQEQLRPREPDPPPPVSLDWMPWNHTMGGNANFNGLLWGGGTLYIddgkpLP--------GMFEETI 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 272 VSIAPVVPPVMMS-----------IAKSPDLDKHDLSSLRMIKSGGAPLGKELED-----TVRAKFPQARLGQGYGMTEA 335
Cdd:PRK12582 310 RNLREISPTVYGNvpagyamlaeaMEKDDALRRSFFKNLRLMAYGGATLSDDLYErmqalAVRTTGHRIPFYTGYGATET 389
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 306440447 336 GPVlAMCLAFAKEpfdiKPGACGTVVRNAEMKIVdpetgaslPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEG 411
Cdd:PRK12582 390 APT-TTGTHWDTE----RVGLIGLPLPGVELKLA--------PVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEG 452
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
46-529 |
5.22e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 107.35 E-value: 5.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 46 NGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLL 125
Cdd:PRK12316 3079 GEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLL 3158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 126 ITQACYyekvkDFARESDVKVMCVDSAPDGClhfseltqadENEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLiT 205
Cdd:PRK12316 3159 LSQSHL-----RLPLAQGVQVLDLDRGDENY----------AEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSAL-S 3222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 206 SVAQQVDGdnpnLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPVMMSI 285
Cdd:PRK12316 3223 NHLCWMQQ----AYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSML 3298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 286 AKS-PDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPqarLGQGYGMTEAgPVLAMCLAFAKEPFDIKPgaCGTVVRNA 364
Cdd:PRK12316 3299 QAFlEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEA-TITVTHWQCVEEGKDAVP--IGRPIANR 3372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 365 EMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTI------DKEGWLHTGDIGYIDDDDELFIVDRLKELIK 438
Cdd:PRK12316 3373 ACYILD-GSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFvpdpfvPGERLYRTGDLARYRADGVIEYIGRVDHQVK 3451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 439 YKGFQVAPAELEALLIAHPEISDAAVVglkdEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPK 518
Cdd:PRK12316 3452 IRGFRIELGEIEARLLEHPWVREAVVL----AVDGRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPL 3527
|
490
....*....|.
gi 306440447 519 APSGKILRKNL 529
Cdd:PRK12316 3528 TPNGKLDRKAL 3538
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
25-529 |
5.85e-24 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 104.56 E-value: 5.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 25 HSYVLENLSNHSSKPCLINgaNGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAA 104
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVD--RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 105 NPFSTPAELAKHAKASRAKLLITQacyyekvkdfaresdvkvmcvdsapdgclhfseltqadeneapqvdisPDDVVALP 184
Cdd:cd17645 79 DPDYPGERIAYMLADSSAKILLTN------------------------------------------------PDDLAYVI 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 185 YSSGTTGLPKGVMLTHKGLIT---------SVAQQvdgDNPNLY--FHSEDVILCVLPmfHIYAlnsimlcglrvGAPIL 253
Cdd:cd17645 111 YTSGSTGLPKGVMIEHHNLVNlcewhrpyfGVTPA---DKSLVYasFSFDASAWEIFP--HLTA-----------GAALH 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 254 IMP---KFEIGSLLGLIEKYKVSIAPVVPPVMMSIAKspdLDKHdlsSLRMIKSGGAPLGkeledtvRAKFPQARLGQGY 330
Cdd:cd17645 175 VVPserRLDLDALNDYFNQEGITISFLPTGAAEQFMQ---LDNQ---SLRVLLTGGDKLK-------KIERKGYKLVNNY 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 331 GMTEAGPVLAMclafakepFDIKPG----ACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATS-- 404
Cdd:cd17645 242 GPTENTVVATS--------FEIDKPyaniPIGKPIDNTRVYILD-EALQLQPIGVAGELCIAGEGLARGYLNRPELTAek 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 405 -------------RTIDKEGWLhtgdigyidDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDED 471
Cdd:cd17645 313 fivhpfvpgermyRTGDLAKFL---------PDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDAD 383
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 306440447 472 AGEVPVAFVVKseKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNL 529
Cdd:cd17645 384 GRKYLVAYVTA--PEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
174-534 |
5.67e-23 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 102.55 E-value: 5.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 174 DISPDDVVALPYSSGTTGLPKGVMLTHKGLITSvAQQVDGDNPNLYFHSEDVILCVlPMFHIYALnSIMLCGLRVGAPiL 253
Cdd:PRK05620 177 ELDETTAAAICYSTGTTGAPKGVVYSHRSLYLQ-SLSLRTTDSLAVTHGESFLCCV-PIYHVLSW-GVPLAAFMSGTP-L 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 254 IMPKFEIG--SLLGLIEKYKVSIAPVVPPVMMSI----AKSPDldkhDLSSLRMIKSGGAPLGKELEDTVRAKFpQARLG 327
Cdd:PRK05620 253 VFPGPDLSapTLAKIIATAMPRVAHGVPTLWIQLmvhyLKNPP----ERMSLQEIYVGGSAVPPILIKAWEERY-GVDVV 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 328 QGYGMTEAGPVLAMclafAKEPfdikPGACGTVVRN-----------AEMKIV-DPETGASLPRNQpGEICIRGDQIMKG 395
Cdd:PRK05620 328 HVWGMTETSPVGTV----ARPP----SGVSGEARWAyrvsqgrfpasLEYRIVnDGQVMESTDRNE-GEIQVRGNWVTAS 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 396 YLNDPE-----ATSRTIDKE-----------GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEI 459
Cdd:PRK05620 399 YYHSPTeegggAASTFRGEDvedandrftadGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEV 478
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 306440447 460 SDAAVVGLKDEDAGEVPVAFVVKS---EKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEKLA 534
Cdd:PRK05620 479 VECAVIGYPDDKWGERPLAVTVLApgiEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHLA 556
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
49-534 |
6.07e-23 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 102.91 E-value: 6.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 49 VYTYAdvELTAR--RVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAI---ITAAnpFStPAELAKHAKASRAK 123
Cdd:PRK00174 98 KITYR--ELHREvcRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVhsvVFGG--FS-AEALADRIIDAGAK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 124 LLITqacyyekvKDFARESDVKVMC---VDSAPDGCLHFS-----ELTQADENEAPQVDISPDDVVALP----------- 184
Cdd:PRK00174 173 LVIT--------ADEGVRGGKPIPLkanVDEALANCPSVEkvivvRRTGGDVDWVEGRDLWWHELVAGAsdecepepmda 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 185 -------YSSGTTGLPKGVMLTHKGLITSVA---QQV----DGDnpnLYFHSEDV--ILCvlpmfHIYalnsiMLCG-LR 247
Cdd:PRK00174 245 edplfilYTSGSTGKPKGVLHTTGGYLVYAAmtmKYVfdykDGD---VYWCTADVgwVTG-----HSY-----IVYGpLA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 248 VGAPILImpkFE-------IGSLLGLIEKYKVSI---APVVPPVMMSIAKSPdLDKHDLSSLRMIKSGGAP--------- 308
Cdd:PRK00174 312 NGATTLM---FEgvpnypdPGRFWEVIDKHKVTIfytAPTAIRALMKEGDEH-PKKYDLSSLRLLGSVGEPinpeawewy 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 309 ---LGKE---LEDTvrakfpqarlgqgYGMTEAGPVLAMCLAFAkepFDIKPGACGTVVRNAEMKIVDpETGASLPRNQP 382
Cdd:PRK00174 388 ykvVGGErcpIVDT-------------WWQTETGGIMITPLPGA---TPLKPGSATRPLPGIQPAVVD-EEGNPLEGGEG 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 383 GEICIR----GdqIMKGYLNDPEATSRT----------------IDKEG--WlhtgdigyiddddelfIVDRLKELIKYK 440
Cdd:PRK00174 451 GNLVIKdpwpG--MMRTIYGDHERFVKTyfstfkgmyftgdgarRDEDGyyW----------------ITGRVDDVLNVS 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 441 GFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVV---KSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIP 517
Cdd:PRK00174 513 GHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTlkgGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLP 592
|
570
....*....|....*..
gi 306440447 518 KAPSGKILRKNLKeKLA 534
Cdd:PRK00174 593 KTRSGKIMRRILR-KIA 608
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
51-531 |
6.95e-23 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 102.67 E-value: 6.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQAC 130
Cdd:PLN02654 122 TYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 131 YYEKVKDFARESDVKVMCVDSAPDG-----CLHF---SELTQADENEAPQVDISPDDVVA------------------LP 184
Cdd:PLN02654 202 VKRGPKTINLKDIVDAALDESAKNGvsvgiCLTYenqLAMKREDTKWQEGRDVWWQDVVPnyptkcevewvdaedplfLL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 185 YSSGTTGLPKGVMLTHKGLI----TSVAQQVDGDNPNLYFHSEDvilCVLPMFHIYALNSIMLCGLRV----GAPILIMP 256
Cdd:PLN02654 282 YTSGSTGKPKGVLHTTGGYMvytaTTFKYAFDYKPTDVYWCTAD---CGWITGHSYVTYGPMLNGATVlvfeGAPNYPDS 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 257 kfeiGSLLGLIEKYKVSIAPVVPPVMMSIAKSPD--LDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQAR--LGQGYGM 332
Cdd:PLN02654 359 ----GRCWDIVDKYKVTIFYTAPTLVRSLMRDGDeyVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGDSRcpISDTWWQ 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 333 TEAGPVLAMCLAFAkepFDIKPGACGTVVRNAEMKIVDpETGASLPRNQPGEICIR-----------GD---------QI 392
Cdd:PLN02654 435 TETGGFMITPLPGA---WPQKPGSATFPFFGVQPVIVD-EKGKEIEGECSGYLCVKkswpgafrtlyGDheryettyfKP 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 393 MKGYLNDPEATSRtiDKEG--WLhtgdigyiddddelfiVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDE 470
Cdd:PLN02654 511 FAGYYFSGDGCSR--DKDGyyWL----------------TGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHE 572
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 306440447 471 DAGEVPVAFVVKSEKSQATEDEIKQYIS---KQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKE 531
Cdd:PLN02654 573 VKGQGIYAFVTLVEGVPYSEELRKSLILtvrNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 636
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
51-457 |
2.03e-22 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 101.35 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGaiITAANPFSTPAE--LAKHAKASRAKLLItq 128
Cdd:PLN02387 108 TYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQN--ITVVTIYASLGEeaLCHSLNETEVTTVI-- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 129 aCYYEKVKDFARESD----VK-VMCVD--------SAPDGC----LHFSELTQ-ADENEAPQVDISPDDVVALPYSSGTT 190
Cdd:PLN02387 184 -CDSKQLKKLIDISSqletVKrVIYMDdegvdsdsSLSGSSnwtvSSFSEVEKlGKENPVDPDLPSPNDIAVIMYTSGST 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 191 GLPKGVMLTHKGLITSVAQqVDGDNPNLyfHSEDVILCVLPMFHIYAL--NSIMLCglrVGAPIlimpkfEIGSLLGL-- 266
Cdd:PLN02387 263 GLPKGVMMTHGNIVATVAG-VMTVVPKL--GKNDVYLAYLPLAHILELaaESVMAA---VGAAI------GYGSPLTLtd 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 267 ----IEKYKVSIAPVVPPVMMSiAKSPDLDK-------------------HDLS-------------------------- 297
Cdd:PLN02387 331 tsnkIKKGTKGDASALKPTLMT-AVPAILDRvrdgvrkkvdakgglakklFDIAykrrlaaiegswfgawglekllwdal 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 298 -----------SLRMIKSGGAPLGKeleDTVRakFPQ----ARLGQGYGMTE--AGPvlamclAFAkEPFDIKPGACGTV 360
Cdd:PLN02387 410 vfkkiravlggRIRFMLSGGAPLSG---DTQR--FINiclgAPIGQGYGLTEtcAGA------TFS-EWDDTSVGRVGPP 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 361 VRNAEMKIVDPETGASLPRNQP---GEICIRGDQIMKGYLNDPEATSRT--IDKEG--WLHTGDIGYIDDDDELFIVDRL 433
Cdd:PLN02387 478 LPCCYVKLVSWEEGGYLISDKPmprGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRK 557
|
490 500
....*....|....*....|....*
gi 306440447 434 KELIKYK-GFQVAPAELEALLIAHP 457
Cdd:PLN02387 558 KDIVKLQhGEYVSLGKVEAALSVSP 582
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
51-527 |
2.10e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 100.96 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGiQQGDVIMLFLPSSPEFVLAFLGASHRGAIitaANPFSTPAElAKHAKASRAKL------ 124
Cdd:PRK07769 57 TWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRI---AVPLFDPAE-PGHVGRLHAVLddctps 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 125 -LITQACYYEKVKDFARESDVK----VMCVDSAPDgclhfseltQADENEAPqVDISPDDVVALPYSSGTTGLPKGVMLT 199
Cdd:PRK07769 132 aILTTTDSAEGVRKFFRARPAKerprVIAVDAVPD---------EVGATWVP-PEANEDTIAYLQYTSGSTRIPAGVQIT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 200 HKGLITSVAQQVDGdnpnLYFHSEDVILCVLPMFHIYALNSIMLCGLrVGAPILIM--------PKFEIgSLLGLIEKYK 271
Cdd:PRK07769 202 HLNLPTNVLQVIDA----LEGQEGDRGVSWLPFFHDMGLITVLLPAL-LGHYITFMspaafvrrPGRWI-RELARKPGGT 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 272 VSIAPVVPPVMMSIAKSPDLDKH-----DLSSLRMIKSGGAPLGKEledTVRaKF---------PQARLGQGYGMTEAgp 337
Cdd:PRK07769 276 GGTFSAAPNFAFEHAAARGLPKDgepplDLSNVKGLLNGSEPVSPA---SMR-KFneafapyglPPTAIKPSYGMAEA-- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 338 vlamCLAFAKEPFDIKPG----------------------------ACGTVVRNAEMKIVDPETGASLPRNQPGEICIRG 389
Cdd:PRK07769 350 ----TLFVSTTPMDEEPTviyvdrdelnagrfvevpadapnavaqvSAGKVGVSEWAVIVDPETASELPDGQIGEIWLHG 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 390 DQIMKGYLNDPEATSRTI-----------------DKEGWLHTgDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELE-- 450
Cdd:PRK07769 426 NNIGTGYWGKPEETAATFqnilksrlseshaegapDDALWVRT-GDYGVYFDGELYITGRVKDLVIIDGRNHYPQDLEyt 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 451 ------AL---LIAH---------PEISDAAVVGLK--DEDAGEvpvAFVVKSEKS--------QATEDEIKQYISKQVI 502
Cdd:PRK07769 505 aqeatkALrtgYVAAfsvpanqlpQVVFDDSHAGLKfdPEDTSE---QLVIVAERApgahkldpQPIADDIRAAIAVRHG 581
|
570 580
....*....|....*....|....*
gi 306440447 503 FYKRIKRVFFIEAIPKAPSGKILRK 527
Cdd:PRK07769 582 VTVRDVLLVPAGSIPRTSSGKIARR 606
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
44-415 |
4.85e-22 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 99.95 E-value: 4.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 44 GANGD--VYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANP-FSTPAelAKHAK-A 119
Cdd:PRK08180 62 GADGGwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPaYSLVS--QDFGKlR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 120 SRAKLLITQACYYEKVKDFAR------ESDVKVMCVDSAPDG--CLHFSELtqADENEAPQVD-----ISPDDVVALPYS 186
Cdd:PRK08180 140 HVLELLTPGLVFADDGAAFARalaavvPADVEVVAVRGAVPGraATPFAAL--LATPPTAAVDaahaaVGPDTIAKFLFT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 187 SGTTGLPKGVMLTHkGLITSVAQQVDGDNPnlYFHSED-VILCVLPMFHIYALNSIMLCGLRVGAPILI-----MPkfei 260
Cdd:PRK08180 218 SGSTGLPKAVINTH-RMLCANQQMLAQTFP--FLAEEPpVLVDWLPWNHTFGGNHNLGIVLYNGGTLYIddgkpTP---- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 261 gsllGLIEKyKV----SIAPV----VPPVMMSIA----KSPDLDKHDLSSLRMIKSGGAPLGKELED-----TVRAKFPQ 323
Cdd:PRK08180 291 ----GGFDE-TLrnlrEISPTvyfnVPKGWEMLVpaleRDAALRRRFFSRLKLLFYAGAALSQDVWDrldrvAEATCGER 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 324 ARLGQGYGMTEAGPvlaMCLaFAKEPFDiKPGACGTVVRNAEMKIVdpetgaslPRNQPGEICIRGDQIMKGYLNDPEAT 403
Cdd:PRK08180 366 IRMMTGLGMTETAP---SAT-FTTGPLS-RAGNIGLPAPGCEVKLV--------PVGGKLEVRVKGPNVTPGYWRAPELT 432
|
410
....*....|..
gi 306440447 404 SRTIDKEGWLHT 415
Cdd:PRK08180 433 AEAFDEEGYYRS 444
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
51-411 |
6.21e-22 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 99.20 E-value: 6.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEF---VLAFLGAshrGAIITAANP----------F--STPAELAK 115
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFfalTFALFKA---GAVPVLVDPgmgiknlkqcLaeAQPDAFIG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 116 HAKASRAKLLitqacyyekvkdFAR-ESDVK-VMCVDSAPDGCLHF-SELTQADENEAPQ-VDISPDDVVALPYSSGTTG 191
Cdd:PRK09274 120 IPKAHLARRL------------FGWgKPSVRrLVTVGGRLLWGGTTlATLLRDGAAAPFPmADLAPDDMAAILFTSGSTG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 192 LPKGVMLTHKglitSVAQQVD------GDNPNlyfhseDVILCVLPMFHIYALnsimLCGLRV-------GAPILIMPKF 258
Cdd:PRK09274 188 TPKGVVYTHG----MFEAQIEalredyGIEPG------EIDLPTFPLFALFGP----ALGMTSvipdmdpTRPATVDPAK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 259 eigsLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQ-ARLGQGYGMTEAGP 337
Cdd:PRK09274 254 ----LFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLPPdAEILTPYGATEALP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 338 VLAM----CLAFAKEPFDIKPGAC-GTVVRNAEMKIVDPETGA--------SLPRNQPGEICIRGDQIMKGYLNDPEAT- 403
Cdd:PRK09274 330 ISSIesreILFATRAATDNGAGICvGRPVDGVEVRIIAISDAPipewddalRLATGEIGEIVVAGPMVTRSYYNRPEATr 409
|
....*....
gi 306440447 404 -SRTIDKEG 411
Cdd:PRK09274 410 lAKIPDGQG 418
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
176-524 |
6.25e-22 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 98.63 E-value: 6.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 176 SPDDVVALPYSSGTTGLPKGVMLTHKG---LITSVAQQVDGDNpnlyfHSEDVILcvlpMFHIYALN-SI--MLCGLRVG 249
Cdd:cd17648 92 NSTDLAYAIYTSGTTGKPKGVLVEHGSvvnLRTSLSERYFGRD-----NGDEAVL----FFSNYVFDfFVeqMTLALLNG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 250 APILIMP---KFEIGSLLGLIEKYKVSIAPVVPPVMMSIakspDLDKhdLSSLRMIKSGGAPLGKELEDTVRAKFPqARL 326
Cdd:cd17648 163 QKLVVPPdemRFDPDRFYAYINREKVTYLSGTPSVLQQY----DLAR--LPHLKRVDAAGEEFTAPVFEKLRSRFA-GLI 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 327 GQGYGMTEAGPVLAMCLAFAKEPFDikpGACGTVVRNAEMKIVDPETgASLPRNQPGEICIRGDQIMKGYLNDPEATS-- 404
Cdd:cd17648 236 INAYGPTETTVTNHKRFFPGDQRFD---KSLGRPVRNTKCYVLNDAM-KRVPVGAVGELYLGGDGVARGYLNRPELTAer 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 405 ---------------------RTIDKEGWLHTgdigyidddDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAA 463
Cdd:cd17648 312 flpnpfqteqerargrnarlyKTGDLVRWLPS---------GELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECA 382
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 306440447 464 VVGLKDEDAGEVP-----VAFVVkSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKI 524
Cdd:cd17648 383 VVAKEDASQAQSRiqkylVGYYL-PEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
51-412 |
1.15e-21 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 98.66 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANP-FSTPAelAKHAKASRA-KLLITQ 128
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPaYSLMS--QDLAKLKHLfELLKPG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 129 ACYYEKVKDFAR------ESDVKVMCVDSAPDG--CLHFSEL--TQADENEAPQVD-ISPDDVVALPYSSGTTGLPKGVM 197
Cdd:cd05921 105 LVFAQDAAPFARalaaifPLGTPLVVSRNAVAGrgAISFAELaaTPPTAAVDAAFAaVGPDTVAKFLFTSGSTGLPKAVI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 198 LTHkGLITSVAQQVDGDNPnlYFHSED-VILCVLPMFHIYALNSIMLCGLRVGAPILI-----MPkfeigsllGLIEKYK 271
Cdd:cd05921 185 NTQ-RMLCANQAMLEQTYP--FFGEEPpVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIddgkpMP--------GGFEETL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 272 VSIAPVVPPVMMSIAKS-----PDLDKHD------LSSLRMIKSGGAPLGKELED-----TVRAKFPQARLGQGYGMTEA 335
Cdd:cd05921 254 RNLREISPTVYFNVPAGwemlvAALEKDEalrrrfFKRLKLMFYAGAGLSQDVWDrlqalAVATVGERIPMMAGLGATET 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 306440447 336 GPVLAMClafaKEPFDiKPGACGTVVRNAEMKIVdpetgaslPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGW 412
Cdd:cd05921 334 APTATFT----HWPTE-RSGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF 397
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
46-499 |
1.93e-21 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 97.12 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 46 NGDVYTYADVELTARRVASGLNKI-GIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKL 124
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 125 LItqacyyekvkdfaresdvkvmcvdsapdgclhfseltqadeneapqvdISPDDVVALPYSSGTTGLPKGVmlthkglI 204
Cdd:cd05937 82 VI------------------------------------------------VDPDDPAILIYTSGTTGLPKAA-------A 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 205 TSVAQQVDGDNP---NLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPV 281
Cdd:cd05937 107 ISWRRTLVTSNLlshDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWKDVRDSGATIIQYVGEL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 282 ---MMSIAKSPDLDKHdlsSLRMIKSGGapLGKELEDTVRAKFPQARLGQGYGMTEAgpVLAMcLAFAKEPFDIkpGACG 358
Cdd:cd05937 187 cryLLSTPPSPYDRDH---KVRVAWGNG--LRPDIWERFRERFNVPEIGEFYAATEG--VFAL-TNHNVGDFGA--GAIG 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 359 --------------TVVR---NAEMKIVDPETG--ASLPRNQPGEICIR----GDQIMKGYLNDPEATS----RTIDKEG 411
Cdd:cd05937 257 hhglirrwkfenqvVLVKmdpETDDPIRDPKTGfcVRAPVGEPGEMLGRvpfkNREAFQGYLHNEDATEsklvRDVFRKG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 412 --WLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLK-DEDAGEVPVAFVVKSEKSQA 488
Cdd:cd05937 337 diYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKvPGHDGRAGCAAITLEESSAV 416
|
490
....*....|.
gi 306440447 489 TEDEIKQYISK 499
Cdd:cd05937 417 PTEFTKSLLAS 427
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
119-466 |
2.40e-21 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 97.96 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 119 ASRAKLLITQACYYEKVKDFARESDVKVMCVDSApdgcLHFSELTQADENeAPQvdisPDDVVALPYSSGTTGLPKGVML 198
Cdd:PLN02430 170 AKRLKAIVSFTSVTEEESDKASQIGVKTYSWIDF----LHMGKENPSETN-PPK----PLDICTIMYTSGTSGDPKGVVL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 199 THKGLITSVaQQVDgdnpnLYFH-------SEDVILCVLPMFHIYAlNSIMLCGLRVGAPIlimpKFEIGSLLGL---IE 268
Cdd:PLN02430 241 THEAVATFV-RGVD-----LFMEqfedkmtHDDVYLSFLPLAHILD-RMIEEYFFRKGASV----GYYHGDLNALrddLM 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 269 KYKVSIAPVVPPVMMSIAK---------SP-------DLDKHDLS-----------------------------SLRMIK 303
Cdd:PLN02430 310 ELKPTLLAGVPRVFERIHEgiqkalqelNPrrrlifnALYKYKLAwmnrgyshkkaspmadflafrkvkaklggRLRLLI 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 304 SGGAPLGKELEDTVRAKfPQARLGQGYGMTEA-GPVlamCLAFAKEPFDIkpGACGTVVRNAEMKIVD-PETGAS-LPRN 380
Cdd:PLN02430 390 SGGAPLSTEIEEFLRVT-SCAFVVQGYGLTETlGPT---TLGFPDEMCML--GTVGAPAVYNELRLEEvPEMGYDpLGEP 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 381 QPGEICIRGDQIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEALLIAHPEI 459
Cdd:PLN02430 464 PRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLsQGEYVALEYLENVYGQNPIV 542
|
....*..
gi 306440447 460 SDAAVVG 466
Cdd:PLN02430 543 EDIWVYG 549
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
47-532 |
4.86e-21 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 96.12 E-value: 4.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 47 GDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRG-AIITAAnpFSTPAE-LAKHAKASRAKL 124
Cdd:PRK04813 25 GEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGhAYIPVD--VSSPAErIEMIIEVAKPSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 125 LITqacyyekVKDFARE-SDVKVMCVDSAPDgclhfSELTQADENEAPQVdiSPDDVVALPYSSGTTGLPKGVMLTHKGL 203
Cdd:PRK04813 103 IIA-------TEELPLEiLGIPVITLDELKD-----IFATGNPYDFDHAV--KGDDNYYIIFTSGTTGKPKGVQISHDNL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 204 ItSVAQQVDGDNP---NLYF-----HSEDvilcvLPMFHIY-ALNSimlcglrvGAPILIMPKFEI---GSLLGLIEKYK 271
Cdd:PRK04813 169 V-SFTNWMLEDFAlpeGPQFlnqapYSFD-----LSVMDLYpTLAS--------GGTLVALPKDMTanfKQLFETLPQLP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 272 VSIApVVPPVMMSIA-KSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEA----------GPVLA 340
Cdd:PRK04813 235 INVW-VSTPSFADMClLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEAtvavtsieitDEMLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 341 MC----LAFAKEPFDIKpgacgtvvrnaemkiVDPETGASLPRNQPGEICIRGDQIMKGYLNDPEATSR---TIDKEGWL 413
Cdd:PRK04813 314 QYkrlpIGYAKPDSPLL---------------IIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEaffTFDGQPAY 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 414 HTGDIGYIDDDDeLFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATE--- 490
Cdd:PRK04813 379 HTGDAGYLEDGL-LFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREfel 457
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 306440447 491 -DEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEK 532
Cdd:PRK04813 458 tKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKALIEE 500
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
448-523 |
1.32e-20 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 85.67 E-value: 1.32e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 306440447 448 ELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGK 523
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
30-535 |
6.63e-20 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 93.10 E-value: 6.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 30 ENLSNHSS---KPCLINGANG--DVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAA 104
Cdd:cd05943 74 ENLLRHADaddPAAIYAAEDGerTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSC 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 105 NP-FSTPAELAKHAKAsRAKLLITQACYYEKVKDFARESDVKVMcVDSAPDG--CLHFSELTQADENEAPQVD--ISPDD 179
Cdd:cd05943 154 SPdFGVPGVLDRFGQI-EPKVLFAVDAYTYNGKRHDVREKVAEL-VKGLPSLlaVVVVPYTVAAGQPDLSKIAkaLTLED 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 180 VVA-----------LP--------YSSGTTGLPKGVMLTHKGL----ITSVAQQVD-GDNPNLYFHSEdvilCVLPMFHi 235
Cdd:cd05943 232 FLAtgaagelefepLPfdhplyilYSSGTTGLPKCIVHGAGGTllqhLKEHILHCDlRPGDRLFYYTT----CGWMMWN- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 236 yalnsIMLCGLRVGAPILIM------PKFEIgsLLGLIEKYKVSIAPVVPPVMMSIAKS---PDLDkHDLSSLRMIKSGG 306
Cdd:cd05943 307 -----WLVSGLAVGATIVLYdgspfyPDTNA--LWDLADEEGITVFGTSAKYLDALEKAglkPAET-HDLSSLRTILSTG 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 307 APLGKELEDTVRAKF-PQARLGQGYGMTEagpvLAMCLAFAKEPFDIKPGACGTVVRNAEMKIVDPEtGASLpRNQPGE- 384
Cdd:cd05943 379 SPLKPESFDYVYDHIkPDVLLASISGGTD----IISCFVGGNPLLPVYRGEIQCRGLGMAVEAFDEE-GKPV-WGEKGEl 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 385 ICIRGDQIMK-GYLNDPEAtSR-------------------TIDKEGwlhtgdigyiddddELFIVDRLKELIKYKGFQV 444
Cdd:cd05943 453 VCTKPFPSMPvGFWNDPDG-SRyraayfakypgvwahgdwiEITPRG--------------GVVILGRSDGTLNPGGVRI 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 445 APAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKSQATEDeikqyiskqviFYKRIK--------------RV 510
Cdd:cd05943 518 GTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDE-----------LRKRIRstirsalsprhvpaKI 586
|
570 580
....*....|....*....|....*
gi 306440447 511 FFIEAIPKAPSGKILRKNLKEKLAG 535
Cdd:cd05943 587 IAVPDIPRTLSGKKVEVAVKKIIAG 611
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
51-529 |
8.60e-20 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 92.15 E-value: 8.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQAc 130
Cdd:cd17656 15 TYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLTQR- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 131 yyEKVKDFARESDVKVMCVDSapdgclhfseLTQADENEAPQVDISpDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQ 210
Cdd:cd17656 94 --HLKSKLSFNKSTILLEDPS----------ISQEDTSNIDYINNS-DDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 211 VDGDNPNLyfhSEDVILCVLPMFHIyALNSImLCGLRVGAPILIMP---KFEIGSLLGLIEKYKVSIAPVVPPVMMSIAK 287
Cdd:cd17656 161 REKTNINF---SDKVLQFATCSFDV-CYQEI-FSTLLSGGTLYIIReetKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 288 SPDLDKHDLSSLRMIKSGGAPL--GKELEDTVRAKfpQARLGQGYGMTEAGpVLAMCLAFAKEPFDIKPgACGTVVRNAE 365
Cdd:cd17656 236 EREFINRFPTCVKHIITAGEQLviTNEFKEMLHEH--NVHLHNHYGPSETH-VVTTYTINPEAEIPELP-PIGKPISNTW 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 366 MKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATS---------------RTIDKEGWLhtgdigyidDDDELFIV 430
Cdd:cd17656 312 IYILD-QEQQLQPQGIVGELYISGASVARGYLNRQELTAekffpdpfdpnermyRTGDLARYL---------PDGNIEFL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 431 DRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVKSEKsqATEDEIKQYISKQVIFYKRIKRV 510
Cdd:cd17656 382 GRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQE--LNISQLREYLAKQLPEYMIPSFF 459
|
490
....*....|....*....
gi 306440447 511 FFIEAIPKAPSGKILRKNL 529
Cdd:cd17656 460 VPLDQLPLTPNGKVDRKAL 478
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
169-450 |
1.94e-19 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 92.01 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 169 EAPQVDI---SPDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQVDG-DNPNLYFHSEDVILCVLPMFHIYAlNSIMLC 244
Cdd:PLN02614 211 EGKQYDLpikKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLlKSANAALTVKDVYLSYLPLAHIFD-RVIEEC 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 245 GLRVGAPIlimpKFEIGSLLGLIE---KYKVSIAPVVPPVM-------------------------------------MS 284
Cdd:PLN02614 290 FIQHGAAI----GFWRGDVKLLIEdlgELKPTIFCAVPRVLdrvysglqkklsdggflkkfvfdsafsykfgnmkkgqSH 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 285 IAKSPDLDKHDLS--------SLRMIKSGGAPLGKELEDTVRAkFPQARLGQGYGMTEAgpvlamCLA-FAKEPFDIKP- 354
Cdd:PLN02614 366 VEASPLCDKLVFNkvkqglggNVRIILSGAAPLASHVESFLRV-VACCHVLQGYGLTES------CAGtFVSLPDELDMl 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 355 GACGTVVRNAEMKIVD-PETG----ASLPRnqpGEICIRGDQIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFI 429
Cdd:PLN02614 439 GTVGPPVPNVDIRLESvPEMEydalASTPR---GEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKI 514
|
330 340
....*....|....*....|..
gi 306440447 430 VDRLKELIKY-KGFQVAPAELE 450
Cdd:PLN02614 515 IDRKKNIFKLsQGEYVAVENIE 536
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
50-529 |
2.42e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 92.54 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLI-TQ 128
Cdd:PRK05691 3746 WSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVcSA 3825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 129 ACyyekvkdfaRESDVKVM-CVDSAPDGCLHFSELTQADE--NEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGLIT 205
Cdd:PRK05691 3826 AC---------REQARALLdELGCANRPRLLVWEEVQAGEvaSHNPGIYSGPDNLAYVIYTSGSTGLPKGVMVEQRGMLN 3896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 206 SVAQQVdgdnPNLYFHSEDVILCVLPM-FHIYALNsiMLCGLRVGAPILIMPK---FEIGSLLGLIEKYKVSIAPVVPPV 281
Cdd:PRK05691 3897 NQLSKV----PYLALSEADVIAQTASQsFDISVWQ--FLAAPLFGARVEIVPNaiaHDPQGLLAHVQAQGITVLESVPSL 3970
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 282 MMSIAKSpdlDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEagpvlamC---LAFAKEPFDIKPGA-- 356
Cdd:PRK05691 3971 IQGMLAE---DRQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAE-------CsddVAFFRVDLASTRGSyl 4040
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 357 -CGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTI-------DKEGWLHTGDIGYIDDDDELF 428
Cdd:PRK05691 4041 pIGSPTDNNRLYLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFvphpfgaPGERLYRTGDLARRRSDGVLE 4119
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 429 IVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAvVGLKDEDAGEVPVAFVVKSEKSQATE---DEIKQYISKQVIFYK 505
Cdd:PRK05691 4120 YVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAA-VAVQEGVNGKHLVGYLVPHQTVLAQGallERIKQRLRAELPDYM 4198
|
490 500
....*....|....*....|....
gi 306440447 506 RIKRVFFIEAIPKAPSGKILRKNL 529
Cdd:PRK05691 4199 VPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
51-492 |
2.56e-19 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 91.36 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLN-KIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQA 129
Cdd:cd17632 69 TYAELWERVGAVAAAHDpEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 130 CYYEKVKDFARE--SDVKVMCVDSAPDGCLHFSELTQADENEAPQ------------------------VDISPDDVVAL 183
Cdd:cd17632 149 EHLDLAVEAVLEggTPPRLVVFDHRPEVDAHRAALESARERLAAVgipvttltliavrgrdlppaplfrPEPDDDPLALL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 184 PYSSGTTGLPKGVMLTHKGLITS---VAQQVDGDNPnlyfhsEDVILCVLPMFHIYALNSImLCGLRVGAPILIMPKFEI 260
Cdd:cd17632 229 IYTSGSTGTPKGAMYTERLVATFwlkVSSIQDIRPP------ASITLNFMPMSHIAGRISL-YGTLARGGTAYFAAASDM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 261 GSL---LGLIEKYKVSIAP------------VVPPVMMSIAKSPDLDKHDLSSLR---------MIKSGGAPLGKELEDT 316
Cdd:cd17632 302 STLfddLALVRPTELFLVPrvcdmlfqryqaELDRRSVAGADAETLAERVKAELRervlggrllAAVCGSAPLSAEMKAF 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 317 VRAKFpQARLGQGYGMTEAGPVLAMclafakepfdikpgacGTVVRNA--EMKIVD-PETGASL-----PRnqpGEICIR 388
Cdd:cd17632 382 MESLL-DLDLHDGYGSTEAGAVILD----------------GVIVRPPvlDYKLVDvPELGYFRtdrphPR---GELLVK 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 389 GDQIMKGYLNDPEATSRTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEALLIAHPEISDAAVVGl 467
Cdd:cd17632 442 TDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQIFVYG- 520
|
490 500
....*....|....*....|....*
gi 306440447 468 kdEDAGEVPVAFVVKSEKSQATEDE 492
Cdd:cd17632 521 --NSERAYLLAVVVPTQDALAGEDT 543
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
51-535 |
2.76e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 90.60 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKhakasrakllitqaC 130
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQ--------------C 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 131 YYEkvkdfaresdvkvmcvdSAPDGclhFSELTQADEneapqvdispddVVALPYSSGTTGLPKGVMLTHKGLitsvAQQ 210
Cdd:cd05910 70 LQE-----------------AEPDA---FIGIPKADE------------PAAILFTSGSTGTPKGVVYRHGTF----AAQ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 211 VDGDNPNLYFHSEDVILCVLPMFHIYA----LNSImLCGLRVGAPILIMPKFeigsLLGLIEKYKVSIAPVVPPVMMSIA 286
Cdd:cd05910 114 IDALRQLYGIRPGEVDLATFPLFALFGpalgLTSV-IPDMDPTRPARADPQK----LVGAIRQYGVSIVFGSPALLERVA 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 287 KSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKF-PQARLGQGYGMTEAGPVLAM----CLAFAKEPFDIKPGAC-GTV 360
Cdd:cd05910 189 RYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLsDEAEILTPYGATEALPVSSIgsreLLATTTAATSGGAGTCvGRP 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 361 VRNAEMKIVD------PETGAS--LPRNQPGEICIRGDQIMKGYLNDPEATSRT-IDKEG---WLHTGDIGYIDDDDELF 428
Cdd:cd05910 269 IPGVRVRIIEiddepiAEWDDTleLPRGEIGEITVTGPTVTPTYVNRPVATALAkIDDNSegfWHRMGDLGYLDDEGRLW 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 429 IVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLkDEDAGEVPVaFVVK-----SEKSQATEDEIKQyISKQVIF 503
Cdd:cd05910 349 FCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV-GKPGCQLPV-LCVEplpgtITPRARLEQELRA-LAKDYPH 425
|
490 500 510
....*....|....*....|....*....|....
gi 306440447 504 YKRIKRVFFIEAIPKAP--SGKILRknlkEKLAG 535
Cdd:cd05910 426 TQRIGRFLIHPSFPVDIrhNAKIFR----EKLAV 455
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
47-466 |
3.21e-19 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 90.81 E-value: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 47 GDVYTYADVELTARRVASGLNK-IGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLL 125
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 126 ITQACYYEKVKDFA---RESDVKV--MCVDSAPDGCLHFSELTQADENEAPQVD----ISPDDVVALPYSSGTTGLPKGV 196
Cdd:cd05938 83 VVAPELQEAVEEVLpalRADGVSVwyLSHTSNTEGVISLLDKVDAASDEPVPASlrahVTIKSPALYIYTSGTTGLPKAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 197 MLTHKGLITSVA-QQVDGdnpnlyFHSEDVILCVLPMFHIYA-LNSIMLCgLRVGAPILIMPKFEIGSLLGLIEKYKVSI 274
Cdd:cd05938 163 RISHLRVLQCSGfLSLCG------VTADDVIYITLPLYHSSGfLLGIGGC-IELGATCVLKPKFSASQFWDDCRKHNVTV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 275 APVVPPVMMSIAKSPDLDKHDLSSLRM-IKSGGAPlgkeleDTVRA---KFPQARLGQGYGMTEAGpvlamcLAFAKepF 350
Cdd:cd05938 236 IQYIGELLRYLCNQPQSPNDRDHKVRLaIGNGLRA------DVWREflrRFGPIRIREFYGSTEGN------IGFFN--Y 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 351 DIKPGACGTVvrNAEMKIV--------DPETGASLPRNQ-------PGE----IC-IRGDQIMKGYLNDPEATSR----- 405
Cdd:cd05938 302 TGKIGAVGRV--SYLYKLLfpfelikfDVEKEEPVRDAQgfcipvaKGEpgllVAkITQQSPFLGYAGDKEQTEKkllrd 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 306440447 406 ---------------TIDKEGWLHtgdigyiddddelFIvDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVG 466
Cdd:cd05938 380 vfkkgdvyfntgdllVQDQQNFLY-------------FH-DRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYG 441
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
39-529 |
5.42e-19 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 91.26 E-value: 5.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 39 PCLINGanGDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAK 118
Cdd:PRK10252 475 PALADA--RYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLE 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 119 ASRAKLLITQAcyyEKVKDFARESDVKVMCVDSAPdgclhfseltqADENEAPQVDISPDDVVALPYSSGTTGLPKGVML 198
Cdd:PRK10252 553 DARPSLLITTA---DQLPRFADVPDLTSLCYNAPL-----------APQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMV 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 199 THKGLItsvaqqvdgdNPNLYFH------SEDVILCVLPM-FHIyalnSI------MLCGLRvgapiLIMPKFEI----G 261
Cdd:PRK10252 619 GQTAIV----------NRLLWMQnhypltADDVVLQKTPCsFDV----SVweffwpFIAGAK-----LVMAEPEAhrdpL 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 262 SLLGLIEKYKVSIAPVVPPvMMSI---AKSPDLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFpQARLGQGYGMTEAGPV 338
Cdd:PRK10252 680 AMQQFFAEYGVTTTHFVPS-MLAAfvaSLTPEGARQSCASLRQVFCSGEALPADLCREWQQLT-GAPLHNLYGPTEAAVD 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 339 LAMCLAFAKEPFDIK--PGACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATS------------ 404
Cdd:PRK10252 758 VSWYPAFGEELAAVRgsSVPIGYPVWNTGLRILD-ARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTAsrfiadpfapge 836
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 405 ---RTIDKEGWLhtgdigyidDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVP----- 476
Cdd:PRK10252 837 rmyRTGDVARWL---------DDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQAAATGgdarq 907
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 306440447 477 -VAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNL 529
Cdd:PRK10252 908 lVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
177-529 |
8.02e-19 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 89.03 E-value: 8.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 177 PDDVVALPYSSGTTGLPKGVMLTHKglitSVAQQVDGDNPNLYFHSEDVILCVLPM-FHIYALNSIMLcgLRVGAPILIM 255
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQ----SLVNLSHGLIKEYGITSSDRVLQFASIaFDVAAEEIYVT--LLSGATLVLR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 256 PK---FEIGSLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKHDL-SSLRMIKSGG-APLGKELEDTVRAKFPQARLGQGY 330
Cdd:cd17644 179 PEemrSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGeAVQPELVRQWQKNVGNFIQLINVY 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 331 GMTEAGPVLAMCLAFAKEPFDIKPGACGTVVRNAEMKIVDpETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKE 410
Cdd:cd17644 259 GPTEATIAATVCRLTQLTERNITSVPIGRPIANTQVYILD-ENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISH 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 411 GWLH--------TGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVV- 481
Cdd:cd17644 338 PFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVp 417
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 306440447 482 KSEKSQATEdEIKQYISKQVIFYKrIKRVF-FIEAIPKAPSGKILRKNL 529
Cdd:cd17644 418 HYEESPSTV-ELRQFLKAKLPDYM-IPSAFvVLEELPLTPNGKIDRRAL 464
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
51-496 |
1.21e-18 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 89.52 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 51 TYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGaiITAANPFSTPAELA-----KHAKASRA--- 122
Cdd:PLN02861 79 TYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQG--ITYVPLYDTLGANAvefiiNHAEVSIAfvq 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 123 --KLLITQAC------YYEKVKDFARESDVKVMCVDSAPDGCLHFSELTQADENEAPQVDISPDDVVALPYSSGTTGLPK 194
Cdd:PLN02861 157 esKISSILSClpkcssNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELPPKQKTDICTIMYTSGTTGEPK 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 195 GVMLTHKGLITSVAQqVDgdnpNLYFHS------EDVILCVLPMFHIY------------------------------AL 238
Cdd:PLN02861 237 GVILTNRAIIAEVLS-TD----HLLKVTdrvateEDSYFSYLPLAHVYdqvietyciskgasigfwqgdirylmedvqAL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 239 NSIMLCGL-RVGAPIL--IMPKFEIGsllGLIEK------YKVSIAPVVPPVMMSIAkSPDLDKHDLSSL--------RM 301
Cdd:PLN02861 312 KPTIFCGVpRVYDRIYtgIMQKISSG---GMLRKklfdfaYNYKLGNLRKGLKQEEA-SPRLDRLVFDKIkeglggrvRL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 302 IKSGGAPLGKELEDTVRAKfPQARLGQGYGMTEAgpvLAMCLAFAKEPFDIKpGACGTVVRNAEMKIVD-PETG----AS 376
Cdd:PLN02861 388 LLSGAAPLPRHVEEFLRVT-SCSVLSQGYGLTES---CGGCFTSIANVFSMV-GTVGVPMTTIEARLESvPEMGydalSD 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 377 LPRnqpGEICIRGDQIMKGYLNDPEATSRTIdKEGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAELEALLIA 455
Cdd:PLN02861 463 VPR---GEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLsQGEYVAVENLENTYSR 538
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 306440447 456 HPEISDAAVVGlkdeDAGEVPVAFVVKSEKsQATEDEIKQY 496
Cdd:PLN02861 539 CPLIASIWVYG----NSFESFLVAVVVPDR-QALEDWAANN 574
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
183-530 |
1.29e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 88.17 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 183 LPYSSGTTGLPKgvmlthkgLITSVAQQVDG--DNPNLYFHSED----VILCvlPMFHIYALNSIMLCGLRVGA-PILIM 255
Cdd:PRK08308 106 LQYSSGTTGEPK--------LIRRSWTEIDReiEAYNEALNCEQdetpIVAC--PVTHSYGLICGVLAALTRGSkPVIIT 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 256 ---PKFeigsLLGLIEKYKVSIAPVVPPVMMSIAKSPDLDKhdlsSLRMIKSGGAPLGKELEDTVRAKfpQARLGQGYGM 332
Cdd:PRK08308 176 nknPKF----ALNILRNTPQHILYAVPLMLHILGRLLPGTF----QFHAVMTSGTPLPEAWFYKLRER--TTYMMQQYGC 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 333 TEAGpvlamCLAFAKepfDIK-PGACGTVVRNAEMkivdpETGASlpRNQPGEICIRGDQimkgylndpeatsRTIdkeg 411
Cdd:PRK08308 246 SEAG-----CVSICP---DMKsHLDLGNPLPHVSV-----SAGSD--ENAPEEIVVKMGD-------------KEI---- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 412 wlHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGE-VPVAFVVKSEksqATE 490
Cdd:PRK08308 294 --FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGErVKAKVISHEE---IDP 368
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 306440447 491 DEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLK 530
Cdd:PRK08308 369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
50-476 |
1.48e-18 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 88.25 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGaIITAANPFSTPAELAKHA-KASRAKLLITQ 128
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIG-VETALINSNLRLESLLHCiTVSKAKALIFN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 129 acyyekvkdfaresdvkvmcvdsapdgclHFSELTQADENEAP-QVDISPDDVVALPYSSGTTGLPKGVMLTHKGLITSV 207
Cdd:cd05939 83 -----------------------------LLDPLLTQSSTEPPsQDDVNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 208 AqqvdGDNPNLYFHSEDVILCVLPMFHIYAlnSIMLCG--LRVGAPILIMPKFEIGSLLGLIEKYKVSIAPVVPPV---M 282
Cdd:cd05939 134 A----GAYYAFGMRPEDVVYDCLPLYHSAG--GIMGVGqaLLHGSTVVIRKKFSASNFWDDCVKYNCTIVQYIGEIcryL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 283 MSIAKSPDLDKHdlsSLRMIKSGGapLGKELEDTVRAKFPQARLGQGYGMTEAGPVLAmclafakePFDIKPGACGTVVR 362
Cdd:cd05939 208 LAQPPSEEEQKH---NVRLAVGNG--LRPQIWEQFVRRFGIPQIGEFYGATEGNSSLV--------NIDNHVGACGFNSR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 363 N------AEMKIVDPETGaSLPRN--------QPGE------ICIRGDQIMK--GYLNDpEATSRTIDKEGWLH------ 414
Cdd:cd05939 275 IlpsvypIRLIKVDEDTG-ELIRDsdglcipcQPGEpgllvgKIIQNDPLRRfdGYVNE-GATNKKIARDVFKKgdsafl 352
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 306440447 415 TGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLkdedagEVP 476
Cdd:cd05939 353 SGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGV------EVP 408
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
178-535 |
2.22e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 86.64 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 178 DDVVALPYS-SGTTGLPKGVMLTHKGLITSvaqqvdGDNPNLYFHSEDVILCVLPMFHIYALNSIMLCGLRVGAPIL--I 254
Cdd:PRK07824 34 DDDVALVVAtSGTTGTPKGAMLTAAALTAS------ADATHDRLGGPGQWLLALPAHHIAGLQVLVRSVIAGSEPVEldV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 255 MPKFEIGSLLGLIEKYK-----VSIAPvvppvmMSIAKSpdLDKHD----LSSLRMIKSGGAPLGKELEDtvRAKFPQAR 325
Cdd:PRK07824 108 SAGFDPTALPRAVAELGggrryTSLVP------MQLAKA--LDDPAataaLAELDAVLVGGGPAPAPVLD--AAAAAGIN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 326 LGQGYGMTEAGpvlamclafakepfdikpGAC---GTVVRNAEMKIVDpetgaslprnqpGEICIRGDQIMKGYLN--DP 400
Cdd:PRK07824 178 VVRTYGMSETS------------------GGCvydGVPLDGVRVRVED------------GRIALGGPTLAKGYRNpvDP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 401 EATSrtidKEGWLHTGDIGYIDDDDeLFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPVAFV 480
Cdd:PRK07824 228 DPFA----EPGWFRTDDLGALDDGV-LTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAV 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 306440447 481 VKSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRKNLKEKLAG 535
Cdd:PRK07824 303 VGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRFAG 357
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
47-529 |
1.36e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 86.76 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 47 GDVYTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLI 126
Cdd:PRK05691 2211 GQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLL 2290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 127 TQACYYEKVKDFaresdvkvmcvdsaPDG----CLHFSELTQADENEAPQVDIS-PDDVVALPYSSGTTGLPKGVMLTHk 201
Cdd:PRK05691 2291 SDRALFEALGEL--------------PAGvarwCLEDDAAALAAYSDAPLPFLSlPQHQAYLIYTSGSTGKPKGVVVSH- 2355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 202 GLITSVAQQVDgdnPNLYFHSEDvilCVLpmfHIYALN---------SIMLCGLRVgaPILIMPKFEIGSLLGLIEKYKV 272
Cdd:PRK05691 2356 GEIAMHCQAVI---ERFGMRADD---CEL---HFYSINfdaaserllVPLLCGARV--VLRAQGQWGAEEICQLIREQQV 2424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 273 SIAPVVPPVMMSIAKSPdLDKHDLSSLRMIKSGGAPLGKELEDTVRAKFPQARLGQGYGMTEAGPVLAMCLAFAKEPFDI 352
Cdd:PRK05691 2425 SILGFTPSYGSQLAQWL-AGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTETVVMPLACLAPEQLEEGA 2503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 353 KPGACGTVVRNAEMKIVDPETgASLPRNQPGEICIRGDQIMKGYLNDPEATSRTIDKEGWLH-------TGDIGYIDDDD 425
Cdd:PRK05691 2504 ASVPIGRVVGARVAYILDADL-ALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdggrlyrTGDLVRLRADG 2582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 426 ELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLkDEDAGEVPVAFVV-----KSEKSQAT-EDEIKQYISK 499
Cdd:PRK05691 2583 LVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLVsavagQDDEAQAAlREALKAHLKQ 2661
|
490 500 510
....*....|....*....|....*....|
gi 306440447 500 QVIFYKRIKRVFFIEAIPKAPSGKILRKNL 529
Cdd:PRK05691 2662 QLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
46-451 |
1.81e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 85.38 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 46 NGDVYTYADVE---------LT----ARR---VASGLNKIGiQQGDVIMLFLPSSPEFVLAFLGASHRGAIitaANPFST 109
Cdd:PRK05850 16 DDAAFTFIDYEqdpagvaetLTwsqlYRRtlnVAEELRRHG-STGDRAVILAPQGLEYIVAFLGALQAGLI---AVPLSV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 110 PAELAKHAKASRA------KLLITQACYYEKVKDFARESDVkvmcvDSAPDgclhFSELTQADENEAPQVDISPDDVVA- 182
Cdd:PRK05850 92 PQGGAHDERVSAVlrdtspSVVLTTSAVVDDVTEYVAPQPG-----QSAPP----VIEVDLLDLDSPRGSDARPRDLPSt 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 183 --LPYSSGTTGLPKGVMLTHKGLITSVAQQVDGdnpnlYF-HSEDV------ILCVLPMFHIyalnsiMlcGLRVG--AP 251
Cdd:PRK05850 163 ayLQYTSGSTRTPAGVMVSHRNVIANFEQLMSD-----YFgDTGGVpppdttVVSWLPFYHD------M--GLVLGvcAP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 252 ILIMPKFEIGSLLGLIEKykvsiapvvpPV--MMSIAKSP---------------------DLDKHDLSSLRMIKSGG-- 306
Cdd:PRK05850 230 ILGGCPAVLTSPVAFLQR----------PArwMQLLASNPhafsaapnfafelavrktsddDMAGLDLGGVLGIISGSer 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 307 ---APLGKELEDTVRAKFPQARLGQGYGMTEAgpVLAMCLAFAKEP-----FD--------IKPGACGT--------VVR 362
Cdd:PRK05850 300 vhpATLKRFADRFAPFNLRETAIRPSYGLAEA--TVYVATREPGQPpesvrFDyeklsaghAKRCETGGgtplvsygSPR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 363 NAEMKIVDPETGASLPRNQPGEICIRGDQIMKGYLNDPEATSRTID----------KEG-WLHTgDIGYIDDDDELFIVD 431
Cdd:PRK05850 378 SPTVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGatlvdpspgtPEGpWLRT-GDLGFISEGELFIVG 456
|
490 500
....*....|....*....|
gi 306440447 432 RLKELIKYKGFQVAPAELEA 451
Cdd:PRK05850 457 RIKDLLIVDGRNHYPDDIEA 476
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
296-531 |
3.63e-17 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 83.89 E-value: 3.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 296 LSSLRMIKSGGAPLGKELEDTvrAKFPQARLGQGYGMTE-AGPVLAMclafakepfdiKPGA-------CGTVVRNAEMK 367
Cdd:PRK07445 229 LAQFRTILLGGAPAWPSLLEQ--ARQLQLRLAPTYGMTEtASQIATL-----------KPDDflagnnsSGQVLPHAQIT 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 368 IVdpetgaslpRNQPGEICIRGDQIMKGYLndPEatsrTIDKEGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPA 447
Cdd:PRK07445 296 IP---------ANQTGNITIQAQSLALGYY--PQ----ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 448 ELEALLIAHPEISDAAVVGLKDEDAGEVPVAFVVkSEKSQATEDEIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILRK 527
Cdd:PRK07445 361 EVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYV-PKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQ 439
|
....
gi 306440447 528 NLKE 531
Cdd:PRK07445 440 QLQQ 443
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
185-526 |
5.05e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 84.41 E-value: 5.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 185 YSSGTTGLPKGVMLTHKGLITSVA---QQVDGDNPNLYFHSEDVILCVLpmFHIYalnsimLCGLRVGAPILIMpkFEIG 261
Cdd:PTZ00237 261 YTSGTTGNSKAVVRSNGPHLVGLKyywRSIIEKDIPTVVFSHSSIGWVS--FHGF------LYGSLSLGNTFVM--FEGG 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 262 ---------SLLGLIEKYKVSIAPVVPPVMMSIAKS-PDLD----KHDLSSLRMIKSGGAPLGKELEDTVRAKFpQARLG 327
Cdd:PTZ00237 331 iiknkhiedDLWNTIEKHKVTHTLTLPKTIRYLIKTdPEATiirsKYDLSNLKEIWCGGEVIEESIPEYIENKL-KIKSS 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 328 QGYGMTEAGPVLAMCLAFAKEPFDikpgACGTVVRNAEMKIVDPEtGASLPRNQPGEICIRgdqimkgyLNDPEATSRTI 407
Cdd:PTZ00237 410 RGYGQTEIGITYLYCYGHINIPYN----ATGVPSIFIKPSILSED-GKELNVNEIGEVAFK--------LPMPPSFATTF 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 408 DKE------------GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEV 475
Cdd:PTZ00237 477 YKNdekfkqlfskfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNV 556
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 306440447 476 PVAF-VVKSEKSQATED------EIKQYISKQVIFYKRIKRVFFIEAIPKAPSGKILR 526
Cdd:PTZ00237 557 PIGLlVLKQDQSNQSIDlnklknEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
50-309 |
9.23e-17 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 83.31 E-value: 9.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANP-FSTPAELAKHAKaSRAKLLITQ 128
Cdd:PRK03584 115 LSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPdFGVQGVLDRFGQ-IEPKVLIAV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 129 ACYYEKVKDFARESDVKVMC-------------------VDSAPDGCLHFSELTQADENEAPQ-VDISPDDVVALPYSSG 188
Cdd:PRK03584 194 DGYRYGGKAFDRRAKVAELRaalpslehvvvvpylgpaaAAAALPGALLWEDFLAPAEAAELEfEPVPFDHPLWILYSSG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 189 TTGLPK-------GVMLTHkglITSVAQQVDgdnpnlyFHSEDVilcvlpmFHIYALNSIM-----LCGLRVGAPILIM- 255
Cdd:PRK03584 274 TTGLPKcivhghgGILLEH---LKELGLHCD-------LGPGDR-------FFWYTTCGWMmwnwlVSGLLVGATLVLYd 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 306440447 256 -----PKFEIgsLLGLIEKYKVSIAPVVPPVMMSIAKS---PdLDKHDLSSLRMIKSGGAPL 309
Cdd:PRK03584 337 gspfyPDPNV--LWDLAAEEGVTVFGTSAKYLDACEKAglvP-GETHDLSALRTIGSTGSPL 395
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
152-535 |
8.42e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 70.57 E-value: 8.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 152 APDGCLHFSELTQADENEAPQVDISPDD--VVALPYSSGTTGLPKGVMLTHKGL---ITSVAQQVDGDNPnlyfhsEDVI 226
Cdd:PRK05851 124 AVDSSVTVHDLATAAHTNRSASLTPPDSggPAVLQGTAGSTGTPRTAILSPGAVlsnLRGLNARVGLDAA------TDVG 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 227 LCVLPMFHIYALnSIMLCGLRVGAPILIMPK--F------------EIGSLL--------GLIEKYKVSIAPVvppvmms 284
Cdd:PRK05851 198 CSWLPLYHDMGL-AFLLTAALAGAPLWLAPTtaFsaspfrwlswlsDSRATLtaapnfayNLIGKYARRVSDV------- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 285 iakspdldkhDLSSLRMIKSGGAPLGKE-----LEDTVRAKFPQARLGQGYGMTEAG-----PVLAMCLAFAkepfDIKP 354
Cdd:PRK05851 270 ----------DLGALRVALNGGEPVDCDgferfATAMAPFGFDAGAAAPSYGLAESTcavtvPVPGIGLRVD----EVTT 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 355 GACGTVVRNA---------EMKIVDPETGASLPRNQPGEICIRGDQIMKGYLNDPeatsrTIDKEGWLHTGDIGYIDDDd 425
Cdd:PRK05851 336 DDGSGARRHAvlgnpipgmEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLGYLVDG- 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 426 ELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAGEVPvAFVVKSEKSQATEDEIKQYISKQVIFYK 505
Cdd:PRK05851 410 GLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARP-GLVIAAEFRGPDEAGARSEVVQRVASEC 488
|
410 420 430
....*....|....*....|....*....|....
gi 306440447 506 RI--KRVFFIE--AIPKAPSGKILRKNLKEKLAG 535
Cdd:PRK05851 489 GVvpSDVVFVApgSLPRTSSGKLRRLAVKRSLEA 522
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
72-484 |
1.11e-12 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 70.51 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 72 QQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQACYYEKVKDFARESDVK----VM 147
Cdd:PRK08043 253 VEGERIGLMLPNATISAAVIFGASLRRRIPAMMNYTAGVKGLTSAITAAEIKTIFTSRQFLDKGKLWHLPEQLTqvrwVY 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 148 CVD-----SAPDGCLHFSELTQADENEAPQvdiSPDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQ-QVDGDnpnlyFH 221
Cdd:PRK08043 333 LEDlkddvTTADKLWIFAHLLMPRLAQVKQ---QPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQiKTIAD-----FT 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 222 SEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPkfeigSLLglieKYKVsiapvVPPVMMS------IAKSPDL---- 291
Cdd:PRK08043 405 PNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYP-----SPL----HYRI-----VPELVYDrnctvlFGTSTFLgnya 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 292 ---DKHDLSSLRMIKSGGAPLGKELEDTVRAKFpQARLGQGYGMTEAGPVLAMCLafakePFDIKPGACGTVVRNAEMKI 368
Cdd:PRK08043 471 rfaNPYDFARLRYVVAGAEKLQESTKQLWQDKF-GLRILEGYGVTECAPVVSINV-----PMAAKPGTVGRILPGMDARL 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 369 VdPETGASlprnQPGEICIRGDQIMKGYL--------NDPEATSRTIDKE-GWLHTGDIGYIDDDDELFIVDRLKELIKY 439
Cdd:PRK08043 545 L-SVPGIE----QGGRLQLKGPNIMNGYLrvekpgvlEVPTAENARGEMErGWYDTGDIVRFDEQGFVQIQGRAKRFAKI 619
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 306440447 440 KGFQVAPAELEAL-LIAHPEISDAAVVGlKDEDAGEVPVAFVVKSE 484
Cdd:PRK08043 620 AGEMVSLEMVEQLaLGVSPDKQHATAIK-SDASKGEALVLFTTDSE 664
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
186-472 |
1.15e-11 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 66.71 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 186 SSGTTGLPKGVMLTHKGL---ITSVAQqvdgdnpNLY---FHSEDVILCVLP--------MFHiyalnsimLCGLRVGAP 251
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLdrwAELFAR-------SLRaagVRPGDRVQNAFGyglftgglGLH--------YGAERLGAT 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 252 ILIMpkfeiGS-----LLGLIEKYKVSIAPVVPPVMMSIAKSPD---LDKHDLSsLRMIKSGGAPLGKELedtvRAKFpQ 323
Cdd:COG1541 156 VIPA-----GGgnterQLRLMQDFGPTVLVGTPSYLLYLAEVAEeegIDPRDLS-LKKGIFGGEPWSEEM----RKEI-E 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 324 ARLG----QGYGMTEAGPVLAM-ClafakepfdikPGACGTVVRNAE--MKIVDPETGASLPRNQPGEI----------- 385
Cdd:COG1541 225 ERWGikayDIYGLTEVGPGVAYeC-----------EAQDGLHIWEDHflVEIIDPETGEPVPEGEEGELvvttltkeamp 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 386 CIR---GDqiMKGYLNDPEATSRT---IDKegwlhtgdigyiddddelfIVDRLKELIKYKGFQVAPAELEALLIAHPEI 459
Cdd:COG1541 294 LIRyrtGD--LTRLLPEPCPCGRThprIGR-------------------ILGRADDMLIIRGVNVFPSQIEEVLLRIPEV 352
|
330
....*....|...
gi 306440447 460 SDAAVVGLKDEDA 472
Cdd:COG1541 353 GPEYQIVVDREGG 365
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
43-535 |
2.43e-11 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 66.22 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 43 NGANGDVYTYADVELTARRVASGL-NKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASR 121
Cdd:cd05905 8 KGKEATTLTWGKLLSRAEKIAAVLqKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 122 AKL-LITQACYYEKVKDFARESDV----------KVMCVDSAPdgclhfSELTQADENEAPQVDISPDDVVALPYSSGTT 190
Cdd:cd05905 88 VRVaLTVEACLKGLPKKLLKSKTAaeiakkkgwpKILDFVKIP------KSKRSKLKKWGPHPPTRDGDTAYIEYSFSSD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 191 GLPKGVMLTHKGLIT---SVAQQVDgdnpnlYFHSEDVILCVLPM----FHIYALNSIMLcglrvGAP-ILIMPK-FEIG 261
Cdd:cd05905 162 GSLSGVAVSHSSLLAhcrALKEACE------LYESRPLVTVLDFKsglgLWHGCLLSVYS-----GHHtILIPPElMKTN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 262 --SLLGLIEKYKVSIAPVVPPVMMSIAKSPD-----LDKHD--LSSLRMIKsggAPLGKELEDTVRAKF--PQARLG--- 327
Cdd:cd05905 231 plLWLQTLSQYKVRDAYVKLRTLHWCLKDLSstlasLKNRDvnLSSLRMCM---VPCENRPRISSCDSFlkLFQTLGlsp 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 328 -----------------QGYGMTEAGPV------LAMCLAFAKEpfDIKPGA-----CGTVVRNAEMKIVDPETGASLPR 379
Cdd:cd05905 308 ravstefgtrvnpficwQGTSGPEPSRVyldmraLRHGVVRLDE--RDKPNSlplqdSGKVLPGAQVAIVNPETKGLCKD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 380 NQPGEICIRGDQIMKGY--LNDPE----------ATSRTIDKEGWLHT----------GDIGYIDDDDELFIVDRLKELI 437
Cdd:cd05905 386 GEIGEIWVNSPANASGYflLDGETndtfkvfpstRLSTGITNNSYARTgllgflrptkCTDLNVEEHDLLFVVGSIDETL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 438 KYKGFQVAPAELEA-LLIAHPEISDAAVVglkdeDAGEVPvafVVKSEKSQATEDEIKQYISKQV-----IFYKRIKRVF 511
Cdd:cd05905 466 EVRGLRHHPSDIEAtVMRVHPYRGRCAVF-----SITGLV---VVVAEQPPGSEEEALDLVPLVLnaileEHQVIVDCVA 537
|
570 580
....*....|....*....|....*..
gi 306440447 512 FIEA--IPKAPSGKILRKNLKE-KLAG 535
Cdd:cd05905 538 LVPPgsLPKNPLGEKQRMEIRQaFLAG 564
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
157-438 |
1.17e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 64.35 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 157 LHFSELTqadENEAPQVDIS---PDDVVALPYSSGTTGLPKGVMLTHKGLITSVAQQVDGD---NPNLYFHsedviLCVL 230
Cdd:PTZ00342 283 ILFDDMT---KNKTTNYKIQnedPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHSifkKYNPKTH-----LSYL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 231 PMFHIYALNSIMLCGLRvGAPILIMPKfEIGSLLGLIEKYKVSIAPVVPPV--------MMSIAKSP-----------DL 291
Cdd:PTZ00342 355 PISHIYERVIAYLSFML-GGTINIWSK-DINYFSKDIYNSKGNILAGVPKVfnriytniMTEINNLPplkrflvkkilSL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 292 DKHD--------------LSS---------LRMIKSGGAPLGKELEDTVRAKFpQARLGQGYGMTE-AGPVlamclaFAK 347
Cdd:PTZ00342 433 RKSNnnggfskflegithISSkikdkvnpnLEVILNGGGKLSPKIAEELSVLL-NVNYYQGYGLTEtTGPI------FVQ 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 348 EPFDIKPGACG-TVVRNAEMKIVDPET---GASLPRnqpGEICIRGDQIMKGYLNDPEATSRTIDKEGWLHTGDIGYIDD 423
Cdd:PTZ00342 506 HADDNNTESIGgPISPNTKYKVRTWETykaTDTLPK---GELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINK 582
|
330
....*....|....*
gi 306440447 424 DDELFIVDRLKELIK 438
Cdd:PTZ00342 583 NGSLTFLDRSKGLVK 597
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
186-524 |
2.83e-10 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 62.49 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 186 SSGTTGLPKGVMLTHKGL---ITSVAQQVDGDNPNLYFhsedviLCVLPMFHIYALNSIMlcGLRVGAPILIMPKfEIGS 262
Cdd:cd17654 126 TSGTTGTPKIVAVPHKCIlpnIQHFRSLFNITSEDILF------LTSPLTFDPSVVEIFL--SLSSGATLLIVPT-SVKV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 263 LLG-----LIEKYKVSIAPVVPPVM----MSIAKSPDLDKHdlSSLRMIKSGGAPLGKELED-TVRAKFPQARLGQGYGM 332
Cdd:cd17654 197 LPSkladiLFKRHRITVLQATPTLFrrfgSQSIKSTVLSAT--SSLRVLALGGEPFPSLVILsSWRGKGNRTRIFNIYGI 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 333 TEAGpvlamCLAFAKE-PFDIKPGACGTVVRNAEMKIVDPETGASLPRNQPGEICIRGdqIMKGYLNDPEATSR-TID-- 408
Cdd:cd17654 275 TEVS-----CWALAYKvPEEDSPVQLGSPLLGTVIEVRDQNGSEGTGQVFLGGLNRVC--ILDDEVTVPKGTMRaTGDfv 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 409 --KEGwlhtgdigyiddddELFIVDRLKELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAgevpVAFVVKSEKS 486
Cdd:cd17654 348 tvKDG--------------ELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQRL----IAFIVGESSS 409
|
330 340 350
....*....|....*....|....*....|....*....
gi 306440447 487 QATEDEI-KQYISKQVIfykrIKRVFFIEAIPKAPSGKI 524
Cdd:cd17654 410 SRIHKELqLTLLSSHAI----PDTFVQIDKLPLTSHGKV 444
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
10-203 |
4.10e-07 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 53.14 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 10 RSKLPDiyiP-KNL-------PLHSYVLENLSNHSSKPCLI-------NGANGDVYTYADVELTARRVASGLNKIGIQQG 74
Cdd:TIGR03443 219 KSLLPD---PtKDLdwsgfrgAIHDIFADNAEKHPDRTCVVetpsfldPSSKTRSFTYKQINEASNILAHYLLKTGIKRG 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 75 DVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPA------ELAKhakaSRAKLLITQA-CYYEKVKDF-ARESDVK- 145
Cdd:TIGR03443 296 DVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPArqtiylSVAK----PRALIVIEKAgTLDQLVRDYiDKELELRt 371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 306440447 146 -VMCVDSAPDGCLHFSELTQADEN----------EAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGL 203
Cdd:TIGR03443 372 eIPALALQDDGSLVGGSLEGGETDvlapyqalkdTPTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSL 440
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
50-535 |
1.25e-05 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 47.90 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 50 YTYADVELTARRVASGLNKIGIQQGDVIMLFLPSSPEFVLAFLGASHRGAIITAANPFSTPAELAKHAKASRAKLLITQa 129
Cdd:cd17647 21 FTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIVI- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 130 cyyekvkdfaresdvkvmcvdsapdgclhfseltqadenEAPQVDISPDDVVALPYSSGTTGLPKGVMLTHKGL---ITS 206
Cdd:cd17647 100 ---------------------------------------RAAGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLayyFPW 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 207 VAQQVdgdnpNLyfhSEDVILCVLPMFHIYALNSIMLCGLRVGAPILIMPKFEIGS---LLGLIEKYKVSIAPVVPP--- 280
Cdd:cd17647 141 MAKRF-----NL---SENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTpgrLAEWMAKYGATVTHLTPAmgq 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 281 VMMSIAKSPdldkhdLSSLRMIKSGGAPLGKelEDTVRAKF--PQARLGQGYGMTEAG--------PVLAMCLAFAKEPF 350
Cdd:cd17647 213 LLTAQATTP------FPKLHHAFFVGDILTK--RDCLRLQTlaENVRIVNMYGTTETQravsyfevPSRSSDPTFLKNLK 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 351 DIKPGacGTVVRNAEMKIVDpetgaslpRNQP---------GEICIRGDQIMKGYLNDPEATSRT------IDKEGWLH- 414
Cdd:cd17647 285 DVMPA--GRGMLNVQLLVVN--------RNDRtqicgigevGEIYVRAGGLAEGYRGLPELNKEKfvnnwfVEPDHWNYl 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306440447 415 TGDIGYIDDDDELFIVDRL---------------------KELIKYKGFQVAPAELEALLIAHPEISDAAVVGLKDEDAG 473
Cdd:cd17647 355 DKDNNEPWRQFWLGPRDRLyrtgdlgrylpngdceccgraDDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEE 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 306440447 474 EVPVAFVVKSEKSQATEDEIKQYISKQVIFYKRIKRVffieaIPKAPSGKILRKNLKEKLAG 535
Cdd:cd17647 435 PTLVSYIVPRFDKPDDESFAQEDVPKEVSTDPIVKGL-----IGYRKLIKDIREFLKKRLAS 491
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
32-77 |
5.17e-03 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 39.84 E-value: 5.17e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 306440447 32 LSNHSSKPCLinGANGDV-----YTYADVELTARRVASGLNKIGIQQGDVI 77
Cdd:PTZ00297 437 VTRHSTFRCL--GQTSESgesewLTYGTVDARARELGSGLLALGVRPGDVI 485
|
|
| |
