|
Name |
Accession |
Description |
Interval |
E-value |
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
146-596 |
0e+00 |
|
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: 854.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 146 DLRESLEEILPKLQAENIRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSGTTGLPKPAILTH 225
Cdd:cd05938 87 ELQEAVEEVLPALRADGVSVWYLSHTSNTEGVISLLDKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGLPKAARISH 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 226 ERVLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYL 305
Cdd:cd05938 167 LRVLQCSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWDDCRKHNVTVIQYIGELLRYL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 306 CNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLLRMLSPFELVQF 385
Cdd:cd05938 247 CNQPQSPNDRDHKVRLAIGNGLRADVWREFLRRFGPIRIREFYGSTEGNIGFFNYTGKIGAVGRVSYLYKLLFPFELIKF 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 386 DMEAAEPVRDNQGFCIPVGLGEPGLLLTKVVSQQPFVGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRD 465
Cdd:cd05938 327 DVEKEEPVRDAQGFCIPVAKGEPGLLVAKITQQSPFLGYAGDKEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHD 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 466 RLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFI 545
Cdd:cd05938 407 RVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVTVPGHEGRIGMAAVKLKPGHEFDGKKLYQHVREYLPAYARPRFL 486
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1007386236 546 RIQDAMEVTSTFKLMKTRLVREGFNVGIVVDPLFVLDNRAQSFRPLTAEMY 596
Cdd:cd05938 487 RIQDSLEITGTFKQQKVRLVEEGFNPSIISDPLYFLDETQKTYVPLTPDIY 537
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
146-606 |
0e+00 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 551.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 146 DLRESLEEILPKLQAENIRCFYLSHTSPTP-GVGALGAALDAAPSHPVPAdlRAGITWRSPALFIYTSGTTGLPKPAILT 224
Cdd:PRK08279 143 ELVEAFEEARADLARPPRLWVAGGDTLDDPeGYEDLAAAAAGAPTTNPAS--RSGVTAKDTAFYIYTSGTTGLPKAAVMS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 225 HERVLQMSKMLSLS-GATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLR 303
Cdd:PRK08279 221 HMRWLKAMGGFGGLlRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFWDDVRRYRATAFQYIGELCR 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 304 YLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKmsCLLRMLSPFELV 383
Cdd:PRK08279 301 YLLNQPPKPTDRDHRLRLMIGNGLRPDIWDEFQQRFGIPRILEFYAASEGNVGFINVFNFDGTVGR--VPLWLAHPYAIV 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 384 QFDMEAAEPVRDNQGFCIPVGLGEPGLLLTKVVSQQPFVGYRGPrELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYF 463
Cdd:PRK08279 379 KYDVDTGEPVRDADGRCIKVKPGEVGLLIGRITDRGPFDGYTDP-EASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQF 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 464 RDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPH 543
Cdd:PRK08279 458 VDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVEVPGTDGRAGMAAIVLADGAEFDLAALAAHLYERLPAYAVPL 537
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1007386236 544 FIRIQDAMEVTSTFKLMKTRLVREGFNVGIVVDPLFVLDNRAQSFRPLTAEMYQAVCEGTWRL 606
Cdd:PRK08279 538 FVRLVPELETTGTFKYRKVDLRKEGFDPSKVDDPLYVLDPGSGGYVPLTAELYAEIAAGKFRL 600
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
205-570 |
1.23e-169 |
|
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: 489.94 E-value: 1.23e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHERVLQMSKML-SLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCF 283
Cdd:cd05940 83 AALYIYTSGTTGLPKAAIISHRRAWRGGAFFaGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNF 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 284 WDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYVGR 363
Cdd:cd05940 163 WDDIRKYQATIFQYIGELCRYLLNQPPKPTERKHKVRMIFGNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFINFFGK 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 364 CGALGKMSCLLRMLSPFELVQFDMEAAEPVRDNQGFCIPVGLGEPGLLLTKVVSQQPFVGYRGPRElSERKLVRNVRQSG 443
Cdd:cd05940 243 PGAIGRNPSLLRKVAPLALVKYDLESGEPIRDAEGRCIKVPRGEPGLLISRINPLEPFDGYTDPAA-TEKKILRDVFKKG 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 444 DVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKVGMAAVQLAPGQTF 523
Cdd:cd05940 322 DAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAGMAAIVLQPNEEF 401
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1007386236 524 DGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVREGFN 570
Cdd:cd05940 402 DLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEGFD 448
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
203-570 |
2.39e-142 |
|
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: 421.45 E-value: 2.39e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 203 RSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLS-GATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTS 281
Cdd:cd05939 104 RDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAfGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSAS 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 282 CFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYV 361
Cdd:cd05939 184 NFWDDCVKYNCTIVQYIGEICRYLLAQPPSEEEQKHNVRLAVGNGLRPQIWEQFVRRFGIPQIGEFYGATEGNSSLVNID 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 362 GRCGALGKMSCLLRMLSPFELVQFDMEAAEPVRDNQGFCIPVGLGEPGLLLTKVVSQQP---FVGYRGPRElSERKLVRN 438
Cdd:cd05939 264 NHVGACGFNSRILPSVYPIRLIKVDEDTGELIRDSDGLCIPCQPGEPGLLVGKIIQNDPlrrFDGYVNEGA-TNKKIARD 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 439 VRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKVGMAAVqLA 518
Cdd:cd05939 343 VFKKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEGRAGMAAI-VD 421
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1007386236 519 PGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVREGFN 570
Cdd:cd05939 422 PERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEGYD 473
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
204-577 |
5.75e-118 |
|
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: 358.67 E-value: 5.75e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 204 SPALFIYTSGTTGLPKPAILTHERVLQMSKMLS-LSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSC 282
Cdd:cd05937 88 DPAILIYTSGTTGLPKAAAISWRRTLVTSNLLShDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 283 FWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNY-V 361
Cdd:cd05937 168 FWKDVRDSGATIIQYVGELCRYLLSTPPSPYDRDHKVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGVFALTNHnV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 362 G--RCGALGKMSCLLRMLSPFE--LVQFDMEAAEPVRDNQ-GFCIPVGLGEPGLLLTKV--VSQQPFVGYRGPRELSERK 434
Cdd:cd05937 248 GdfGAGAIGHHGLIRRWKFENQvvLVKMDPETDDPIRDPKtGFCVRAPVGEPGEMLGRVpfKNREAFQGYLHNEDATESK 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 435 LVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKVGMAA 514
Cdd:cd05937 328 LVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAA 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1007386236 515 VQL----APGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVREGfnvgivVDP 577
Cdd:cd05937 408 ITLeessAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEG------VDP 468
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
206-567 |
3.60e-73 |
|
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: 241.64 E-value: 3.60e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVLQMSKMLSLS-GATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFW 284
Cdd:COG0318 103 ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAAlGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 285 DDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGpIRIWEVYGSTEGNM------- 355
Cdd:COG0318 183 ELIERERVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVsgGAPLPPELLERFEERFG-VRIVEGYGLTETSPvvtvnpe 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 356 -GLVNYVGRCGalgkmscllrmlspfeLVQFDMEAAepVRDNQGfcIPVGLGEPGLLLTKvvSQQPFVGYRGPRELSERK 434
Cdd:COG0318 262 dPGERRPGSVG----------------RPLPGVEVR--IVDEDG--RELPPGEVGEIVVR--GPNVMKGYWNDPEATAEA 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 435 LVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGcEGKVGMAA 514
Cdd:COG0318 320 FR-------DGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEK-WGERVVAF 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1007386236 515 VQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVRE 567
Cdd:COG0318 392 VVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRER 444
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
204-564 |
5.02e-73 |
|
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: 240.27 E-value: 5.02e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 204 SPALFIYTSGTTGLPKPAILTHERVLQMSK-MLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSC 282
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTFAGYySARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 283 FWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGpIRIWEVYGSTEGNMGLVNYVG 362
Cdd:cd05934 162 FWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFG-VRLLEGYGMTETIVGVIGPRD 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 363 rcGALGKMSCLLRMlspfelvqFDMEAAepVRDNQGFCIPVglGEPG-LLLTKVVSQQPFVGYRGpRELSERKLVRNvrq 441
Cdd:cd05934 241 --EPRRPGSIGRPA--------PGYEVR--IVDDDGQELPA--GEPGeLVIRGLRGWGFFKGYYN-MPEATAEAMRN--- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 442 sgdVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKVgMAAVQLAPGQ 521
Cdd:cd05934 303 ---GWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGEDEV-KAVVVLRPGE 378
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1007386236 522 TFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:cd05934 379 TLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
205-560 |
1.12e-64 |
|
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: 215.61 E-value: 1.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHERVLQMSK-MLSLSGATADDVVYTVLPLYHVmGLVVGILGCLDLGATCVLAPKFSTSCF 283
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAaLAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 284 WDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNG--LRADVWETFQQRFGpIRIWEVYGSTEGN-----MG 356
Cdd:cd04433 81 LELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGapLPPELLERFEEAPG-IKLVNGYGLTETGgtvatGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 357 LVNYVGRCGALGKmscllrmlsPFELVQFDmeaaepVRDNQGfcIPVGLGEPGLLLTKvvSQQPFVGYRGPRELSERKLv 436
Cdd:cd04433 160 PDDDARKPGSVGR---------PVPGVEVR------IVDPDG--GELPPGEIGELVVR--GPSVMKGYWNNPEATAAVD- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 437 rnvrqsGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGcEGKVGMAAVQ 516
Cdd:cd04433 220 ------EDGWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPE-WGERVVAVVV 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1007386236 517 LAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLM 560
Cdd:cd04433 293 LRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
191-569 |
5.38e-59 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 206.15 E-value: 5.38e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 191 PVPAdlrAGITWRSPALFIYTSGTTGLPKPAILTHERV----LQMSKMLslsGATADDVVYTVLPLYHVMGLVVGILGCL 266
Cdd:PRK06155 171 PAPA---AAVQPGDTAAILYTSGTTGPSKGVCCPHAQFywwgRNSAEDL---EIGADDVLYTTLPLFHTNALNAFFQALL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 267 DlGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGpIRIWE 346
Cdd:PRK06155 245 A-GATYVLEPRFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFRERFG-VDLLD 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 347 VYGSTEGN--MGLVNYVGRCGALGkmscllRMLSPFELVQFDmEAAEPVRDnqgfcipvglGEPGLLLtkVVSQQPFV-- 422
Cdd:PRK06155 323 GYGSTETNfvIAVTHGSQRPGSMG------RLAPGFEARVVD-EHDQELPD----------GEPGELL--LRADEPFAfa 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 423 -GYRGPRElserKLVRNVRqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 501
Cdd:PRK06155 384 tGYFGMPE----KTVEAWR---NLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPV 456
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1007386236 502 CVPGCEGKVgMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVREGF 569
Cdd:PRK06155 457 PSELGEDEV-MAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGV 523
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
188-594 |
2.36e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 204.14 E-value: 2.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 188 PSHPVPADLragitwrspALFIYTSGTTGLPKPAILTHERVLQMSKMLSLS-GATADDVVYTVLPLYHVMGLVVGILGCL 266
Cdd:PRK07867 146 FRVADPDDL---------FMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRfGLGPDDVCYVSMPLFHSNAVMAGWAVAL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 267 DLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGN-GLRADVwETFQQRFGpIRIW 345
Cdd:PRK07867 217 AAGASIALRRKFSASGFLPDVRRYGATYANYVGKPLSYVLATPERPDDADNPLRIVYGNeGAPGDI-ARFARRFG-CVVV 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 346 EVYGSTEGNMGLVNYVG-RCGALGKMSCLLRMLSPfelvqfdmEAAEPvrdnqgfCIPVGLGEPGLL--------LTKVV 416
Cdd:PRK07867 295 DGFGSTEGGVAITRTPDtPPGALGPLPPGVAIVDP--------DTGTE-------CPPAEDADGRLLnadeaigeLVNTA 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 417 SQQPFVGYRGPRELSERKLVRNVRQSGDVYYNtgdvlamDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQV 496
Cdd:PRK07867 360 GPGGFEGYYNDPEADAERMRGGVYWSGDLAYR-------DADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEV 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 497 NVYGVCVPGCEGKVgMAAVQLAPGQTFDGEKL--YQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVREGFNVGiv 574
Cdd:PRK07867 433 AVYAVPDPVVGDQV-MAALVLAPGAKFDPDAFaeFLAAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGVDCA-- 509
|
410 420
....*....|....*....|.
gi 1007386236 575 vDPLFVL-DNRAQSFRPLTAE 594
Cdd:PRK07867 510 -DPVWWIrRLTPSDYAALADE 529
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
200-594 |
3.74e-50 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 182.15 E-value: 3.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 200 ITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLS-GATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKF 278
Cdd:PRK13388 147 VDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERfGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKF 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 279 STSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGpIRIWEVYGSTEGNMGLV 358
Cdd:PRK13388 227 SASGFLDDVRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEASPRDIAEFSRRFG-CQVEDGYGSSEGAVIVV 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 359 NYVGR-CGALGKmscllrmlsPFE-LVQFDMEAAEPvrdnqgfCIPVGLGEPGLLLT------KVVSQQ---PFVGY-RG 426
Cdd:PRK13388 306 REPGTpPGSIGR---------GAPgVAIYNPETLTE-------CAVARFDAHGALLNadeaigELVNTAgagFFEGYyNN 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 427 PRELSERklVRNvrqsGDvyYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPgc 506
Cdd:PRK13388 370 PEATAER--MRH----GM--YWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDE-- 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 507 egKVG---MAAVQLAPGQTFDGEKLYQHVRAW--LPAYATPHFIRIQDAMEVTSTFKLMKTRLVREGFNVGivvDPLFVL 581
Cdd:PRK13388 440 --RVGdqvMAALVLRDGATFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRELIAQGWATG---DPVTLW 514
|
410
....*....|....
gi 1007386236 582 DNRAQS-FRPLTAE 594
Cdd:PRK13388 515 VRRGGPaYRLMSEP 528
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
194-561 |
4.78e-40 |
|
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: 151.61 E-value: 4.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 194 ADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMS-KMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATC 272
Cdd:cd17631 89 ADSGAKVLFDDLALLMYTSGTTGRPKGAMLTHRNLLWNAvNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 273 VLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNG--LRADVWETFqQRFGPiRIWEVYGS 350
Cdd:cd17631 169 VILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGapMPERLLRAL-QARGV-KFVQGYGM 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 351 TEGNMGLV-----NYVGRCGALGK--MSCLLRMLSPfelvqfDMEAAEPvrdnqgfcipvglGEPGLLLtkvvsqqpfvg 423
Cdd:cd17631 247 TETSPGVTflspeDHRRKLGSAGRpvFFVEVRIVDP------DGREVPP-------------GEVGEIV----------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 424 YRGPRELSE--RKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGv 501
Cdd:cd17631 297 VRGPHVMAGywNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIG- 375
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1007386236 502 cVPGCE-GKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMK 561
Cdd:cd17631 376 -VPDEKwGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
193-565 |
1.41e-39 |
|
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: 151.18 E-value: 1.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 193 PADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVL---QMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLG 269
Cdd:cd05936 115 PLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVanaLQIKAWLEDLLEGDDVVLAALPLFHVFGLTVALLLPLALG 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 270 ATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNG--LRADVWETFQQRFGpIRIWEV 347
Cdd:cd05936 195 ATIVLIPRFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRDFSSLRLCISGGapLPVEVAERFEELTG-VPIVEG 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 348 YGSTE------GNmgLVNYVGRCGALGKmscllrmlsPFElvqfDMEAAepVRDNQGfcIPVGLGEPGLLLTKvvSQQPF 421
Cdd:cd05936 274 YGLTEtspvvaVN--PLDGPRKPGSIGI---------PLP----GTEVK--IVDDDG--EELPPGEVGELWVR--GPQVM 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 422 VGYRGPRELSERKLVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 501
Cdd:cd05936 333 KGYWNRPEETAEAFV-------DGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGV 405
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1007386236 502 CVPGcEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLV 565
Cdd:cd05936 406 PDPY-SGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
149-474 |
1.07e-37 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 144.76 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 149 ESLEEILPKLQAenIRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAGitwRSPALFIYTSGTTGLPKPAILTHE-- 226
Cdd:pfam00501 106 EELLEALGKLEV--VKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDP---DDLAYIIYTSGTTGKPKGVMLTHRnl 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 227 --RVLQMSKM-LSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSC---FWDDCRQHGVTVILYVGE 300
Cdd:pfam00501 181 vaNVLSIKRVrPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPALDpaaLLELIERYKVTVLYGVPT 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 301 LLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGPiRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLLRMLS 378
Cdd:pfam00501 261 LLNMLLEAGAPKRALLSSLRLVLsgGAPLPPELARRFRELFGG-ALVNGYGLTETTGVVTTPLPLDEDLRSLGSVGRPLP 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 379 PFELVQFDMEAAEPVRDnqgfcipvglGEPGLLLTKvvSQQPFVGYRGPRELSERKLVRnvrqsgDVYYNTGDVLAMDRE 458
Cdd:pfam00501 340 GTEVKIVDDETGEPVPP----------GEPGELCVR--GPGVMKGYLNDPELTAEAFDE------DGWYRTGDLGRRDED 401
|
330
....*....|....*.
gi 1007386236 459 GFLYFRDRLGDTFRWK 474
Cdd:pfam00501 402 GYLEIVGRKKDQIKLG 417
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
198-564 |
6.64e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 138.50 E-value: 6.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 198 AGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSK-MLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAP 276
Cdd:PRK07656 161 PEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAAdWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLP 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 277 KFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGlrADV----WETFQQRFGPIRIWEVYGSTE 352
Cdd:PRK07656 241 VFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGA--ASMpvalLERFESELGVDIVLTGYGLSE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 353 gnmglvnyvgrcgALGkMSCLLRMLSPFELVQ----FDMEAAE-PVRDNQGfcIPVGLGEPGLLLTKvvsqQPFV--GYR 425
Cdd:PRK07656 319 -------------ASG-VTTFNRLDDDRKTVAgtigTAIAGVEnKIVNELG--EEVPVGEVGELLVR----GPNVmkGYY 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 426 G-PRELSErklvrNVRQSGDVYynTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVP 504
Cdd:PRK07656 379 DdPEATAA-----AIDADGWLH--TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIG--VP 449
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1007386236 505 gCE--GKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:PRK07656 450 -DErlGEVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
205-567 |
1.01e-34 |
|
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: 137.44 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHERVLqmSKMLSLSGA---TADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTS 281
Cdd:cd05926 151 LALILHTSGTTGRPKGVPLTHRNLA--ASATNITNTyklTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSAS 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 282 CFWDDCRQHGVTVILYVGELLRYLCNIPQ-QPEDRTHTVRLAM--GNGLRADVWETFQQRFGpIRIWEVYGSTEgnmglv 358
Cdd:cd05926 229 TFWPDVRDYNATWYTAVPTIHQILLNRPEpNPESPPPKLRFIRscSASLPPAVLEALEATFG-APVLEAYGMTE------ 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 359 nyvgrcgALGKMSCllrmlSPFelvqfdmeaaEPVRDNQG-FCIPVG-----LGEPGLLLT-----KVVSQQPFV--GYR 425
Cdd:cd05926 302 -------AAHQMTS-----NPL----------PPGPRKPGsVGKPVGvevriLDEDGEILPpgvvgEICLRGPNVtrGYL 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 426 GPRElserklVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPg 505
Cdd:cd05926 360 NNPE------ANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDE- 432
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1007386236 506 CEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKtRLVRE 567
Cdd:cd05926 433 KYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQR-RKVAE 493
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
203-567 |
2.03e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 134.16 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 203 RSPALFIYTSGTTGLPKPAILTHERVLQMSK-MLSLSGATADDVVYTVLPLYHVMGLVVGILGcLDLGATCVLAPKFSTS 281
Cdd:PRK06187 167 NDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLaVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLA-LMAGAKQVIPRRFDPE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 282 CFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGpIRIWEVYGSTEgnmglvn 359
Cdd:PRK06187 246 NLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIygGAALPPALLREFKEKFG-IDLVQGYGMTE------- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 360 yvgrCGALgkMSCLL----------RMLS---PFELVqfdmEAAepVRDNQGFCIPVGLGEPGLLLTKvvSQQPFVGYRG 426
Cdd:PRK06187 318 ----TSPV--VSVLPpedqlpgqwtKRRSagrPLPGV----EAR--IVDDDGDELPPDGGEVGEIIVR--GPWLMQGYWN 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 427 PRELSERKLVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPGc 506
Cdd:PRK06187 384 RPEATAETID-------GGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIG--VPD- 453
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1007386236 507 E--GKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKtRLVRE 567
Cdd:PRK06187 454 EkwGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILK-RVLRE 515
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
205-564 |
3.68e-33 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 133.27 E-value: 3.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSGA-TADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCF 283
Cdd:PRK08008 175 TAEILFTSGTTSRPKGVVITHYNLRFAGYYSAWQCAlRDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSARAF 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 284 WDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVR-----LAMGNGLRadvwETFQQRFGpIRIWEVYGSTEGNMGLV 358
Cdd:PRK08008 255 WGQVCKYRATITECIPMMIRTLMVQPPSANDRQHCLRevmfyLNLSDQEK----DAFEERFG-VRLLTSYGMTETIVGII 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 359 N----------YVGRCGalgkmscllrmlspfelvqFDMEAAepVRDNQGFCIPVGL-------GEPGLLLTKvvsqqpf 421
Cdd:PRK08008 330 GdrpgdkrrwpSIGRPG-------------------FCYEAE--IRDDHNRPLPAGEigeicikGVPGKTIFK------- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 422 vGYRGPRELSERKLvrnvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 501
Cdd:PRK08008 382 -EYYLDPKATAKVL------EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGI 454
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1007386236 502 CVPGCEGKVgMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:PRK08008 455 KDSIRDEAI-KAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
188-566 |
5.43e-33 |
|
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: 131.64 E-value: 5.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 188 PSHPvPADLRAGIT------WRSPALFIYTSGTTGLPKPAILTHERVLQMSKML-SLSGATADDVVYTVLPLYHVMGLVV 260
Cdd:cd05941 69 PSYP-LAELEYVITdsepslVLDPALILYTSGTTGRPKGVVLTHANLAANVRALvDAWRWTEDDVLLHVLPLHHVHGLVN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 261 GILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYV----GELLRYLCNIPQQPEDRT----HTVRLAM-GNG-LRAD 330
Cdd:cd05941 148 ALLCPLFAGASVEFLPKFDPKEVAISRLMPSITVFMGVptiyTRLLQYYEAHFTDPQFARaaaaERLRLMVsGSAaLPVP 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 331 VWETFQQRFGPiRIWEVYGSTEGNMGLVN-YVG--RCGALGkmscllrmlSPFELVQfdmeaAEPVRDNQGfcIPVGLGE 407
Cdd:cd05941 228 TLEEWEAITGH-TLLERYGMTEIGMALSNpLDGerRPGTVG---------MPLPGVQ-----ARIVDEETG--EPLPRGE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 408 PGLLLTKvvSQQPFVGYRGPRELSERKLVrnvrqsGDVYYNTGDVLAMDREGFLYFRDRLG-DTFRWKGENVSTHEVEGV 486
Cdd:cd05941 291 VGEIQVR--GPSVFKEYWNKPEATKEEFT------DDGWFKTGDLGVVDEDGYYWILGRSSvDIIKSGGYKVSALEIERV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 487 LSQVDFLQQVNVYGvcVPGCE-GKVGMAAVQLAPG-QTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:cd05941 363 LLAHPGVSECAVIG--VPDPDwGERVVAVVVLRAGaAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
..
gi 1007386236 565 VR 566
Cdd:cd05941 441 RK 442
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
208-568 |
2.77e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 133.30 E-value: 2.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 208 FIYTSGTTGLPKPAILTHERvLQMSKMLSLSGATAD--DVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWD 285
Cdd:PRK07868 610 FIAFSTAGGELVAKQITNYR-WALSAFGTASAAALDrrDTVYCLTPLHHESGLLVSLGGAVVGGSRIALSRGLDPDRFVQ 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 286 DCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYVGrcg 365
Cdd:PRK07868 689 EVRQYGVTVVSYTWAMLREVVDDPAFVLHGNHPVRLFIGSGMPTGLWERVVEAFAPAHVVEFFATTDGQAVLANVSG--- 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 366 alGKMSCLLRML---SPFELVQFDMEAAEPVRDNQGFCIPVGLGEPGLLLTKVvsqqpfvgyRGPRELSErKLVRNVRQS 442
Cdd:PRK07868 766 --AKIGSKGRPLpgaGRVELAAYDPEHDLILEDDRGFVRRAEVNEVGVLLARA---------RGPIDPTA-SVKRGVFAP 833
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 443 GDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEgkVGMAAVQLAPGQT 522
Cdd:PRK07868 834 ADTWISTEYLFRRDDDGDYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEVGGRQ--LAVAAVTLRPGAA 911
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1007386236 523 FDGEKLYQHVRAwLPAYATPHFIRIQDAMEVTSTFKLMKTRLVREG 568
Cdd:PRK07868 912 ITAADLTEALAS-LPVGLGPDIVHVVPEIPLSATYRPTVSALRAAG 956
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
190-539 |
6.89e-31 |
|
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: 126.17 E-value: 6.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 190 HPVPADLRAGITwrSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLS---GATADDVVYTVLPLYHVMGLVvGILGCL 266
Cdd:cd05911 135 EDLPPPLKDGKD--DTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFlygNDGSNDVILGFLPLYHIYGLF-TTLASL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 267 DLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGPIRI 344
Cdd:cd05911 212 LNGATVIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILsgGAPLSKELQELLAKRFPNATI 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 345 WEVYGSTEG------NMGLVNYVGRCGalgkmscllRMLSPFELVQFDMEaaepvrDNQGfcipVGLGEPGLLLTKvvSQ 418
Cdd:cd05911 292 KQGYGMTETggiltvNPDGDDKPGSVG---------RLLPNVEAKIVDDD------GKDS----LGPNEPGEICVR--GP 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 419 QPFVGY-RGPRELSERklvrnvrQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVN 497
Cdd:cd05911 351 QVMKGYyNNPEATKET-------FDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAA 423
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1007386236 498 VYGVCVPGCeGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAY 539
Cdd:cd05911 424 VIGIPDEVS-GELPRAYVVRKPGEKLTEKEVKDYVAKKVASY 464
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
205-559 |
4.64e-28 |
|
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: 117.82 E-value: 4.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHERVL----QMSKMLSlsgATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPK-FS 279
Cdd:cd05909 149 PAVILFTSGSEGLPKGVVLSHKNLLanveQITAIFD---PNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNpLD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 280 TSCFWDDCRQHGVTVILYVGELLRYLCNiPQQPEDrTHTVRLAM--GNGLRADVWETFQQRFGpIRIWEVYGSTEG---- 353
Cdd:cd05909 226 YKKIPELIYDKKATILLGTPTFLRGYAR-AAHPED-FSSLRLVVagAEKLKDTLRQEFQEKFG-IRILEGYGTTECspvi 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 354 NMGLVNYVGRCGALGKmscllrmlsPFELVQFDMEAAEPVrdnqgfcIPVGLGEPGLLLTKVVSQqpFVGYRGPRELSER 433
Cdd:cd05909 303 SVNTPQSPNKEGTVGR---------PLPGMEVKIVSVETH-------EEVPIGEGGLLLVRGPNV--MLGYLNEPELTSF 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 434 KLvrnvrqsGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVdFLQQVNVYGVCVPgCEGKvGMA 513
Cdd:cd05909 365 AF-------GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEI-LPEDNEVAVVSVP-DGRK-GEK 434
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1007386236 514 AVQLAPGQTFDGEKLYQHVR-AWLPAYATPHFIRIQDAMEVTSTFKL 559
Cdd:cd05909 435 IVLLTTTTDTDPSSLNDILKnAGISNLAKPSYIHQVEEIPLLGTGKP 481
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
206-564 |
5.42e-28 |
|
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: 116.79 E-value: 5.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVLQMSKMLS--LSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFST-SC 282
Cdd:cd05919 94 AYLLYSSGTTGPPKGVMHAHRDPLLFADAMAreALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPTaER 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 283 FWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGpIRIWEVYGSTE-GNMGLVN 359
Cdd:cd05919 174 VLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRLCVsaGEALPRGLGERWMEHFG-GPILDGIGATEvGHIFLSN 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 360 YVG--RCGALGkmscllRMLSPFELvqfdmeaaePVRDNQGFCIPVGlgEPGLLLTKVVSQqpFVGYRGPRELSERKLVr 437
Cdd:cd05919 253 RPGawRLGSTG------RPVPGYEI---------RLVDEEGHTIPPG--EEGDLLVRGPSA--AVGYWNNPEKSRATFN- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 438 nvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCvPGCEGKVGMAAVQL 517
Cdd:cd05919 313 ------GGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVP-ESTGLSRLTAFVVL 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1007386236 518 APGQTFDG---EKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:cd05919 386 KSPAAPQEslaRDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
195-564 |
5.58e-28 |
|
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: 117.85 E-value: 5.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 195 DLRAGITWR-SPALFIYTSGTTGLPKPAILTHERVLQMSKMLS--LSGATADDVVYTVLPLYHVMGLVVGILGCLDLGAT 271
Cdd:cd05959 154 QLKPAATHAdDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYArnVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGAT 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 272 CVLAPKFST-SCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGpIRIWEVY 348
Cdd:cd05959 234 TVLMPERPTpAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVsaGEALPAEVGERWKARFG-LDILDGI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 349 GSTE-GNMGLVNYVG--RCGALGKMscllrmlSPFELVQFDMEAAEPVRDnqgfcipvglGEPGLLLTKVVSQQPfvGYR 425
Cdd:cd05959 313 GSTEmLHIFLSNRPGrvRYGTTGKP-------VPGYEVELRDEDGGDVAD----------GEPGELYVRGPSSAT--MYW 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 426 GPRELSerklvRNVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPG 505
Cdd:cd05959 374 NNRDKT-----RDTFQGE--WTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDED 446
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1007386236 506 CEGKVgMAAVQLAPGQTFDG---EKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:cd05959 447 GLTKP-KAFVVLRPGYEDSEaleEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
188-567 |
1.32e-26 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 114.05 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 188 PSHPVPADlragitwrSPALFIYTSGTTGLPKPAILTHeR--VLQMSKMLSLS-GATADDVVYTVLPLYHVMGLVVGILG 264
Cdd:COG0365 177 EPEPTDAD--------DPLFILYTSGTTGKPKGVVHTH-GgyLVHAATTAKYVlDLKPGDVFWCTADIGWATGHSYIVYG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 265 CLDLGATCVL---APKFST-SCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTH--TVRLAMGNG--LRADVWETFQ 336
Cdd:COG0365 248 PLLNGATVVLyegRPDFPDpGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDlsSLRLLGSAGepLNPEVWEWWY 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 337 QRFGpIRIWEVYGSTEGNMGLVNYVG----RCGALGKmscllrmlsPFelvqFDMEAAepVRDNQGfcIPVGLGEPGLLl 412
Cdd:COG0365 328 EAVG-VPIVDGWGQTETGGIFISNLPglpvKPGSMGK---------PV----PGYDVA--VVDEDG--NPVPPGEEGEL- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 413 tkVVsQQP----FVGYRGPRElserKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLS 488
Cdd:COG0365 389 --VI-KGPwpgmFRGYWNDPE----RYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALV 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 489 QVDFLQQVNVygVCVPGCEGKVGMAA-VQLAPGQTFDGE---KLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKtRL 564
Cdd:COG0365 462 SHPAVAEAAV--VGVPDEIRGQVVKAfVVLKPGVEPSDElakELQAHVREELGPYAYPREIEFVDELPKTRSGKIMR-RL 538
|
...
gi 1007386236 565 VRE 567
Cdd:COG0365 539 LRK 541
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
171-567 |
4.50e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 109.70 E-value: 4.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 171 TSPTPG-------VGALGAALDAAPSHPVPadlragiTWRSPALFIYTSGTTGLPKPAILTHERV---LQMSKMLSLSGA 240
Cdd:PRK05605 187 TGPAPGtvpwetlVDAAIGGDGSDVSHPRP-------TPDDVALILYTSGTTGKPKGAQLTHRNLfanAAQGKAWVPGLG 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 241 TADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRylcNIPQQPEDR---TH 317
Cdd:PRK05605 260 DGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPLYE---KIAEAAEERgvdLS 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 318 TVRLAMGNG--LRADVWETFQQRFGPiRIWEVYGSTE------GNMglVNYVGRCGALGkmscllrmlSPFELVqfDMEA 389
Cdd:PRK05605 337 GVRNAFSGAmaLPVSTVELWEKLTGG-LLVEGYGLTEtspiivGNP--MSDDRRPGYVG---------VPFPDT--EVRI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 390 AEPvrDNQGFCIPVglGEPGLLLTKvvSQQPFVGYRGPRELSERKLVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGD 469
Cdd:PRK05605 403 VDP--EDPDETMPD--GEEGELLVR--GPQVFKGYWNRPEETAKSFL-------DGWFRTGDVVVMEEDGFIRIVDRIKE 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 470 TFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVP-GCEGKVgmAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQ 548
Cdd:PRK05605 470 LIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREdGSEEVV--AAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHV 547
|
410
....*....|....*....
gi 1007386236 549 DAMEVTSTFKLMKtRLVRE 567
Cdd:PRK05605 548 DELPRDQLGKVRR-REVRE 565
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
206-567 |
9.45e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 108.58 E-value: 9.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVLQMSKM---LSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSC 282
Cdd:PRK06710 209 ALLQYTGGTTGFPKGVMLTHKNLVSNTLMgvqWLYNCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKM 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 283 FWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNG--LRADVWETFQQRFGPiRIWEVYGSTEGN-MGLVN 359
Cdd:PRK06710 289 VFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSapLPVEVQEKFETVTGG-KLVEGYGLTESSpVTHSN 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 360 YVGRCGALGKMSCllrmlsPF---ELVQFDMEAAEPVRDnqgfcipvglGEPGLLLTKvvSQQPFVGY-RGPRELSErkl 435
Cdd:PRK06710 368 FLWEKRVPGSIGV------PWpdtEAMIMSLETGEALPP----------GEIGEIVVK--GPQIMKGYwNKPEETAA--- 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 436 vrnVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPgCEGKVGMAAV 515
Cdd:PRK06710 427 ---VLQDG--WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDP-YRGETVKAFV 500
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1007386236 516 QLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVRE 567
Cdd:PRK06710 501 VLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEE 552
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
210-564 |
6.97e-24 |
|
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: 103.13 E-value: 6.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 210 YTSGTTGLPKPAILTHERVLQMSKMLSLS-GATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVL-APKFS-----TSC 282
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERlGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFpSPSFDplavlEAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 283 FWDDCRQ-HGVTVIlYVGELlrylcNIPQQPEDRTHTVR--LAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGN----M 355
Cdd:cd05917 89 EKEKCTAlHGVPTM-FIAEL-----EHPDFDKFDLSSLRtgIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSpvstQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 356 GL--------VNYVGRcgalgkmscllrmLSPF-ELVQFDMEAaepvrdnqgfCIPVGLGEPGLLLTKVVSQQpfVGYRG 426
Cdd:cd05917 163 TRtddsiekrVNTVGR-------------IMPHtEAKIVDPEG----------GIVPPVGVPGELCIRGYSVM--KGYWN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 427 PRELSERKLvrnvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPGC 506
Cdd:cd05917 218 DPEKTAEAI------DGDGWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVG--VPDE 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1007386236 507 E-GKVGMAAVQLAPGQTFDGEklyqHVRAW----LPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:cd05917 290 RyGEEVCAWIRLKEGAELTEE----DIKAYckgkIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
209-561 |
8.81e-24 |
|
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: 102.58 E-value: 8.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 209 IYTSGTTGLPKPAILTHERVLQMSKMLS-LSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDDC 287
Cdd:cd17638 6 MFTSGTTGRSKGVMCAHRQTLRAAAAWAdCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAILEAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 288 RQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNG--LRADVWETFQQRFGPIRIWEVYGSTEGNMGlvnyvgrcg 365
Cdd:cd17638 86 ERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAatVPVELVRRMRSELGFETVLTAYGLTEAGVA--------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 366 algkmsCLLRMLSPFELVQFDMEAAEPvrdnqGFciPVGLGEPGLLLtkVVSQQPFVGYRGPRELSERKLvrnvrqSGDV 445
Cdd:cd17638 157 ------TMCRPGDDAETVATTCGRACP-----GF--EVRIADDGEVL--VRGYNVMQGYLDDPEATAEAI------DADG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 446 YYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPGCE-GKVGMAAVQLAPGQTFD 524
Cdd:cd17638 216 WLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIG--VPDERmGEVGKAFVVARPGVTLT 293
|
330 340 350
....*....|....*....|....*....|....*..
gi 1007386236 525 GEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMK 561
Cdd:cd17638 294 EEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
209-545 |
1.01e-23 |
|
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: 102.35 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 209 IYTSGTTGLPKPAILTHERVL--QMSKMLSLsGATADDVVYTVLPLYHVMGLVVGiLGCLDLGATCVLAPKFSTSCFWDD 286
Cdd:cd17637 6 IHTAAVAGRPRGAVLSHGNLIaaNLQLIHAM-GLTEADVYLNMLPLFHIAGLNLA-LATFHAGGANVVMEKFDPAEALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 287 CRQHGVTVIlyvGELLRYLCNIPQQPEDrtHTVRLAmgnGLRA----DVWETFQ--QRFGPIRIWEVYGSTEgNMGLVN- 359
Cdd:cd17637 84 IEEEKVTLM---GSFPPILSNLLDAAEK--SGVDLS---SLRHvlglDAPETIQrfEETTGATFWSLYGQTE-TSGLVTl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 360 --YVGRCGALGKMScllrMLSPFELVQFDmeaaepvrDNqgfciPVGLGEPGllltKVVSQQP--FVGYRGPRELSERKL 435
Cdd:cd17637 155 spYRERPGSAGRPG----PLVRVRIVDDN--------DR-----PVPAGETG----EIVVRGPlvFQGYWNLPELTAYTF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 436 vRNvrqsGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWK--GENVSTHEVEGVLSQVDFLQQVNVYGvcVPGCEGKVGMA 513
Cdd:cd17637 214 -RN----G--WHHTGDLGRFDEDGYLWYAGRKPEKELIKpgGENVYPAEVEKVILEHPAIAEVCVIG--VPDPKWGEGIK 284
|
330 340 350
....*....|....*....|....*....|...
gi 1007386236 514 AV-QLAPGQTFDGEKLYQHVRAWLPAYATPHFI 545
Cdd:cd17637 285 AVcVLKPGATLTADELIEFVGSRIARYKKPRYV 317
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
205-566 |
1.79e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 101.09 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHERVL--QMSKMLSLSgATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSC 282
Cdd:PRK06839 151 SFIICYTSGTTGKPKGAVLTQENMFwnALNNTFAID-LTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKFEPTK 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 283 FWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRA--DVWETFQQRfgPIRIWEVYGSTEGNMGLV-- 358
Cdd:PRK06839 230 ALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCpeELMREFIDR--GFLFGQGFGMTETSPTVFml 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 359 ---NYVGRCGALGK--MSCLLRMLSPfelvqfdmeaaepvrdNQGfciPVGLGEPGLLLTkvvsqqpfvgyRGPRELSE- 432
Cdd:PRK06839 308 seeDARRKVGSIGKpvLFCDYELIDE----------------NKN---KVEVGEVGELLI-----------RGPNVMKEy 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 433 ---RKLVRNVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCeGK 509
Cdd:PRK06839 358 wnrPDATEETIQDG--WLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKW-GE 434
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1007386236 510 VGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVR 566
Cdd:PRK06839 435 IPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
206-564 |
2.05e-22 |
|
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: 100.11 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVL--QMSKMLSLsGATADDVVYTVLPLYHVMGLVVgILGCLDLGATCVLAPKFSTSCF 283
Cdd:cd05912 80 ATIMYTSGTTGKPKGVQQTFGNHWwsAIGSALNL-GLTEDDNWLCALPLFHISGLSI-LMRSVIYGMTVYLVDKFDAEQV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 284 WDDCRQHGVTVILYVGELLRYLcnIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRfgPIRIWEVYGSTEGNMGLVNYV 361
Cdd:cd05912 158 LHLINSGKVTIISVVPTMLQRL--LEILGEGYPNNLRCILlgGGPAPKPLLEQCKEK--GIPVYQSYGMTETCSQIVTLS 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 362 GRcGALGKMSCLLRMLSPFELvqfdmeaaEPVRDNQGfciPVGLGEpgllltkVVSQQPFV--GYRGPRELSERKLVRNv 439
Cdd:cd05912 234 PE-DALNKIGSAGKPLFPVEL--------KIEDDGQP---PYEVGE-------ILLKGPNVtkGYLNRPDATEESFENG- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 440 rqsgdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPGCE-GKVGMAAVQLA 518
Cdd:cd05912 294 ------WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVG--IPDDKwGQVPVAFVVSE 365
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1007386236 519 pgQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:cd05912 366 --RPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
203-564 |
2.25e-22 |
|
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: 100.29 E-value: 2.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 203 RSPALFIYTSGTTGLPKPAILTHE----RVLQMSKMLSLsgaTADDVVYTVLPLYHVMGlVVGILGCLDLGATCVLAPK- 277
Cdd:cd05930 93 DDLAYVIYTSGSTGKPKGVMVEHRglvnLLLWMQEAYPL---TPGDRVLQFTSFSFDVS-VWEIFGALLAGATLVVLPEe 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 278 --FSTSCFWDDCRQHGVTVILYVGELLRYLcnIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGPIRIWEVYGSTEG 353
Cdd:cd05930 169 vrKDPEALADLLAEEGITVLHLTPSLLRLL--LQELELAALPSLRLVLvgGEALPPDLVRRWRELLPGARLVNLYGPTEA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 354 NMGLVNYVgrcgalgkmscllrmlspfelVQFDMEAAEPV-----RDNQGFCI------PVGLGEPGLLLtkVVSQQPFV 422
Cdd:cd05930 247 TVDATYYR---------------------VPPDDEEDGRVpigrpIPNTRVYVldenlrPVPPGVPGELY--IGGAGLAR 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 423 GYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDT-----FRwkgenVSTHEVEGVLSQVDFLQQVn 497
Cdd:cd05930 304 GYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQvkirgYR-----IELGEIEAALLAHPGVREA- 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 498 vygVCVP---GCEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:cd05930 378 ---AVVAredGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
205-558 |
8.13e-22 |
|
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: 98.67 E-value: 8.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHERVL-QMSKMLSLSGATADDVVYTVLPLYHVMGLVVgILGCLDLGATCVLAPKFST-SC 282
Cdd:cd05922 119 LALLLYTSGSTGSPKLVRLSHQNLLaNARSIAEYLGITADDRALTVLPLSYDYGLSV-LNTHLLRGATLVLTNDGVLdDA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 283 FWDDCRQHGVT---VILYVGELLRYLCNIPQQ-PEDRTHTvrlAMGNGLRADVWETFQQRFGPIRIWEVYGSTEgnmglv 358
Cdd:cd05922 198 FWEDLREHGATglaGVPSTYAMLTRLGFDPAKlPSLRYLT---QAGGRLPQETIARLRELLPGAQVYVMYGQTE------ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 359 nyvgrcgALGKMSCLlrmlsPFELVQFDMEAAEP--------VRDNQGFciPVGLGEPGllltKVVSQQPFVGYRGPREL 430
Cdd:cd05922 269 -------ATRRMTYL-----PPERILEKPGSIGLaipggefeILDDDGT--PTPPGEPG----EIVHRGPNVMKGYWNDP 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 431 SERklvRNVRQSGDVYYnTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKV 510
Cdd:cd05922 331 PYR---RKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLA 406
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1007386236 511 gmAAVQLAPGQTFDgeKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFK 558
Cdd:cd05922 407 --LFVTAPDKIDPK--DVLRSLAERLPPYKVPATVRVVDELPLTASGK 450
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
205-564 |
1.26e-21 |
|
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: 97.79 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHERVL-QMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVL--APKFSTS 281
Cdd:cd05972 83 PALIYFTSGTTGLPKGVLHTHSYPLgHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVyeGPRFDAE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 282 CFWDDCRQHGVTVILYVGELLRYLcnIPQQPEDRT-HTVRLAMGNG--LRADVWETFQQRFG-PIRiwEVYGSTEGNMGL 357
Cdd:cd05972 163 RILELLERYGVTSFCGPPTAYRML--IKQDLSSYKfSHLRLVVSAGepLNPEVIEWWRAATGlPIR--DGYGQTETGLTV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 358 VNYVG---RCGALGK-MSCllrmlspfelvqFDMEaaepVRDNQGfcIPVGLGEPGLLLTKVVSQQPFVGYRGPRELSER 433
Cdd:cd05972 239 GNFPDmpvKPGSMGRpTPG------------YDVA----IIDDDG--RELPPGEEGDIAIKLPPPGLFLGYVGDPEKTEA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 434 KLVrnvrqsGDvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPgCEGKVGMA 513
Cdd:cd05972 301 SIR------GD-YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDP-VRGEVVKA 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1007386236 514 AVQLAPG---QTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:cd05972 373 FVVLTSGyepSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
206-566 |
2.84e-21 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 98.10 E-value: 2.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVLQMSKML-SLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAP------KF 278
Cdd:PRK07529 216 AAYFHTGGTTGMPKLAQHTHGNEVANAWLGaLLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLATpqgyrgPG 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 279 STSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRThTVRLAMGNG--LRADVWETFQQRFGpIRIWEVYGSTEGNMG 356
Cdd:PRK07529 296 VIANFWKIVERYRINFLSGVPTVYAALLQVPVDGHDIS-SLRYALCGAapLPVEVFRRFEAATG-VRIVEGYGLTEATCV 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 357 L-VNYVG---RCGALGkmsclLRMlsPFE---LVQFDmEAAEPVRDnqgfCIPvglGEPGLLLTkvvsQQP--FVGYRGP 427
Cdd:PRK07529 374 SsVNPPDgerRIGSVG-----LRL--PYQrvrVVILD-DAGRYLRD----CAV---DEVGVLCI----AGPnvFSGYLEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 428 RElsERKLVrnvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLsqvdfLQQVNVYGVCVPG-- 505
Cdd:PRK07529 435 AH--NKGLW-----LEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEAL-----LRHPAVALAAAVGrp 502
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1007386236 506 --CEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYAT-PHFIRIQDAMEVTSTFKLMKTRLVR 566
Cdd:PRK07529 503 daHAGELPVAYVQLKPGASATEAELLAFARDHIAERAAvPKHVRILDALPKTAVGKIFKPALRR 566
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
205-501 |
3.01e-21 |
|
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: 97.19 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTH----ERVLQMSKMLSLSGAtADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFST 280
Cdd:cd05923 152 PAFVFYTSGTTGLPKGAVIPQraaeSRVLFMSTQAGLRHG-RHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDP 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 281 SCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVR------LAMGNGLRADVwetfqQRFGPIRIWEVYGSTEGN 354
Cdd:cd05923 231 ADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRhvtfagATMPDAVLERV-----NQHLPGEKVNIYGTTEAM 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 355 MGLVNYVGRCGALGKMSCllrmlspFELVQFdmeaaepVRDNQGFCIPVGLGEPGLLLTKVVSQQPFVGYRGPRELSERK 434
Cdd:cd05923 306 NSLYMRDARTGTEMRPGF-------FSEVRI-------VRIGGSPDEALANGEEGELIVAAAADAAFTGYLNQPEATAKK 371
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1007386236 435 LVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 501
Cdd:cd05923 372 LQ-------DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGV 431
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
206-567 |
3.85e-21 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 97.43 E-value: 3.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVLqmSKMLSLSGATA------DDVVYTVLPLYHVMGLVVGILGCLDLGATCVLA--PK 277
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRNML--ANLEQAKAAYGpllhpgKELVVTALPLYHIFALTVNCLLFIELGGQNLLItnPR 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 278 fSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLR-----ADVWETFQQRfgpiRIWEVYGSTE 352
Cdd:PRK08974 287 -DIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAvqqavAERWVKLTGQ----YLLEGYGLTE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 353 gnmglvnyvgrCGALgkMSCllrmlSPFELVQFDMEAAEPV-------RDNQGFCIPvgLGEPGLLLTKvvSQQPFVGY- 424
Cdd:PRK08974 362 -----------CSPL--VSV-----NPYDLDYYSGSIGLPVpsteiklVDDDGNEVP--PGEPGELWVK--GPQVMLGYw 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 425 RGPRELSErklvrnVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVP 504
Cdd:PRK08974 420 QRPEATDE------VIKDG--WLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSE 491
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1007386236 505 GCEGKVGMAAVQLAPGQTfdGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKtRLVRE 567
Cdd:PRK08974 492 VSGEAVKIFVVKKDPSLT--EEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILR-RELRD 551
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
206-560 |
5.33e-21 |
|
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: 96.01 E-value: 5.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHeRVLQMSKMLSL--SGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCF 283
Cdd:cd05935 87 ALIPYTSGTTGLPKGCMHTH-FSAAANALQSAvwTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 284 WDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNG--LRADVWETFQQRFGpIRIWEVYGSTEG-NMGLVNY 360
Cdd:cd05935 166 LELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLKVLTGGGapMPPAVAEKLLKLTG-LRFVEGYGLTETmSQTHTNP 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 361 VGRCgalgKMSCLLRMLSPFELVQFDMEAAEPVRDNQgfcipvgLGEpgllltkVVSQQP--FVGY-RGPRELSERKlvr 437
Cdd:cd05935 245 PLRP----KLQCLGIP*FGVDARVIDIETGRELPPNE-------VGE-------IVVRGPqiFKGYwNRPEETEESF--- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 438 nVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPGCE-GKVGMAAVQ 516
Cdd:cd05935 304 -IEIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVIS--VPDERvGEEVKAFIV 380
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1007386236 517 LAPGQ--TFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLM 560
Cdd:cd05935 381 LRPEYrgKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKIL 426
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
205-569 |
1.33e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 95.38 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHERVLQ--MSKMLSLsGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSC 282
Cdd:PRK08316 173 LAQILYTSGTESLPKGAMLTHRALIAeyVSCIVAG-DMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPEL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 283 FWDDCRQHGVTVI-----LYVGeLLRYlcnipqqPEDRTHTVRlamgnGLR----------ADVWETFQQRFGPIRIWEV 347
Cdd:PRK08316 252 ILRTIEAERITSFfapptVWIS-LLRH-------PDFDTRDLS-----SLRkgyygasimpVEVLKELRERLPGLRFYNC 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 348 YGSTEgnMGLVNYV-------GRCGALGKMScllrmlspfelvqFDMEAAepVRDNQGFCIPVGlgEPGllltKVV--SQ 418
Cdd:PRK08316 319 YGQTE--IAPLATVlgpeehlRRPGSAGRPV-------------LNVETR--VVDDDGNDVAPG--EVG----EIVhrSP 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 419 QPFVGYRGPRELSERKLvrnvrqsGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNV 498
Cdd:PRK08316 376 QLMLGYWDDPEKTAEAF-------RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAV 448
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1007386236 499 YGVCVPGCEGKVgMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKtRLVREGF 569
Cdd:PRK08316 449 IGLPDPKWIEAV-TAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILK-RELRERY 517
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
206-567 |
9.72e-20 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 92.94 E-value: 9.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHER-VLQMSKMLSLSGATADDVVYTVLPLYHVMGLVvGILGCLDLGATCVLAPKFSTSCFW 284
Cdd:PLN02860 175 VLICFTSGTTGRPKGVTISHSAlIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLS-SALAMLMVGACHVLLPKFDAKAAL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 285 DDCRQHGVTVILYVGELLRYLCNIPQQPEDR--THTVR--LAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGnmglvny 360
Cdd:PLN02860 254 QAIKQHNVTSMITVPAMMADLISLTRKSMTWkvFPSVRkiLNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEA------- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 361 vgrCGALGKMSCLLRMLSPFE--LVQFDMEAAEPVRDNQGFCipVGLGEPGLLLTKVVSQQPFVG---YRGP----RELS 431
Cdd:PLN02860 327 ---CSSLTFMTLHDPTLESPKqtLQTVNQTKSSSVHQPQGVC--VGKPAPHVELKIGLDESSRVGrilTRGPhvmlGYWG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 432 ERKLVRNVRQSgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPGCE-GKV 510
Cdd:PLN02860 402 QNSETASVLSN-DGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVG--VPDSRlTEM 478
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1007386236 511 GMAAVQLAPG--------------QTFDGEKLYQHVRAW-LPAYATPH-FIRIQDAMEVTSTFKLMKTRLVRE 567
Cdd:PLN02860 479 VVACVRLRDGwiwsdnekenakknLTLSSETLRHHCREKnLSRFKIPKlFVQWRKPFPLTTTGKIRRDEVRRE 551
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
206-564 |
1.04e-19 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 93.02 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVL----QMSKMLSLSGATAD--DVVYTVLPLYHVMGLVVGILGCLDLGATCVLA--PK 277
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVanmqQAHQWLAGTGKLEEgcEVVITALPLYHIFALTANGLVFMKIGGCNHLIsnPR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 278 fSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGL--RADVWETFQQRFGpIRIWEVYGSTEGNM 355
Cdd:PRK08751 291 -DMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMavQRSVAERWKQVTG-LTLVEAYGLTETSP 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 356 GlvnyvgrcgalgkmSCLlrmlSPFELVQFDMEAAEPV-------RDNQGFCIPvgLGEPGLLLTKvvSQQPFVGY-RGP 427
Cdd:PRK08751 369 A--------------ACI----NPLTLKEYNGSIGLPIpstdaciKDDAGTVLA--IGEIGELCIK--GPQVMKGYwKRP 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 428 RELSERklvrnvrQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPGCE 507
Cdd:PRK08751 427 EETAKV-------MDADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVG--VPDEK 497
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1007386236 508 GKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:PRK08751 498 SGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
209-570 |
1.20e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 92.33 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 209 IYTSGTTGLPKPAILTHERVL--QMSKMLSLsGATADDVVYTVLPLYHVMGLVVgILGCLDLGATCVLAPKFSTSCFWDD 286
Cdd:PRK03640 147 MYTSGTTGKPKGVIQTYGNHWwsAVGSALNL-GLTEDDCWLAAVPIFHISGLSI-LMRSVIYGMRVVLVEKFDAEKINKL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 287 CRQHGVTVILYVGELLRYLcnIPQQPEDRTH-TVRLAMGNGLRAD--VWETFQQRfgPIRIWEVYGSTEGNMGLV----- 358
Cdd:PRK03640 225 LQTGGVTIISVVSTMLQRL--LERLGEGTYPsSFRCMLLGGGPAPkpLLEQCKEK--GIPVYQSYGMTETASQIVtlspe 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 359 NYVGRCGALGKmscllrmlsPFelvqFDMEAAepVRDNQGFCIPVGLGEpgllltkVVSQQPFV--GYrgpreLSERKLV 436
Cdd:PRK03640 301 DALTKLGSAGK---------PL----FPCELK--IEKDGVVVPPFEEGE-------IVVKGPNVtkGY-----LNREDAT 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 437 RNVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPGCE-GKVGMAAV 515
Cdd:PRK03640 354 RETFQDG--WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVG--VPDDKwGQVPVAFV 429
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1007386236 516 QLapGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVREGFN 570
Cdd:PRK03640 430 VK--SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEE 482
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
188-570 |
1.22e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 92.26 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 188 PSHPV-PADLragitwrspALFIYTSGTTGLPKPAILTHERVLQMS--KMLSLsGATADDVVYTVLPLYHVMGLVVGILG 264
Cdd:PRK06145 142 PQAAVaPTDL---------VRLMYTSGTTDRPKGVMHSYGNLHWKSidHVIAL-GLTASERLLVVGPLYHVGAFDLPGIA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 265 CLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWE--TFQQRFGPI 342
Cdd:PRK06145 212 VLWVGGTLRIHREFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRirDFTRVFTRA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 343 RIWEVYGSTEGNMG-LVNYVGRcgALGKMSCLLRMLSPFELvqfdmeaaePVRDNQGFCIPVGL-GEPGLLLTKVVSqqp 420
Cdd:PRK06145 292 RYIDAYGLTETCSGdTLMEAGR--EIEKIGSTGRALAHVEI---------RIADGAGRWLPPNMkGEICMRGPKVTK--- 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 421 fvGYRGPRELSERKLVRNVRQSGDVYYntgdvlaMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYG 500
Cdd:PRK06145 358 --GYWKDPEKTAEAFYGDWFRSGDVGY-------LDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIG 428
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 501 VCVPGCeGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKtRLVREGFN 570
Cdd:PRK06145 429 VHDDRW-GERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLK-RVLRDELN 496
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
206-567 |
2.83e-19 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 91.35 E-value: 2.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVLQMSK-MLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTS--- 281
Cdd:PRK06087 190 AAVLFTSGTEGLPKGVMLTHNNILASERaYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDacl 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 282 -------CFWddcrQHGVTVILYvgellRYLCNIPQQPEDRThTVRLAMGNG--LRADVWETFQQRfgPIRIWEVYGSTE 352
Cdd:PRK06087 270 alleqqrCTC----MLGATPFIY-----DLLNLLEKQPADLS-ALRFFLCGGttIPKKVARECQQR--GIKLLSVYGSTE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 353 GN-MGLVNyvgrcgaLGKmsCLLRMlspfelVQFDMEAAEPVR----DNQGFCIPVG-LGEPgllltkvVSQQP--FVGY 424
Cdd:PRK06087 338 SSpHAVVN-------LDD--PLSRF------MHTDGYAAAGVEikvvDEARKTLPPGcEGEE-------ASRGPnvFMGY 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 425 RGPRELSERKLvrnvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLsqvdfLQQVNVYGVCVP 504
Cdd:PRK06087 396 LDEPELTARAL------DEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDIL-----LQHPKIHDACVV 464
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1007386236 505 GC-EGKVG----MAAVQLAPGQTFDGEKLYQHV-RAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVRE 567
Cdd:PRK06087 465 AMpDERLGerscAYVVLKAPHHSLTLEEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKD 533
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
206-564 |
3.81e-19 |
|
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: 90.23 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVLQMSKMLSLS--GATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCF 283
Cdd:cd05958 100 CILAFTSGTTGAPKATMHFHRDPLASADRYAVNvlRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 284 WDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGpIRIWEVYGSTEG-NMGLVNY 360
Cdd:cd05958 180 LSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVsaGEALPAALHRAWKEATG-IPIIDGIGSTEMfHIFISAR 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 361 VG--RCGALGKMscllrmLSPFELVQFDmEAAEPVRDnqgfcipvglGEPGLLLTkvvsQQPfVGYRGPRELSERKLVRn 438
Cdd:cd05958 259 PGdaRPGATGKP------VPGYEAKVVD-DEGNPVPD----------GTIGRLAV----RGP-TGCRYLADKRQRTYVQ- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 439 vrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLsqvdfLQQVNVYGVCVPGCE----GKVGMAA 514
Cdd:cd05958 316 -----GGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVL-----LQHPAVAECAVVGHPdesrGVVVKAF 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1007386236 515 VQLAPGQTFD---GEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:cd05958 386 VVLRPGVIPGpvlARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
194-564 |
4.67e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 90.64 E-value: 4.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 194 ADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSG-ATADDVVYTVLPLYHVMGLVVGILGCLDLGATC 272
Cdd:PRK09088 126 PADTPSIPPERVSLILFTSGTSGQPKGVMLSERNLQQTAHNFGVLGrVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSI 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 273 VLAPKF--STSCFWDDCRQHGVTVILYVGELLRYLCNIPQ-QPEDRTHTVRLAMGNG--LRADVWETFQQrfgPIRIWEV 347
Cdd:PRK09088 206 LVSNGFepKRTLGRLGDPALGITHYFCVPQMAQAFRAQPGfDAAALRHLTALFTGGAphAAEDILGWLDD---GIPMVDG 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 348 YGSTEG--------NMGLVNyvGRCGALGkmscllrmlSPFELVQFDmeaaepVRDNQGFCIPVGlgEPGLLLTKVVSQQ 419
Cdd:PRK09088 283 FGMSEAgtvfgmsvDCDVIR--AKAGAAG---------IPTPTVQTR------VVDDQGNDCPAG--VPGELLLRGPNLS 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 420 PfvGY-RGPRELSERKlvrnvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNV 498
Cdd:PRK09088 344 P--GYwRRPQATARAF-------TGDGWFRTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAV 414
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1007386236 499 YGVCVPGCeGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:PRK09088 415 VGMADAQW-GEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
206-564 |
6.23e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 88.69 E-value: 6.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVLQMSKMLS-LSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAP------KF 278
Cdd:cd05944 5 AAYFHTGGTTGTPKLAQHTHSNEVYNAWMLAlNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGpagyrnPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 279 STSCFWDDCRQHGVTVILYVGELLRYLCnipQQPEDR-THTVRLAMGNG--LRADVWETFQQRFGpIRIWEVYGSTEGNM 355
Cdd:cd05944 85 LFDNFWKLVERYRITSLSTVPTVYAALL---QVPVNAdISSLRFAMSGAapLPVELRARFEDATG-LPVVEGYGLTEATC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 356 GL-VNYVGRCGALGkmSCLLRMlsPFELVQFdmeaaePVRDNQGFCI-PVGLGEPGLLLtkVVSQQPFVGYRGprelSER 433
Cdd:cd05944 161 LVaVNPPDGPKRPG--SVGLRL--PYARVRI------KVLDGVGRLLrDCAPDEVGEIC--VAGPGVFGGYLY----TEG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 434 KLVRNVrqsGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCeGKVGMA 513
Cdd:cd05944 225 NKNAFV---ADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHA-GELPVA 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1007386236 514 AVQLAPGQTFDGEKLYQHVRAWLPAY-ATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:cd05944 301 YVQLKPGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
205-567 |
8.16e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 90.10 E-value: 8.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHErvlQMSKMLS------LSGATADDVVYTVLPLYHVMGlvVGILGCLDLGATCVLAP-- 276
Cdd:PRK07470 165 PCWFFFTSGTTGRPKAAVLTHG---QMAFVITnhladlMPGTTEQDASLVVAPLSHGAG--IHQLCQVARGAATVLLPse 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 277 KFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNG---LRADvwetfQQR----FGPIrIWEVYG 349
Cdd:PRK07470 240 RFDPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGapmYRAD-----QKRalakLGKV-LVQYFG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 350 STE--GNM------------GLVNYVGRCGalgkmscllrmlspFElvQFDMEAAepVRDNQGfcIPVGLGEPGLLLtkV 415
Cdd:PRK07470 314 LGEvtGNItvlppalhdaedGPDARIGTCG--------------FE--RTGMEVQ--IQDDEG--RELPPGETGEIC--V 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 416 VSQQPFVGYRGPRELSERKLVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQ 495
Cdd:PRK07470 372 IGPAVFAGYYNNPEANAKAFR-------DGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSE 444
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1007386236 496 VNVYGVCVPgCEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKtRLVRE 567
Cdd:PRK07470 445 VAVLGVPDP-VWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITK-KMVRE 514
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
205-487 |
1.20e-18 |
|
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: 89.22 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHERV---LQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTS 281
Cdd:cd05904 160 VAALLYSSGTTGRSKGVMLTHRNLiamVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 282 CFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNG--LRADVWETFQQRFGPIRIWEVYGSTE-GNMGLV 358
Cdd:cd05904 240 ELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQIMSGAapLGKELIEAFRAKFPNVDLGQGYGMTEsTGVVAM 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 359 NYVGRCGALGKMSCllRMLSPfelvqfDMEaAEPVRDNQGFCIPVglGEPGLLLTKvvSQQPFVGYRGPRELSERKLVrn 438
Cdd:cd05904 320 CFAPEKDRAKYGSV--GRLVP------NVE-AKIVDPETGESLPP--NQTGELWIR--GPSIMKGYLNNPEATAATID-- 384
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1007386236 439 vrqsGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVL 487
Cdd:cd05904 385 ----KEGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALL 429
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
203-564 |
2.06e-18 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 88.60 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 203 RSPALFIYTSGTTGLPK---PAILTHERVLQMSKMLSLS-GATADDVVYTVLPLYH----VMGLVVGilgclDLGATCVL 274
Cdd:PRK12406 152 PQPQSMIYTSGTTGHPKgvrRAAPTPEQAAAAEQMRALIyGLKPGIRALLTGPLYHsapnAYGLRAG-----RLGGVLVL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 275 APKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDR---------THT-------VRLAMgnglrADVWetfqqr 338
Cdd:PRK12406 227 QPRFDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKydvsslrhvIHAaapcpadVKRAM-----IEWW------ 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 339 fGPIrIWEVYGSTEgnMGLVNYVGRCGALGKMSCLLRMLSPFELVQFDMEAAepvrdnqgfciPVGLGEPGLLLTKVVSQ 418
Cdd:PRK12406 296 -GPV-IYEYYGSTE--SGAVTFATSEDALSHPGTVGKAAPGAELRFVDEDGR-----------PLPQGEIGEIYSRIAGN 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 419 QPFVGYRGPRELSErklvrnVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNV 498
Cdd:PRK12406 361 PDFTYHNKPEKRAE------IDRGG--FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAV 432
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1007386236 499 YGvcVPGCE-GKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:PRK12406 433 FG--IPDAEfGEALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
205-564 |
2.36e-18 |
|
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: 87.89 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHERVLQMSKMLSLS-GATADDVVYTVLPLYHVMGLVVgILGCLDLGATCVLAPKFSTscF 283
Cdd:TIGR01923 113 IATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENlGFTEDDNWLLSLPLYHISGLSI-LFRWLIEGATLRIVDKFNQ--L 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 284 WDDCRQHGVTVILYVGELL-RYLcnipqQPEDRTHTVR--LAMGNGLRADVWETFQQRFGPIriWEVYGSTEgnmglvny 360
Cdd:TIGR01923 190 LEMIANERVTHISLVPTQLnRLL-----DEGGHNENLRkiLLGGSAIPAPLIEEAQQYGLPI--YLSYGMTE-------- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 361 vgrcgalgkmscllrMLSPFELVQFDMEAAEP----VRDNQGFCIPV-GLGEPGLLLTKvvSQQPFVGYRGPRELSERkl 435
Cdd:TIGR01923 255 ---------------TCSQVTTATPEMLHARPdvgrPLAGREIKIKVdNKEGHGEIMVK--GANLMKGYLYQGELTPA-- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 436 vrnVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVnvygVCVPGCEGKVGMAAV 515
Cdd:TIGR01923 316 ---FEQQG--WFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGIQEA----VVVPKPDAEWGQVPV 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1007386236 516 QLAPGQ-TFDGEKLYQHVRAWLPAYATP-HFIRIqDAMEVTSTFKLMKTRL 564
Cdd:TIGR01923 387 AYIVSEsDISQAKLIAYLTEKLAKYKVPiAFEKL-DELPYNASGKILRNQL 436
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
205-566 |
4.41e-18 |
|
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: 87.10 E-value: 4.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHeRVL-------QMSKMLSlsgATADDVVYTVLPLYHVMGLVVGILGCLDLGATcVLA-- 275
Cdd:cd05971 90 PALIIYTSGTTGPPKGALHAH-RVLlghlpgvQFPFNLF---PRDGDLYWTPADWAWIGGLLDVLLPSLYFGVP-VLAhr 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 276 -PKFSTSCFWDDCRQHGVTVILYVGELLRYlcnIPQQPEDRTHTVR--LAMGNG---LRADVWETFQQRFGpIRIWEVYG 349
Cdd:cd05971 165 mTKFDPKAALDLMSRYGVTTAFLPPTALKM---MRQQGEQLKHAQVklRAIATGgesLGEELLGWAREQFG-VEVNEFYG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 350 STEGNMglvnYVGRCGALgkmscllrmlspFELVQFDMEAAEP-----VRDNQGFCIPVG-LGEPGLLLTKVVSqqpFVG 423
Cdd:cd05971 241 QTECNL----VIGNCSAL------------FPIKPGSMGKPIPghrvaIVDDNGTPLPPGeVGEIAVELPDPVA---FLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 424 YRGPRELSERKLVrnvrqsGDvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCV 503
Cdd:cd05971 302 YWNNPSATEKKMA------GD-WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPD 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1007386236 504 PgCEGKVGMAAVQLAPGQTFDGE---KLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVR 566
Cdd:cd05971 375 P-IRGEIVKAFVVLNPGETPSDAlarEIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
210-567 |
5.83e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 87.52 E-value: 5.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 210 YTSGTTGLPKPAILTHERVLQMSKMLSLS-GATADDVVYTVLPLYHVMGLVVGILGCLDLGAtCVLAPK--FSTSCFWDD 286
Cdd:PRK12583 208 YTSGTTGFPKGATLSHHNILNNGYFVAESlGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGA-CLVYPNeaFDPLATLQA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 287 CRQHGVTVI-----LYVGELlrylcNIPQQPEDRTHTVRLAMGNGLRADVwETFQQRFGPIRIWEV---YGSTEGNmGLV 358
Cdd:PRK12583 287 VEEERCTALygvptMFIAEL-----DHPQRGNFDLSSLRTGIMAGAPCPI-EVMRRVMDEMHMAEVqiaYGMTETS-PVS 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 359 NYVGRCGALGK-MSCLLRMLSPFELVQFDMEAAEpvrdnqgfcipVGLGEPGLLLTKVVSQqpFVGYRGPRELSERKLvr 437
Cdd:PRK12583 360 LQTTAADDLERrVETVGRTQPHLEVKVVDPDGAT-----------VPRGEIGELCTRGYSV--MKGYWNNPEATAESI-- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 438 nvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPgCE--GKVGMAAV 515
Cdd:PRK12583 425 ----DEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFG--VP-DEkyGEEIVAWV 497
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1007386236 516 QLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLvRE 567
Cdd:PRK12583 498 RLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRM-RE 548
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
194-567 |
6.22e-18 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 87.42 E-value: 6.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 194 ADLRAGITWRSP-----ALFIYTSGTTGLPKPAILTHERVlqMSKMLSLS---GATADDVVYTVLPLYHVMGLVVGILGC 265
Cdd:PRK13295 183 PDAPAILARLRPgpddvTQLIYTSGTTGEPKGVMHTANTL--MANIVPYAerlGLGADDVILMASPMAHQTGFMYGLMMP 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 266 LDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVR--LAMGNGLRADVWETFQQRFGpIR 343
Cdd:PRK13295 261 VMLGATAVLQDIWDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESGRPVSSLRtfLCAGAPIPGALVERARAALG-AK 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 344 IWEVYGSTEGnmGLVNYVGRCGALGKMS----CLLrmlsPFELVQfdmeaaepVRDNQGFCIPVglGEPGLLLTKVVSQq 419
Cdd:PRK13295 340 IVSAWGMTEN--GAVTLTKLDDPDERASttdgCPL----PGVEVR--------VVDADGAPLPA--GQIGRLQVRGCSN- 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 420 pFVGYRGPRELSerklvrnvRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVy 499
Cdd:PRK13295 403 -FGGYLKRPQLN--------GTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAI- 472
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 500 gVCVPGCE-GKVGMAAVQLAPGQTFDGEKLYQHVRAW-LPAYATPHFIRIQDAMEVTSTFKLMKTRLvRE 567
Cdd:PRK13295 473 -VAYPDERlGERACAFVVPRPGQSLDFEEMVEFLKAQkVAKQYIPERLVVRDALPRTPSGKIQKFRL-RE 540
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
201-567 |
8.44e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 86.90 E-value: 8.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 201 TWRSPA-LFIYTSGTTGLPKPAILTHERVLQ-MSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGcLDLGATCVLAPKF 278
Cdd:PRK07788 204 KPPKPGgIVILTSGTTGTPKGAPRPEPSPLApLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLA-MALGSTVVLRRRF 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 279 STSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM----GNGLRADVWETFQQRFGPIrIWEVYGSTEgn 354
Cdd:PRK07788 283 DPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIifvsGSALSPELATRALEAFGPV-LYNLYGSTE-- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 355 mglVNYVGrcgalgkmscllrMLSPFELVQFDMEAAEPVR-------DNQGFCIPVglGEPGLLLtkVVSQQPFVGYRGP 427
Cdd:PRK07788 360 ---VAFAT-------------IATPEDLAEAPGTVGRPPKgvtvkilDENGNEVPR--GVVGRIF--VGNGFPFEGYTDG 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 428 RelsERKLVRNVRQSGDVYYntgdvlaMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPGCE 507
Cdd:PRK07788 420 R---DKQIIDGLLSSGDVGY-------FDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIG--VDDEE 487
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1007386236 508 -GKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATP---HFIriqDAMEVTSTFKLMKtRLVRE 567
Cdd:PRK07788 488 fGQRLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPrdvVFL---DELPRNPTGKVLK-RELRE 547
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
196-490 |
1.01e-17 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 87.29 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 196 LRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKMLS-LSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVL 274
Cdd:PRK08633 775 YGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISdVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVY 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 275 APkfstscfwdD----------CRQHGVTVILYVGELLR-YLCNIPQQPEDRThTVRLAMGNG--LRADVWETFQQRFGp 341
Cdd:PRK08633 855 HP---------DptdalgiaklVAKHRATILLGTPTFLRlYLRNKKLHPLMFA-SLRLVVAGAekLKPEVADAFEEKFG- 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 342 IRIWEVYGSTEgnmglvnyvgrcgalgkmscllrmLSPFELVQF-DMEAAEPVRdnQGFCIP--VGL------------- 405
Cdd:PRK08633 924 IRILEGYGATE------------------------TSPVASVNLpDVLAADFKR--QTGSKEgsVGMplpgvavrivdpe 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 406 -------GEPGLLLTKvvSQQPFVGYRGPRELSErKLVRNVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENV 478
Cdd:PRK08633 978 tfeelppGEDGLILIG--GPQVMKGYLGDPEKTA-EVIKDIDGIG--WYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMV 1052
|
330
....*....|..
gi 1007386236 479 STHEVEGVLSQV 490
Cdd:PRK08633 1053 PLGAVEEELAKA 1064
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
188-576 |
2.23e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 85.60 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 188 PSHPvPADlragITWRSPALFIYTSGTTGLPKPAILTHERVL-QMSKMLSLSGA-TADDVVYTVLPLYHVMGLvVGILGC 265
Cdd:PRK07786 164 PAHA-PVD----IPNDSPALIMYTSGTTGRPKGAVLTHANLTgQAMTCLRTNGAdINSDVGFVGVPLFHIAGI-GSMLPG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 266 LDLGATCVLAP--KFSTSCFWDDCRQHGVTVILYVGELLRYLCNiPQQPEDRTHTVR-LAMGNGLRAD-VWETFQQRFGP 341
Cdd:PRK07786 238 LLLGAPTVIYPlgAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCA-EQQARPRDLALRvLSWGAAPASDtLLRQMAATFPE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 342 IRIWEVYGSTEgnMGLVNyvgrCGALGKMSclLRMLSPFELVqFDMEAAEPVRDNQGfciPVGLGEPGLLLtkvvsqqpf 421
Cdd:PRK07786 317 AQILAAFGQTE--MSPVT----CMLLGEDA--IRKLGSVGKV-IPTVAARVVDENMN---DVPVGEVGEIV--------- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 422 vgYRGPRELSErkLVRNVRQSGDVY----YNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVN 497
Cdd:PRK07786 376 --YRAPTLMSG--YWNNPEATAEAFaggwFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVA 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 498 VYGVCVPGCeGKVGMAAVQLAPG-QTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLvREGFNVGIVVD 576
Cdd:PRK07786 452 VIGRADEKW-GEVPVAVAAVRNDdAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL-RERYGACVNVE 529
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
203-561 |
2.31e-17 |
|
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: 83.85 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 203 RSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSG--ATADDVVYTVLPLYHVMGLVvGILGCLDLGATCVLAPKFST 280
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGlnWVVGDVTYLPLPATHIGGLW-WILTCLIHGGLCVTGGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 281 -SCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRA---DVweTFQQRFGPIRIWEVYGSTEGNMG 356
Cdd:cd17635 80 yKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAiaaDV--RFIEATGLTNTAQVYGLSETGTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 357 LVNYVGR----CGALGKmscllrmlsPFELVQFDmeaaepVRDNQGFCIPVGlgEPGLLLTKvvSQQPFVGYRGPRELSE 432
Cdd:cd17635 158 LCLPTDDdsieINAVGR---------PYPGVDVY------LAATDGIAGPSA--SFGTIWIK--SPANMLGYWNNPERTA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 433 RKLVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKVGM 512
Cdd:cd17635 219 EVLI-------DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGL 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1007386236 513 AAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMK 561
Cdd:cd17635 292 AVVASAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
205-560 |
4.14e-17 |
|
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: 84.94 E-value: 4.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTH--ERVLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVL---APKFS 279
Cdd:cd17634 234 PLFILYTSGTTGKPKGVLHTTggYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLyegVPNWP 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 280 T-SCFWDDCRQHGVTVILYVGELLRYLcnIPQQPE-----DRTHTVRL-AMGNGLRADVWETFqqrfgpiriWEVYGSte 352
Cdd:cd17634 314 TpARMWQVVDKHGVNILYTAPTAIRAL--MAAGDDaiegtDRSSLRILgSVGEPINPEAYEWY---------WKKIGK-- 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 353 GNMGLVNYVGRCGALGKMSCLLRML------SPFELVqFDMEAAepVRDNQGFCIPVGlGEPGLLLTKVVSQQPFVGYRG 426
Cdd:cd17634 381 EKCPVVDTWWQTETGGFMITPLPGAielkagSATRPV-FGVQPA--VVDNEGHPQPGG-TEGNLVITDPWPGQTRTLFGD 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 427 PRELSERKLVRNvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPgC 506
Cdd:cd17634 457 HERFEQTYFSTF-----KGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHA-I 530
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1007386236 507 EGKVGMAAVQLAPGQTfDGEKLYQHVRAW----LPAYATPHFIRIQDAMEVTSTFKLM 560
Cdd:cd17634 531 KGQAPYAYVVLNHGVE-PSPELYAELRNWvrkeIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
204-564 |
1.36e-16 |
|
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: 82.68 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 204 SPALFIYTSGTTGLPKPAILTHERVLQMSK-MLSLSGATADDVVyTVLPLYHVMGLVVGILGCLDLGATCVLAPK----- 277
Cdd:cd05945 98 DNAYIIFTSGSTGRPKGVQISHDNLVSFTNwMLSDFPLGPGDVF-LNQAPFSFDLSVMDLYPALASGATLVPVPRdatad 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 278 ----------------FSTSCFWDDCRQHG---------VTVILYVGELLrylcnipqqpedrthTVRLAmgnglradvw 332
Cdd:cd05945 177 pkqlfrflaehgitvwVSTPSFAAMCLLSPtftpeslpsLRHFLFCGEVL---------------PHKTA---------- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 333 ETFQQRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLlrmlsPFELVQFDMEAAepVRDNQGfcIPVGLGEPGLLL 412
Cdd:cd05945 232 RALQQRFPDARIYNTYGPTEATVAVTYIEVTPEVLDGYDRL-----PIGYAKPGAKLV--ILDEDG--RPVPPGEKGELV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 413 tkVVSQQPFVGYRGPRELSERKLVRNvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDF 492
Cdd:cd05945 303 --ISGPSVSKGYLNNPEKTAAAFFPD---EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPG 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1007386236 493 LQQVNVygVCVPGCEGKVGMAA-VQLAPGQTFDGEK-LYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:cd05945 378 VKEAVV--VPKYKGEKVTELIAfVVPKPGAEAGLTKaIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
205-559 |
1.66e-16 |
|
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: 82.26 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHERVlqMSKMLSLS---GATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPkfSTS 281
Cdd:cd05907 89 LATIIYTSGTTGRPKGVMLSHRNI--LSNALALAerlPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS--SAE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 282 CFWDDCRQHGVTVILYVGELLRYLCNIPQQ---PEDRTHTVRLAMGNGLR----------ADVWETFQQrFGpIRIWEVY 348
Cdd:cd05907 165 TLLDDLSEVRPTVFLAVPRVWEKVYAAIKVkavPGLKRKLFDLAVGGRLRfaasggaplpAELLHFFRA-LG-IPVYEGY 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 349 GSTE------GNMGLVNYVGRCGalgkmscllrmlspfelvqfdmeaaEPVRDNQgfcipVGLGEPGLLLTK--VVsqqp 420
Cdd:cd05907 243 GLTEtsavvtLNPPGDNRIGTVG-------------------------KPLPGVE-----VRIADDGEILVRgpNV---- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 421 FVGYRGPRELSERKLVRnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRW-KGENVSTHEVEGVLSQVDFLQQVNVY 499
Cdd:cd05907 289 MLGYYKNPEATAEALDA------DGWLHTGDLGEIDEDGFLHITGRKKDLIITsGGKNISPEPIENALKASPLISQAVVI 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 500 G--------VCVPGCEGKVGMAAVQLAPGQTFDG----EKLYQHVRAW-------LPAYATPHFIRI------QDAMEVT 554
Cdd:cd05907 363 GdgrpflvaLIVPDPEALEAWAEEHGIAYTDVAElaanPAVRAEIEAAveaanarLSRYEQIKKFLLlpepftIENGELT 442
|
....*
gi 1007386236 555 STFKL 559
Cdd:cd05907 443 PTLKL 447
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
205-566 |
1.92e-16 |
|
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: 82.16 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHERVLQ--MSKMLSLsGATADDVVY-TVLPLYhVMGLVVGILGCLDLGATCVL-APKFST 280
Cdd:cd05969 91 PTLLHYTSGTTGTPKGVLHVHDAMIFyyFTGKYVL-DLHPDDIYWcTADPGW-VTGTVYGIWAPWLNGVTNVVyEGRFDA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 281 SCFWDDCRQHGVTVILYVGELLRYLCNIPQQPE---DRTHT-VRLAMGNGLRADVWETFQQRFGpIRIWEVYGSTE-GNM 355
Cdd:cd05969 169 ESWYGIIERVKVTVWYTAPTAIRMLMKEGDELArkyDLSSLrFIHSVGEPLNPEAIRWGMEVFG-VPIHDTWWQTEtGSI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 356 GLVNYVG---RCGALGKmscllrmlsPFELVqfdmEAAepVRDNQGFCIPVGlgEPGLLLTKVVSQQPFVGYRGPRELSE 432
Cdd:cd05969 248 MIANYPCmpiKPGSMGK---------PLPGV----KAA--VVDENGNELPPG--TKGILALKPGWPSMFRGIWNDEERYK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 433 RKLVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPgCEGKVGM 512
Cdd:cd05969 311 NSFI-------DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDP-LRGEIIK 382
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1007386236 513 AAVQLAPGqtFD-----GEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKtRLVR 566
Cdd:cd05969 383 AFISLKEG--FEpsdelKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMR-RVLK 438
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
205-564 |
3.92e-16 |
|
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: 81.22 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHERVLQMSKM-LSLSGATADDVVYTVLPLYHVMGLVV-GILGCLDLGATCVLAPKFS-TS 281
Cdd:cd05920 141 VALFLLSGGTTGTPKLIPRTHNDYAYNVRAsAEVCGLDQDTVYLAVLPAAHNFPLACpGVLGTLLAGGRVVLAPDPSpDA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 282 CFwDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADvwETFQQRFGPI---RIWEVYGSTEGnmgLV 358
Cdd:cd05920 221 AF-PLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGARLS--PALARRVPPVlgcTLQQVFGMAEG---LL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 359 NYVgrcgalgkmscllRMLSPFELVQFD----MEAAEPVR--DNQGfcIPVGLGEPGLLLTkvvsqqpfvgyRGPRELSE 432
Cdd:cd05920 295 NYT-------------RLDDPDEVIIHTqgrpMSPDDEIRvvDEEG--NPVPPGEEGELLT-----------RGPYTIRG 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 433 --RKLVRNVRQ-SGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVygVCVPGCEGK 509
Cdd:cd05920 349 yyRAPEHNARAfTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAV--VAMPDELLG 426
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1007386236 510 VGMAAVQLAPGQTFDGEKLYQHVRAW-LPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:cd05920 427 ERSCAFVVLRDPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
206-549 |
4.08e-16 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 81.46 E-value: 4.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVLQMSKML-SLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFW 284
Cdd:PRK07514 159 AAILYTSGTTGRSKGAMLSHGNLLSNALTLvDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 285 DDCRQhgVTVI-----LYVgellRYLcnipQQPE-DRTHT--VRLAM-GNG-LRADVWETFQQRFGPiRIWEVYGSTEGN 354
Cdd:PRK07514 239 ALMPR--ATVMmgvptFYT----RLL----QEPRlTREAAahMRLFIsGSApLLAETHREFQERTGH-AILERYGMTETN 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 355 MGLVN-YVG--RCGALGkmscllRMLSPFELVQFDMEAAEpvrdnqgfciPVGLGEPGLLltKVVSQQPFVGY-RGPR-- 428
Cdd:PRK07514 308 MNTSNpYDGerRAGTVG------FPLPGVSLRVTDPETGA----------ELPPGEIGMI--EVKGPNVFKGYwRMPEkt 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 429 --ELSErklvrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGC 506
Cdd:PRK07514 370 aeEFRA-----------DGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDF 438
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1007386236 507 eGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQD 549
Cdd:PRK07514 439 -GEGVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVD 480
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
191-565 |
5.24e-16 |
|
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: 80.88 E-value: 5.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 191 PVPADLRAGitwrspALFIYTSGTTGLPK------PAILTHErVLQMSKMLsLSGATADDVVYTVLPLYHVMGLVVGILG 264
Cdd:cd05929 119 TPIEDEAAG------WKMLYSGGTTGRPKgikrglPGGPPDN-DTLMAAAL-GFGPGADSVYLSPAPLYHAAPFRWSMTA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 265 cLDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDR--THTVRLAMGNGLRADVWetFQQR---F 339
Cdd:cd05929 191 -LFMGGTLVLMEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAydLSSLKRVIHAAAPCPPW--VKEQwidW 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 340 GPIRIWEVYGSTEGN-MGLVN---------YVGRCGaLGKMSCL---LRMLSPFELVQFDMEAAEPVrdnqgfcipvglg 406
Cdd:cd05929 268 GGPIIWEYYGGTEGQgLTIINgeewlthpgSVGRAV-LGKVHILdedGNEVPPGEIGEVYFANGPGF------------- 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 407 epgllltkvvsqQPFVGYRGPRELSERKLVRNVrqsGDVYYntgdvlaMDREGFLYFRDRLGDTFRWKGENVSTHEVEGV 486
Cdd:cd05929 334 ------------EYTNDPEKTAAARNEGGWSTL---GDVGY-------LDEDGYLYLTDRRSDMIISGGVNIYPQEIENA 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 487 LSQVDFLQQVNVYGvcVPGCE-GKVGMAAVQLAPG---QTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKT 562
Cdd:cd05929 392 LIAHPKVLDAAVVG--VPDEElGQRVHAVVQPAPGadaGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRR 469
|
...
gi 1007386236 563 RLV 565
Cdd:cd05929 470 LLR 472
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
194-566 |
5.26e-16 |
|
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: 80.64 E-value: 5.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 194 ADLRAGITwRSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLS-GATADDVVYTVLPLYHVMGLVVGILGCLDLG-AT 271
Cdd:cd05973 80 AANRHKLD-SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAvDLRPEDSFWNAADPGWAYGLYYAITGPLALGhPT 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 272 CVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYL----CNIPQQPEDRTHTVRLAmGNGLRADVWETFQQRFGpIRIWEV 347
Cdd:cd05973 159 ILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLmaagAEVPARPKGRLRRVSSA-GEPLTPEVIRWFDAALG-VPIHDH 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 348 YGSTEGNMGLVNYVG-----RCGALGkmscllRMLSPFELVQFDMEAAEPvrdnqgfcipvGLGEPGLLLTKVvSQQP-- 420
Cdd:cd05973 237 YGQTELGMVLANHHAlehpvHAGSAG------RAMPGWRVAVLDDDGDEL-----------GPGEPGRLAIDI-ANSPlm 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 421 -FVGYRGPRELSerklvrnvrQSGDvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVY 499
Cdd:cd05973 299 wFRGYQLPDTPA---------IDGG-YYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVI 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1007386236 500 GVCVPgCEGKVGMAAVQLAPGqtFDG-----EKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVR 566
Cdd:cd05973 369 GVPDP-ERTEVVKAFVVLRGG--HEGtpalaDELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLLRR 437
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
188-569 |
6.17e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 80.80 E-value: 6.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 188 PSHPVPADLRAGITWrspalFIYTSGTTGLPKPAILTHERVLQMSKMLSLSGATADDVVY-TVLPLYHVMGLVVgiLGCL 266
Cdd:PRK06188 158 PAPLVAAALPPDIAG-----LAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFlMCTPLSHAGGAFF--LPTL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 267 DLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNipqQPEDRTHT----------------VRLAMGnglrad 330
Cdd:PRK06188 231 LRGGTVIVLAKFDPAEVLRAIEEQRITATFLVPTMIYALLD---HPDLRTRDlssletvyygaspmspVRLAEA------ 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 331 vwetfQQRFGPIrIWEVYGSTEGNMgLVNYVGRCGALGKMSCLLR---MLSPFELVQfdmeaaepVRDNQGfcIPVGLGE 407
Cdd:PRK06188 302 -----IERFGPI-FAQYYGQTEAPM-VITYLRKRDHDPDDPKRLTscgRPTPGLRVA--------LLDEDG--REVAQGE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 408 PGLLLTKvvsqQPFV--GYRGPRELSERKLvrnvrqsGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEG 485
Cdd:PRK06188 365 VGEICVR----GPLVmdGYWNRPEETAEAF-------RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVED 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 486 VLSQVDFLQQVNVYGVCVPGCeGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKtRLV 565
Cdd:PRK06188 434 VLAEHPAVAQVAVIGVPDEKW-GEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDK-KAL 511
|
....
gi 1007386236 566 REGF 569
Cdd:PRK06188 512 RARY 515
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
210-559 |
8.34e-16 |
|
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: 78.60 E-value: 8.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 210 YTSGTTGLPKpAILTHERVLQMS-----KMLSLSGataDDVVYTVLPLYHVMGLVvGILGCLDLGATCVLAPKFSTSCFW 284
Cdd:cd17633 7 FTSGTTGLPK-AYYRSERSWIESfvcneDLFNISG---EDAILAPGPLSHSLFLY-GAISALYLGGTFIGQRKFNPKSWI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 285 DDCRQHGVTVILYVGELLRYLCNIpQQPEDRTHTVrLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNYVG-- 362
Cdd:cd17633 82 RKINQYNATVIYLVPTMLQALART-LEPESKIKSI-FSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQes 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 363 -RCGALGKmscllrmlsPFELVQFDMEAAEPvrdnqgfcipvglGEPGLLltKVVSQQPFVGYRGPRELSErklvrnvrq 441
Cdd:cd17633 160 rPPNSVGR---------PFPNVEIEIRNADG-------------GEIGKI--FVKSEMVFSGYVRGGFSNP--------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 442 sgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPgcEGKVGMAAVQLAPGQ 521
Cdd:cd17633 207 --DGWMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVG--IP--DARFGEIAVALYSGD 280
|
330 340 350
....*....|....*....|....*....|....*...
gi 1007386236 522 TFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKL 559
Cdd:cd17633 281 KLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
170-564 |
5.45e-15 |
|
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: 77.63 E-value: 5.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 170 HTSPTPGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSGATADDVVYTV 249
Cdd:cd12117 103 SLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNTNYVTLGPDDRVLQT 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 250 LPL-YHVMGLvvGILGCLDLGATCVLAPK---FSTSCFWDDCRQHGVTVILYVGELLRYLCnipQQPEDRTHTVRLAMGN 325
Cdd:cd12117 183 SPLaFDASTF--EIWGALLNGARLVLAPKgtlLDPDALGALIAEEGVTVLWLTAALFNQLA---DEDPECFAGLRELLTG 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 326 GLRADV--WETFQQRFGPIRIWEVYGSTEgNMGLVNYvgrcgalgkmscllrmlspFELVQFDMEAAEP----------- 392
Cdd:cd12117 258 GEVVSPphVRRVLAACPGLRLVNGYGPTE-NTTFTTS-------------------HVVTELDEVAGSIpigrpiantrv 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 393 -VRDNQGfcIPVGLGEPGLL------LTKvvsqqpfvGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRD 465
Cdd:cd12117 318 yVLDEDG--RPVPPGVPGELyvggdgLAL--------GYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLG 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 466 RLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVygVCVPGCEGKVGMAAVqLAPGQTFDGEKLYQHVRAWLPAYATPHFI 545
Cdd:cd12117 388 RIDDQVKIRGFRIELGEIEAALRAHPGVREAVV--VVREDAGGDKRLVAY-VVAEGALDAAELRAFLRERLPAYMVPAAF 464
|
410
....*....|....*....
gi 1007386236 546 RIQDAMEVTSTFKLMKTRL 564
Cdd:cd12117 465 VVLDELPLTANGKVDRRAL 483
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
193-564 |
5.60e-15 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 77.88 E-value: 5.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 193 PADLRAGITWRSPALFIYTSGTTGLPKPAILTHER-VLQMSKMLSLSGATADDVVYTVLPLYHVMGLvVGILGCLDLGAT 271
Cdd:PRK13382 186 HAGQRPEPTGRKGRVILLTSGTTGTPKGARRSGPGgIGTLKAILDRTPWRAEEPTVIVAPMFHAWGF-SQLVLAASLACT 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 272 CVLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDR--THTVRLAMGNG--LRADVWETFQQRFGPIrIWEV 347
Cdd:PRK13382 265 IVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRysGRSLRFAAASGsrMRPDVVIAFMDQFGDV-IYNN 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 348 YGSTEGNMglvnyvgrcgalgkmsclLRMLSPFELVQFDMEAAEP-------VRDNQGFCIPVglGEPGLLLTKVVSQqp 420
Cdd:PRK13382 344 YNATEAGM------------------IATATPADLRAAPDTAGRPaegteirILDQDFREVPT--GEVGTIFVRNDTQ-- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 421 FVGYRGPRElserklvrnvRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYG 500
Cdd:PRK13382 402 FDGYTSGST----------KDFHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIG 471
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1007386236 501 vcVPGCE-GKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:PRK13382 472 --VDDEQyGQRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
203-559 |
9.50e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 78.28 E-value: 9.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 203 RSPALFIYTSGTTGLPKPAILTH----ERVLQMSKMLSLsgaTADDVVYTVLPLYHVMGlVVGILGCLDLGATCVLAPK- 277
Cdd:PRK12467 656 DNLAYVIYTSGSTGQPKGVAISHgalaNYVCVIAERLQL---AADDSMLMVSTFAFDLG-VTELFGALASGATLHLLPPd 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 278 --FSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNM 355
Cdd:PRK12467 732 caRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTV 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 356 GLVnyVGRCGALGKMSCLLRMLSPFElvqfdmEAAEPVRDNQGFCIPVGLgePGLLLtkVVSQQPFVGYRGPRELS-ERK 434
Cdd:PRK12467 812 GVS--TYELSDEERDFGNVPIGQPLA------NLGLYILDHYLNPVPVGV--VGELY--IGGAGLARGYHRRPALTaERF 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 435 LVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVygVCVPGCEGK----- 509
Cdd:PRK12467 880 VPDPFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVV--LAQPGDAGLqlvay 957
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1007386236 510 -VGMAAVQLAPGQTFdGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKL 559
Cdd:PRK12467 958 lVPAAVADGAEHQAT-RDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKL 1007
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
203-567 |
1.08e-14 |
|
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: 76.90 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 203 RSPALFIYTSGTTGLPKPAILTHER-VLQmskmlSLSGATAD-------DVVYTVLPLYHVMGLVVGILGCLdLGATCVL 274
Cdd:cd12119 163 NTAAAICYTSGTTGNPKGVVYSHRSlVLH-----AMAALLTDglglsesDVVLPVVPMFHVNAWGLPYAAAM-VGAKLVL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 275 -APKFSTSCFWDDCRQHGVTVILYVGE----LLRYLCNIPQqpeDRTHTVRLAMGNG-LRADVWETFQQRFgpIRIWEVY 348
Cdd:cd12119 237 pGPYLDPASLAELIEREGVTFAAGVPTvwqgLLDHLEANGR---DLSSLRRVVIGGSaVPRSLIEAFEERG--VRVIHAW 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 349 GSTEgnmglvnyvgrCGALGKMSCLlrmlsPFELVQFDMEAAEPVRDNQGFCIP-VGL---GEPGLLLTK-------VVS 417
Cdd:cd12119 312 GMTE-----------TSPLGTVARP-----PSEHSNLSEDEQLALRAKQGRPVPgVELrivDDDGRELPWdgkavgeLQV 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 418 QQPFV--GYRGPRELSERKLVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQ 495
Cdd:cd12119 376 RGPWVtkSYYKNDEESEALTE-------DGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAE 448
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1007386236 496 VNVYGVCVPgcegKVG---MAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLvRE 567
Cdd:cd12119 449 AAVIGVPHP----KWGerpLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL-RE 518
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
143-569 |
1.26e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 76.48 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 143 VTFDLRESLEEILPKLQAEnIRCFYLShTSPTPGVGALGAALDAAPSHPvPADLRAGitwrspALFIYTSGTTGLPK--- 219
Cdd:PRK08276 89 VSAALADTAAELAAELPAG-VPLLLVV-AGPVPGFRSYEEALAAQPDTP-IADETAG------ADMLYSSGTTGRPKgik 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 220 ---PAILTHERVLQMSKMLSLSGATADDVVYTV-LPLYHVMGLVVGiLGCLDLGATCVLAPKFSTSCFWDDCRQHGVTVI 295
Cdd:PRK08276 160 rplPGLDPDEAPGMMLALLGFGMYGGPDSVYLSpAPLYHTAPLRFG-MSALALGGTVVVMEKFDAEEALALIERYRVTHS 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 296 LYVGELLRYLCNIPqqPEDRT-----------HT-------VRLAMgnglrADVWetfqqrfGPIrIWEVYGSTEGNMGL 357
Cdd:PRK08276 239 QLVPTMFVRMLKLP--EEVRArydvsslrvaiHAaapcpveVKRAM-----IDWW-------GPI-IHEYYASSEGGGVT 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 358 V----NYVGRCGALGK-MSCLLRMLspfelvqfdmeaaepvrDNQGfcIPVGLGEPGLLLTKvVSQQPFvGYRGPRElse 432
Cdd:PRK08276 304 VitseDWLAHPGSVGKaVLGEVRIL-----------------DEDG--NELPPGEIGTVYFE-MDGYPF-EYHNDPE--- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 433 rKLVRNVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPGCE-GKVG 511
Cdd:PRK08276 360 -KTAAARNPHG--WVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFG--VPDEEmGERV 434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1007386236 512 MAAVQLAPGQTFD---GEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKtRLVREGF 569
Cdd:PRK08276 435 KAVVQPADGADAGdalAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYK-RRLRDRY 494
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
206-564 |
3.47e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 75.57 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHER----VLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPK-FST 280
Cdd:PRK05677 210 AVLQYTGGTTGVAKGAMLTHRNlvanMLQCRALMGSNLNEGCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILISNpRDL 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 281 SCFWDDCRQHGVTVILYVGELLRYLCNIP--QQPEDRTHTVRLAMGNGLRADVWETFQQRFGpIRIWEVYGSTEGN-MGL 357
Cdd:PRK05677 290 PAMVKELGKWKFSGFVGLNTLFVALCNNEafRKLDFSALKLTLSGGMALQLATAERWKEVTG-CAICEGYGMTETSpVVS 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 358 VNYVG--RCGALGkmscllrMLSPFELVQfdmeaaepVRDNQGFCIPvgLGEPGLLLTKvvSQQPFVGYRGPRELSERKL 435
Cdd:PRK05677 369 VNPSQaiQVGTIG-------IPVPSTLCK--------VIDDDGNELP--LGEVGELCVK--GPQVMKGYWQRPEATDEIL 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 436 vrnvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPgcEGKVGMAA- 514
Cdd:PRK05677 430 ------DSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIG--VP--DEKSGEAIk 499
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1007386236 515 --VQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:PRK05677 500 vfVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
204-564 |
5.03e-14 |
|
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: 74.34 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 204 SPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLS-GATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSC 282
Cdd:cd05903 94 AVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERlGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 283 FWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVR--LAMGNGLRADVWETFQQRFGPIrIWEVYGSTEgnmglvny 360
Cdd:cd05903 174 ALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRtfVCGGATVPRSLARRAAELLGAK-VCSAYGSTE-------- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 361 vgRCGALGKMS---CLLRMLS---PFELVQFDmeaaepVRDNQGFCIPVglGEPGLLLTKvvSQQPFVGYRGPRELserk 434
Cdd:cd05903 245 --CPGAVTSITpapEDRRLYTdgrPLPGVEIK------VVDDTGATLAP--GVEGELLSR--GPSVFLGYLDRPDL---- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 435 lvrNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLsqvdfLQQVNVYGVCVPGCE----GKV 510
Cdd:cd05903 309 ---TADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLL-----LGHPGVIEAAVVALPderlGER 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1007386236 511 GMAAVQLAPGQTFDGEKLYQHV-RAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:cd05903 381 ACAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
112-569 |
6.30e-14 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 74.54 E-value: 6.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 112 PPDTFVDAFERRARAQP--GRALLV-WTGPGagsvtfdlreslEEILPKLQAENIRCFYLSHTSPTPGVGALGAALDAAP 188
Cdd:PRK05852 97 PLDPALPIAEQRVRSQAagARVVLIdADGPH------------DRAEPTTRWWPLTVNVGGDSGPSGGTLSVHLDAATEP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 189 SH--PVPADLRAgitwrSPALFIYTSGTTGLPKPAILTHERVL-QMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGC 265
Cdd:PRK05852 165 TPatSTPEGLRP-----DDAMIMFTGGTTGLPKMVPWTHANIAsSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLAT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 266 LDLGATcVLAP---KFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQ-QPEDRTHT----VRlAMGNGLRADVWETFQQ 337
Cdd:PRK05852 240 LASGGA-VLLPargRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAAtEPSGRKPAalrfIR-SCSAPLTAETAQALQT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 338 RFGPIRIwEVYGSTEGNMGL----VNYVGrCGALGKMSCLLRMLSPFELVQFdmeaaepVRDNQGFCIPVGLGEPGLLLT 413
Cdd:PRK05852 318 EFAAPVV-CAFGMTEATHQVtttqIEGIG-QTENPVVSTGLVGRSTGAQIRI-------VGSDGLPLPAGAVGEVWLRGT 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 414 KVVSqqpfvGYRGPRELSERKLVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFL 493
Cdd:PRK05852 389 TVVR-----GYLGDPTITAANFT-------DGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNV 456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1007386236 494 QQVNVYGVCVPGCEGKVGMAAVQLAPGQTfDGEKLYQHVRAWLPAYATPhfIRIQDAMEVTSTFK-LMKTRLVREGF 569
Cdd:PRK05852 457 MEAAVFGVPDQLYGEAVAAVIVPRESAPP-TAEELVQFCRERLAAFEIP--ASFQEASGLPHTAKgSLDRRAVAEQF 530
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
206-532 |
7.61e-14 |
|
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: 74.49 E-value: 7.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVLqmskmLSLSGA---------TADDVVYTVLPLYHVMGLVVgILGCLDLGATCVLAP 276
Cdd:cd17642 187 ALIMNSSGSTGLPKGVQLTHKNIV-----ARFSHArdpifgnqiIPDTAILTVIPFHHGFGMFT-TLGYLICGFRVVLMY 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 277 KFSTSCFWDDCRQHGVTVILYVGELLRYLCNIP-QQPEDRTHTVRLAMGNG-LRADVWETFQQRFGPIRIWEVYGSTEGN 354
Cdd:cd17642 261 KFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTlVDKYDLSNLHEIASGGApLSKEVGEAVAKRFKLPGIRQGYGLTETT 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 355 MG-LVNYVGRC--GALGKmscllrmLSPFELVQ-FDMEAAEPVRDNQgfcipvgLGE---PGLLLTKvvsqqpfvGYRGP 427
Cdd:cd17642 341 SAiLITPEGDDkpGAVGK-------VVPFFYAKvVDLDTGKTLGPNE-------RGElcvKGPMIMK--------GYVNN 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 428 RELSERKLVRnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCe 507
Cdd:cd17642 399 PEATKALIDK------DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDA- 471
|
330 340
....*....|....*....|....*
gi 1007386236 508 GKVGMAAVQLAPGQTFDGEKLYQHV 532
Cdd:cd17642 472 GELPAAVVVLEAGKTMTEKEVMDYV 496
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
206-564 |
1.22e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 73.50 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPK---PAILTHERVLQMSKMLSLSGA----TADDVVYTVLPLYHVMGLV-VGILGCLdlGATCVLAPK 277
Cdd:PRK13390 151 AVMLYSSGTTGFPKgiqPDLPGRDVDAPGDPIVAIARAfydiSESDIYYSSAPIYHAAPLRwCSMVHAL--GGTVVLAKR 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 278 FSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTvrlamgNGLRA----------DVWETFQQRFGPIrIWEV 347
Cdd:PRK13390 229 FDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDV------SSLRAvihaaapcpvDVKHAMIDWLGPI-VYEY 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 348 YGSTEGN-MGLVN---YVGRCGALGKmscllRMLSPFELVqfdmeaaepvrDNQGFCIPVGlgEPGLLLTKVvSQQPFVG 423
Cdd:PRK13390 302 YSSTEAHgMTFIDspdWLAHPGSVGR-----SVLGDLHIC-----------DDDGNELPAG--RIGTVYFER-DRLPFRY 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 424 YRGPRELSErklvrnVRQSGDVYYNT-GDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVC 502
Cdd:PRK13390 363 LNDPEKTAA------AQHPAHPFWTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVP 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1007386236 503 VPGCEGKVgMAAVQLAPGQTFDGE---KLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:PRK13390 437 DPEMGEQV-KAVIQLVEGIRGSDElarELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
206-560 |
2.21e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 73.07 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVlqMSKMLS---LSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKfstsc 282
Cdd:PRK08314 193 AVLPYTSGTTGVPKGCMHTHRTV--MANAVGsvlWSNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPR----- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 283 fWDdcRQhgvtvilYVGELL-RYLC----NIPQQPEDRTHTVRLA---------MGNG---LRADVWETFQQRFGpIRIW 345
Cdd:PRK08314 266 -WD--RE-------AAARLIeRYRVthwtNIPTMVVDFLASPGLAerdlsslryIGGGgaaMPEAVAERLKELTG-LDYV 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 346 EVYGSTEgNMG--LVNYVGRcgalGKMSCLlrmLSPFelvqFDMEAAepVRDNQGFcIPVGLGEPGLLltkVVS-QQPFV 422
Cdd:PRK08314 335 EGYGLTE-TMAqtHSNPPDR----PKLQCL---GIPT----FGVDAR--VIDPETL-EELPPGEVGEI---VVHgPQVFK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 423 GY-RGPRELSERKLVRNvrqsGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGV 501
Cdd:PRK08314 397 GYwNRPEATAEAFIEID----GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIAT 472
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1007386236 502 CVP--GCEGKvgmAAVQLAPGQTfdGEKLYQHVRAW----LPAYATPHFIRIQDAMEVTSTFKLM 560
Cdd:PRK08314 473 PDPrrGETVK---AVVVLRPEAR--GKTTEEEIIAWarehMAAYKYPRIVEFVDSLPKSGSGKIL 532
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
194-500 |
2.57e-13 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 72.83 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 194 ADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKML-SLSGATADDVVYTVLPLYHVMGLVVGIlGCLDLGATC 272
Cdd:COG1022 174 EARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALlERLPLGPGDRTLSFLPLAHVFERTVSY-YALAAGATV 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 273 VLAPKFSTscFWDDCRQHGVTVILYV----------------------GELLRYLCNI-----PQQPEDRTHTVRLAMGN 325
Cdd:COG1022 253 AFAESPDT--LAEDLREVKPTFMLAVprvwekvyagiqakaeeagglkRKLFRWALAVgrryaRARLAGKSPSLLLRLKH 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 326 GLrAD--VWETFQQRFGP------------------------IRIWEVYGSTE-GNMGLVNYVGRC--GALGKmscllrm 376
Cdd:COG1022 331 AL-ADklVFSKLREALGGrlrfavsggaalgpelarffralgIPVLEGYGLTEtSPVITVNRPGDNriGTVGP------- 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 377 lspfelvqfdmeaaePVRDNQgfcipVGLGEPGLLLTKvvSQQPFVGYRGPRELSERKLVRnvrqsgDVYYNTGDVLAMD 456
Cdd:COG1022 403 ---------------PLPGVE-----VKIAEDGEILVR--GPNVMKGYYKNPEATAEAFDA------DGWLHTGDIGELD 454
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1007386236 457 REGFLYFRDRLGDTFrwK---GENVSTHEVEGVLSQVDFLQQVNVYG 500
Cdd:COG1022 455 EDGFLRITGRKKDLI--VtsgGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
206-539 |
2.68e-13 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 72.57 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVLQMSKML-----SLSGATADDVVY-TVLPLYHVMGLVVGILGCLDLGATCVLAPKFS 279
Cdd:PLN02574 201 AAIMYSSGTTGASKGVVLTHRNLIAMVELFvrfeaSQYEYPGSDNVYlAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFD 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 280 TSCFWDDCRQHGVTVILYVGELLRYLcnipqqpedrTHTVRLAMGNGLRADVW-------------ETFQQRFGPIRIWE 346
Cdd:PLN02574 281 ASDMVKVIDRFKVTHFPVVPPILMAL----------TKKAKGVCGEVLKSLKQvscgaaplsgkfiQDFVQTLPHVDFIQ 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 347 VYGSTEGNMglvnyvgrCGALGKMSCLLRMLSPFELVQFDMEaAEPVRDNQGFCIPVG-LGEPGLlltkvvsQQPFV--G 423
Cdd:PLN02574 351 GYGMTESTA--------VGTRGFNTEKLSKYSSVGLLAPNMQ-AKVVDWSTGCLLPPGnCGELWI-------QGPGVmkG 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 424 YRGPRELSERKLVRnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCV 503
Cdd:PLN02574 415 YLNNPKATQSTIDK------DGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPD 488
|
330 340 350
....*....|....*....|....*....|....*.
gi 1007386236 504 PGCeGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAY 539
Cdd:PLN02574 489 KEC-GEIPVAFVVRRQGSTLSQEAVINYVAKQVAPY 523
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
204-564 |
3.23e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 72.38 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 204 SPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSGAT--ADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTS 281
Cdd:PRK06178 210 ALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVggEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLARWDAV 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 282 CFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNG----LRADVWETFQQRFGPIRIWEVYGSTE----- 352
Cdd:PRK06178 290 AFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVRVVSfvkkLNPDYRQRWRALTGSVLAEAAWGMTEthtcd 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 353 --------GNMGLVNYVGRCGalgkmscLLRMLSPFELVQFDMEAaepvrdnqgfciPVGLGEPGLLLtkVVSQQPFVGY 424
Cdd:PRK06178 370 tftagfqdDDFDLLSQPVFVG-------LPVPGTEFKICDFETGE------------LLPLGAEGEIV--VRTPSLLKGY 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 425 RGPRELSERKLVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVP 504
Cdd:PRK06178 429 WNKPEATAEALR-------DGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDP 501
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 505 GcEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHfIRIQDAMEVTSTFKLMKTRL 564
Cdd:PRK06178 502 D-KGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDL 559
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
204-569 |
3.33e-13 |
|
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: 70.82 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 204 SPALFIYTSGTTGLPKPAILTHeRVLQMSKMLSLS--GATADDVVYTVLPLYHVMGLVVgILGCLDLGATCVLAPKfsTS 281
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTA-ANLLASAAGLHSrlGFGGGDSWLLSLPLYHVGGLAI-LVRSLLAGAELVLLER--NQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 282 CFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNG-LRADVWETFQQRfgPIRIWEVYGSTEgnMGLVNY 360
Cdd:cd17630 77 ALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGApIPPELLERAADR--GIPLYTTYGMTE--TASQVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 361 VGRCGALGKMSCllrmlspfelvqfdmeaAEPVRDNQgfcipVGLGEPGLLLTKVVSQqpFVGYRGPRELSERklvrnvr 440
Cdd:cd17630 153 TKRPDGFGRGGV-----------------GVLLPGRE-----LRIVEDGEIWVGGASL--AMGYLRGQLVPEF------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 441 qSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPGCE-GKVGMAAVQLAP 519
Cdd:cd17630 202 -NEDGWFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVG--VPDEElGQRPVAVIVGRG 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1007386236 520 GQtfDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKtRLVREGF 569
Cdd:cd17630 279 PA--DPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDR-RALRAWL 325
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
188-280 |
6.97e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 71.17 E-value: 6.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 188 PSHPVPADLRAGITW-----RSPALFIYTSGTTGLPKPAILTHERVlqMSKMLSLSGA---TADDVVYTVLPLYHVMGLV 259
Cdd:PRK07787 108 PHVPVRLHARSWHRYpepdpDAPALIVYTSGTTGPPKGVVLSRRAI--AADLDALAEAwqwTADDVLVHGLPLFHVHGLV 185
|
90 100
....*....|....*....|.
gi 1007386236 260 VGILGCLDLGATCVLAPKFST 280
Cdd:PRK07787 186 LGVLGPLRIGNRFVHTGRPTP 206
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
193-567 |
8.20e-13 |
|
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: 70.94 E-value: 8.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 193 PADLR-AGITWRSPALFIYTSGTTGLPKPAILTH-ERVLQMSKMLSLSGATADDVVYTVLPLYHVMGLVV-GILGCLDLG 269
Cdd:COG1021 173 PADLSePRPDPDDVAFFQLSGGTTGLPKLIPRTHdDYLYSVRASAEICGLDADTVYLAALPAAHNFPLSSpGVLGVLYAG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 270 ATCVLAPKFSTscfwDDC----RQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLaMGNG---LRADVWETFQQRFGpI 342
Cdd:COG1021 253 GTVVLAPDPSP----DTAfpliERERVTVTALVPPLALLWLDAAERSRYDLSSLRV-LQVGgakLSPELARRVRPALG-C 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 343 RIWEVYGSTEgnmGLVNY----------VGRCGalgkmscllRMLSPFELVQfdmeaaepVRDNQGfcIPVGLGEPGLLL 412
Cdd:COG1021 327 TLQQVFGMAE---GLVNYtrlddpeeviLTTQG---------RPISPDDEVR--------IVDEDG--NPVPPGEVGELL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 413 TKvvsqQP--FVGY-RGPRElserklvrNVRQ-SGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLs 488
Cdd:COG1021 385 TR----GPytIRGYyRAPEH--------NARAfTPDGFYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLL- 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 489 qvdfLQQVNVYGVCVpgcegkVGM----------AAVQLApGQTFDGEKLYQHVRAW-LPAYATPHFIRIQDAMEVTSTF 557
Cdd:COG1021 452 ----LAHPAVHDAAV------VAMpdeylgerscAFVVPR-GEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVG 520
|
410
....*....|
gi 1007386236 558 KLMKTRLVRE 567
Cdd:COG1021 521 KIDKKALRAA 530
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
210-564 |
1.69e-12 |
|
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: 70.02 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 210 YTSGTTGLPKPAILTHERVLQMSKMLSLSGATADDVVY-TVLPLYHVMGLVvGILGCLDLGATCVLAPKFSTSCFWDDCR 288
Cdd:cd12118 140 YTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYlWTLPMFHCNGWC-FPWTVAAVGGTNVCLRKVDAKAIYDLIE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 289 QHGVTVILYVGELLRYLCNIPqqPEDR---THTVRLAMGNGL-RADVWETFQQrfGPIRIWEVYGSTEG-NMGLVNY--- 360
Cdd:cd12118 219 KHKVTHFCGAPTVLNMLANAP--PSDArplPHRVHVMTAGAPpPAAVLAKMEE--LGFDVTHVYGLTETyGPATVCAwkp 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 361 -------------VGRCGalgkmsclLRMLSPFELVQFDMEAAEPV-RDNQGfcipvgLGEpgllltkVVsqqpFVG--- 423
Cdd:cd12118 295 ewdelpteerarlKARQG--------VRYVGLEEVDVLDPETMKPVpRDGKT------IGE-------IV----FRGniv 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 424 ----YRGPRelSERKLVRnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVY 499
Cdd:cd12118 350 mkgyLKNPE--ATAEAFR------GGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVV 421
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1007386236 500 GVCVPgCEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDaMEVTSTFKLMKTRL 564
Cdd:cd12118 422 ARPDE-KWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVL 484
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
203-279 |
3.28e-12 |
|
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: 69.19 E-value: 3.28e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1007386236 203 RSPALFIYTSGTTGLPKPAILTHERVL-QMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFS 279
Cdd:cd05931 149 DDIAYLQYTSGSTGTPKGVVVTHRNLLaNVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAA 226
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
173-498 |
3.33e-12 |
|
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: 68.45 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 173 PTPGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQM-SKMLSLSGATADDVVYTVLP 251
Cdd:TIGR01733 90 VLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLlAWLARRYGLDPDDRVLQFAS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 252 LYHVMGlVVGILGCLDLGATCVLAPKFSTSC---FWDDC-RQHGVTVILYVGELLRYLCniPQQPEDRTH--TVRLAmGN 325
Cdd:TIGR01733 170 LSFDAS-VEEIFGALLAGATLVVPPEDEERDdaaLLAALiAEHPVTVLNLTPSLLALLA--AALPPALASlrLVILG-GE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 326 GLRADVWETFQQRFGPIRIWEVYGSTEGNMGlvnyvgrcgalgkmscllrmlSPFELVQFDMEAAEPVR------DNQGF 399
Cdd:TIGR01733 246 ALTPALVDRWRARGPGARLINLYGPTETTVW---------------------STATLVDPDDAPRESPVpigrplANTRL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 400 CI------PVGLGEPGLLLtkVVSQQPFVGYRGPRELSERKLVRNVRQSGD--VYYNTGDVLAMDREGFLYFRDRLGDTF 471
Cdd:TIGR01733 305 YVldddlrPVPVGVVGELY--IGGPGVARGYLNRPELTAERFVPDPFAGGDgaRLYRTGDLVRYLPDGNLEFLGRIDDQV 382
|
330 340
....*....|....*....|....*..
gi 1007386236 472 RWKGENVSTHEVEGVLSQVDFLQQVNV 498
Cdd:TIGR01733 383 KIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
175-564 |
1.15e-11 |
|
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: 67.30 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 175 PGVGALGAALDAAPSHPVPADLRAGITWRSPALFIYTSGTTGLPKPAILTH----ERVLQMSKMLSLsgaTADDVVYTVL 250
Cdd:cd17646 110 PAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHagivNRLLWMQDEYPL---GPGDRVLQKT 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 251 PL-YHVMglVVGILGCLDLGATCVLA-------PKFSTSCFwddcRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLA 322
Cdd:cd17646 187 PLsFDVS--VWELFWPLVAGARLVVArpgghrdPAYLAALI----REHGVTTCHFVPSMLRVFLAEPAAGSCASLRRVFC 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 323 MGNGLRADVWETFQQRFGpIRIWEVYGSTEGNMGLVNYVGRCGALGKMSCLLRMLSPFELVQFDmEAAEPVrdnqgfciP 402
Cdd:cd17646 261 SGEALPPELAARFLALPG-AELHNLYGPTEAAIDVTHWPVRGPAETPSVPIGRPVPNTRLYVLD-DALRPV--------P 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 403 VGL-GE---PGLLLTKvvsqqpfvGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENV 478
Cdd:cd17646 331 VGVpGElylGGVQLAR--------GYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRV 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 479 STHEVEGVLsqvdfLQQVNVYGVCV----PGCEGKVGMAAVQLAPGQT-FDGEKLYQHVRAWLPAYATP-HFIRIqDAME 552
Cdd:cd17646 403 EPGEIEAAL-----AAHPAVTHAVVvaraAPAGAARLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPaAFVVL-DALP 476
|
410
....*....|..
gi 1007386236 553 VTSTFKLMKTRL 564
Cdd:cd17646 477 LTANGKLDRAAL 488
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
210-567 |
2.59e-11 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 66.16 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 210 YTSGTTGLPKPAILTHERVLQ--MSKMLSLSGATADDVV-YTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSCFWDD 286
Cdd:PLN02330 191 FSSGTTGISKGVMLTHRNLVAnlCSSLFSVGPEMIGQVVtLGLIPFFHIYGITGICCATLRNKGKVVVMSRFELRTFLNA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 287 CRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRL----AMGNGLRADVWETFQQRFGPIRIWEVYGSTEgnmglvnyvg 362
Cdd:PLN02330 271 LITQEVSFAPIVPPIILNLVKNPIVEEFDLSKLKLqaimTAAAPLAPELLTAFEAKFPGVQVQEAYGLTE---------- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 363 rcgalgkMSCLlrmlspfELVQFDMEAAEPV--RDNQGFCIP---VGLGEP--GLLLTK-------VVSQQPFVGYRGPR 428
Cdd:PLN02330 341 -------HSCI-------TLTHGDPEKGHGIakKNSVGFILPnleVKFIDPdtGRSLPKntpgelcVRSQCVMQGYYNNK 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 429 ELSERKLvrnvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVygVCVPGCE- 507
Cdd:PLN02330 407 EETDRTI------DEDGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAV--VPLPDEEa 478
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 508 GKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKtRLVRE 567
Cdd:PLN02330 479 GEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMR-RLLKE 537
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
193-564 |
2.63e-11 |
|
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: 66.16 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 193 PADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVL-QMSKMLSLSGATADDVVYTVLPLYHVMGlVVGILGCLDLGAT 271
Cdd:cd12116 116 PAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVnFLHSMRERLGLGPGDRLLAVTTYAFDIS-LLELLLPLLAGAR 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 272 CVLAPKFSTS---CFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTvrLAMGNGLRADVWETFQQRFGpiRIWEVY 348
Cdd:cd12116 195 VVIAPRETQRdpeALARLIEAHSITVMQATPATWRMLLDAGWQGRAGLTA--LCGGEALPPDLAARLLSRVG--SLWNLY 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 349 GSTE----GNMGLVNYVGRCGALGKmscllrmlsPFELVQFdmeaaePVRDNQGfcIPVGLGEPGLLLT--KVVSQqpfv 422
Cdd:cd12116 271 GPTEttiwSTAARVTAAAGPIPIGR---------PLANTQV------YVLDAAL--RPVPPGVPGELYIggDGVAQ---- 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 423 GYRGPRELSERKLVRN-VRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVnvyGV 501
Cdd:cd12116 330 GYLGRPALTAERFVPDpFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQA---AV 406
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1007386236 502 CVPGCEGKVGMAA-VQLAPGQTFDGEKLYQHVRAWLPAYATP-HFIRIqDAMEVTSTFKLMKTRL 564
Cdd:cd12116 407 VVREDGGDRRLVAyVVLKAGAAPDAAALRAHLRATLPAYMVPsAFVRL-DALPLTANGKLDRKAL 470
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
144-567 |
4.32e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 65.48 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 144 TFDLRESLEEILPKLQAenirCFYLSHTSPTPGVGALGAALDAAPSHPVPaDLRAGitwrspALFIYTSGTTG------- 216
Cdd:PRK13391 106 KLDVARALLKQCPGVRH----RLVLDGDGELEGFVGYAEAVAGLPATPIA-DESLG------TDMLYSSGTTGrpkgikr 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 217 -LPKPAILTHERVLQMSKMLSlsGATADDVVYTVLPLYHVMGLVVGILGcLDLGATCVLAPKFSTSCFWDDCRQHGVTVI 295
Cdd:PRK13391 175 pLPEQPPDTPLPLTAFLQRLW--GFRSDMVYLSPAPLYHSAPQRAVMLV-IRLGGTVIVMEHFDAEQYLALIEEYGVTHT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 296 LYVGELLRYLCNIPQQPEDR--THTVRLAMGNG--LRADVWETFQQRFGPIrIWEVYGSTEGNMGLV----NYVGRCGAL 367
Cdd:PRK13391 252 QLVPTMFSRMLKLPEEVRDKydLSSLEVAIHAAapCPPQVKEQMIDWWGPI-IHEYYAATEGLGFTAcdseEWLAHPGTV 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 368 GK-MSCLLRMLspfelvqfdmeaaepvrDNQGFCIPVglGEPGLLLTKvvSQQPFVGYRGPRELSErklvrnvRQSGDVY 446
Cdd:PRK13391 331 GRaMFGDLHIL-----------------DDDGAELPP--GEPGTIWFE--GGRPFEYLNDPAKTAE-------ARHPDGT 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 447 YNT-GDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPGCE-GKVGMAAVQLAPGQTFD 524
Cdd:PRK13391 383 WSTvGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFG--VPNEDlGEEVKAVVQPVDGVDPG 460
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1007386236 525 ---GEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKtRLVRE 567
Cdd:PRK13391 461 palAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYK-RLLRD 505
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
205-559 |
5.74e-11 |
|
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: 65.21 E-value: 5.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKpaILTHERVLQMSKMLSLS---GATADDVVYTVLPL---YHVMGLVVG--ILGC----LDLGatc 272
Cdd:cd05970 187 ILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTAKywqNVREGGLHLTVADTgwgKAVWGKIYGqwIAGAavfvYDYD--- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 273 vlapKFSTSCFWDDCRQHGVTVILYVGELLRYLCNipqqpEDRTH----TVRLAM--GNGLRADVWETFQQRFGpIRIWE 346
Cdd:cd05970 262 ----KFDPKALLEKLSKYGVTTFCAPPTIYRFLIR-----EDLSRydlsSLRYCTtaGEALNPEVFNTFKEKTG-IKLME 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 347 VYGSTEGNMGLVNYVG---RCGALGKMScllrmlsPfelvQFDMEaaepVRDNQGFCIPVGlgEPGLLLTKVVSQQP--- 420
Cdd:cd05970 332 GFGQTETTLTIATFPWmepKPGSMGKPA-------P----GYEID----LIDREGRSCEAG--EEGEIVIRTSKGKPvgl 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 421 FVGY-RGPRELSErklvrnVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVY 499
Cdd:cd05970 395 FGGYyKDAEKTAE------VWHDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVT 466
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1007386236 500 GVCVPgCEGKVGMAAVQLA----PGQTFDGEkLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKL 559
Cdd:cd05970 467 GVPDP-IRGQVVKATIVLAkgyePSEELKKE-LQDHVKKVTAPYKYPRIVEFVDELPKTISGKI 528
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
122-564 |
6.34e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 65.15 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 122 RRARAqpgRALLVWtgPGAGSVTFD--LRESLEEILPKLQAENIRCFYLSHT-SPTPGVGALGAALDAAPSHPVPADLRA 198
Cdd:PRK06164 104 GRGRA---RWLVVW--PGFKGIDFAaiLAAVPPDALPPLRAIAVVDDAADATpAPAPGARVQLFALPDPAPPAAAGERAA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 199 GITwrSPALFIYTSGTTGLPK------PAILTHERvlQMSKMLSLSgatADDVVYTVLPLYHVMGLvVGILGCLDLGATC 272
Cdd:PRK06164 179 DPD--AGALLFTTSGTTSGPKlvlhrqATLLRHAR--AIARAYGYD---PGAVLLAALPFCGVFGF-STLLGALAGGAPL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 273 VLAPKFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRA--DVWETFQQRFGPIRiwEVYGS 350
Cdd:PRK06164 251 VCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFASFAPAlgELAALARARGVPLT--GLYGS 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 351 TEgnmglvnyvgrcgaLGKMSCLLRMLSPFEL------VQFDMEAAEPVRDNQ--GFCIPvglGEPGLLltKVVSQQPFV 422
Cdd:PRK06164 329 SE--------------VQALVALQPATDPVSVriegggRPASPEARVRARDPQdgALLPD---GESGEI--EIRAPSLMR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 423 GYRGPRELSERKLVRnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVC 502
Cdd:PRK06164 390 GYLDNPDATARALTD------DGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT 463
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1007386236 503 VpgcEGK-VGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVT---STFKLMKTRL 564
Cdd:PRK06164 464 R---DGKtVPVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTesaNGAKIQKHRL 526
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
210-294 |
6.69e-11 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 65.00 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 210 YTSGTTGLPKPAILTHervlqmsKMLSLSGA------------TADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPK 277
Cdd:PLN02246 186 YSSGTTGLPKGVMLTH-------KGLVTSVAqqvdgenpnlyfHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPK 258
|
90
....*....|....*..
gi 1007386236 278 FSTSCFWDDCRQHGVTV 294
Cdd:PLN02246 259 FEIGALLELIQRHKVTI 275
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
205-569 |
9.78e-11 |
|
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: 64.43 E-value: 9.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTH-----ERVLQMSKMLSLSgatADDVVYTVLPLYHVMGLVVgILGCLDLGATCVL---AP 276
Cdd:cd05968 238 PLMIIYTSGTTGKPKGTVHVHagfplKAAQDMYFQFDLK---PGDLLTWFTDLGWMMGPWL-IFGGLILGATMVLydgAP 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 277 KFSTSC-FWDDCRQHGVTVILYVGELLRYL---CNIPQQPEDRThTVRLAMGNG--LRADVWETFQQRFGpiriwevygs 350
Cdd:cd05968 314 DHPKADrLWRMVEDHEITHLGLSPTLIRALkprGDAPVNAHDLS-SLRVLGSTGepWNPEPWNWLFETVG---------- 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 351 tEGNMGLVNYVGRCGALGKMSC--LLRMLSP--FELVQFDMEAAepVRDNQGFCIPVGLGEpgLLLTKvvsqqPFVGY-R 425
Cdd:cd05968 383 -KGRNPIINYSGGTEISGGILGnvLIKPIKPssFNGPVPGMKAD--VLDESGKPARPEVGE--LVLLA-----PWPGMtR 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 426 GPRELSERKLVRNVRQSGDVYYNtGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPg 505
Cdd:cd05968 453 GFWRDEDRYLETYWSRFDNVWVH-GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHP- 530
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1007386236 506 CEGKVGMAAVQLAPGQTFDG---EKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKtRLVREGF 569
Cdd:cd05968 531 VKGEAIVCFVVLKPGVTPTEalaEELMERVADELGKPLSPERILFVKDLPKTRNAKVMR-RVIRAAY 596
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
203-542 |
1.61e-10 |
|
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: 63.17 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 203 RSP--ALFIYTSGTTGLPKPAILTHERVLQMSK---------------MLSLSGATADDVVYTVLPLYHVMGLVVGILGC 265
Cdd:cd05924 1 RSAddLYILYTGGTTGMPKGVMWRQEDIFRMLMggadfgtgeftpsedAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 266 LDLGATCVLAPKFSTSCFWDDCRQHGVTVILYVGE-LLRYLCNIPQQPEDRTHTVRLAMGNG---LRADVWETFQQRFGP 341
Cdd:cd05924 81 LGGQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDaMARPLIDALRDAGPYDLSSLFAISSGgalLSPEVKQGLLELVPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 342 IRIWEVYGSTEGNMGLVNYVGRCGALGKmscllrmlsPFELVQFDMEaaepVRDNQGFCIPVGLGEPGLLLTK-VVSqqp 420
Cdd:cd05924 161 ITLVDAFGSSETGFTGSGHSAGSGPETG---------PFTRANPDTV----VLDDDGRVVPPGSGGVGWIARRgHIP--- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 421 fVGYRGprelSERKLVRNVRQSGDVYYN-TGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSqvdflQQVNVY 499
Cdd:cd05924 225 -LGYYG----DEAKTAETFPEVDGVRYAvPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALK-----SHPAVY 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1007386236 500 GVCVPGCE----GKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATP 542
Cdd:cd05924 295 DVLVVGRPderwGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLP 341
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
205-559 |
1.89e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.21 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHeRVLQ--MSKMLSLSGATADDVVYTVLPLYHVMGlVVGILGCLDLGATCVLAPK---FS 279
Cdd:PRK12316 657 LAYVIYTSGSTGKPKGAGNRH-RALSnrLCWMQQAYGLGVGDTVLQKTPFSFDVS-VWEFFWPLMSGARLVVAAPgdhRD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 280 TSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGL-- 357
Cdd:PRK12316 735 PAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVth 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 358 ---VNYVGRCGALGKMSCLLRMLspfelvqfdmeaaepVRDNQGFCIPVG-LGE---PGLLLTKvvsqqpfvGYRGPREL 430
Cdd:PRK12316 815 wtcVEEGGDSVPIGRPIANLACY---------------ILDANLEPVPVGvLGElylAGRGLAR--------GYHGRPGL 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 431 SERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLsqvdfLQQVNVYGVCVPGCEGKV 510
Cdd:PRK12316 872 TAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARL-----LEHPWVREAAVLAVDGKQ 946
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1007386236 511 GMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKL 559
Cdd:PRK12316 947 LVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKL 995
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
210-564 |
2.14e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 63.26 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 210 YTSGTTGLPKPAILTHErvlqmSKMLSLS------GATADDVVYTVLPLYHVMGLVvGILGCLDLGATCVLAPKFSTSCF 283
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQ-----SWLHSFDcnvhdfHMKREDSVLIAGTLVHSLFLY-GAISTLYVGQTVHLMRKFIPNQV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 284 WDDCRQHGVTVILYVGELLRYLCNIPQQPEdrtHTVR-LAMGNGLRADVWETFQQRFGPIRIWEVYGSTEgnMGLVNYVG 362
Cdd:PRK07638 224 LDKLETENISVMYTVPTMLESLYKENRVIE---NKMKiISSGAKWEAEAKEKIKNIFPYAKLYEFYGASE--LSFVTALV 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 363 RCGALGKMSCLLRmlsPFELVQFDMEAAEPVRdnqgfCIPvglGEPGLLLTKvvSQQPFVGY----RGPRELSErklvrn 438
Cdd:PRK07638 299 DEESERRPNSVGR---PFHNVQVRICNEAGEE-----VQK---GEIGTVYVK--SPQFFMGYiiggVLARELNA------ 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 439 vrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPgcegKVGMAAVQLA 518
Cdd:PRK07638 360 -----DGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDS----YWGEKPVAII 430
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1007386236 519 PGQTfDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:PRK07638 431 KGSA-TKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
191-559 |
2.81e-10 |
|
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: 62.75 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 191 PVPADLRAGITWRSPALFIYTSGTTGLPKPAILTH----------ERVLQM---SKMLSLSGATADDVVYTVLPlyhvmg 257
Cdd:cd17651 124 GADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHrslanlvawqARASSLgpgARTLQFAGLGFDVSVQEIFS------ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 258 lvvgilgCLDLGATCVLAP---KFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWET 334
Cdd:cd17651 198 -------TLCAGATLVLPPeevRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLTED 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 335 FQQ---RFGPIRIWEVYGSTEgnmglvNYVGRCGALGKMSC-------LLRMLSPFELVQFDmEAAEPVrdnqgfciPVG 404
Cdd:cd17651 271 LREfcaGLPGLRLHNHYGPTE------THVVTALSLPGDPAawpapppIGRPIDNTRVYVLD-AALRPV--------PPG 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 405 lgEPGLLLTKVVSQQPfvGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVE 484
Cdd:cd17651 336 --VPGELYIGGAGLAR--GYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIE 411
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1007386236 485 GVLsqvdfLQQVNVYGVCVPGCEGKVG----MAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKL 559
Cdd:cd17651 412 AAL-----ARHPGVREAVVLAREDRPGekrlVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKL 485
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
205-566 |
3.44e-10 |
|
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: 62.33 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHERVLQ-MSKMLSLSGATADDVVYTVL-PLYHVMGLVvgILGCLDLGATCVLAPKFSTsc 282
Cdd:cd17653 107 LAYIIFTSGSTGIPKGVMVPHRGVLNyVSQPPARLDVGPGSRVAQVLsIAFDACIGE--IFSTLCNGGTLVLADPSDP-- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 283 FWDDCRQhgVTVILYVGELLRYLcniPQQPEDRTHTVRLAmGNGLRADVWETFqqRFGPiRIWEVYGSTEgnmglvnyvg 362
Cdd:cd17653 183 FAHVART--VDALMSTPSILSTL---SPQDFPNLKTIFLG-GEAVPPSLLDRW--SPGR-RLYNAYGPTE---------- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 363 rCgalgKMSCLLRMLSPFELVQFdmeaAEPVRdNQGFCI------PVGLGEPGLLLtkVVSQQPFVGYRGPRELSERKLV 436
Cdd:cd17653 244 -C----TISSTMTELLPGQPVTI----GKPIP-NSTCYIldadlqPVPEGVVGEIC--ISGVQVARGYLGNPALTASKFV 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 437 RNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDflqqvnvygvcvpgceGKVGMAAVQ 516
Cdd:cd17653 312 PDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQ----------------PEVTQAAAI 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1007386236 517 LAPG--------QTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVR 566
Cdd:cd17653 376 VVNGrlvafvtpETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
482-558 |
4.27e-10 |
|
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: 56.01 E-value: 4.27e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1007386236 482 EVEGVLSQVDFLQQVNVYGVCVPGcEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFK 558
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDEL-KGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
188-352 |
4.71e-10 |
|
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: 62.95 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 188 PSHPVPADLRAGitwrSPALFIYTSGTTGLPKPAILTHE----RVLQMSKMLSLsgaTADDVVYTVLPLYHVMGlVVGIL 263
Cdd:COG1020 606 PATNPPVPVTPD----DLAYVIYTSGSTGRPKGVMVEHRalvnLLAWMQRRYGL---GPGDRVLQFASLSFDAS-VWEIF 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 264 GCLDLGATCVLAPK---FSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVrLAMGNGLRADVWETFQQRFG 340
Cdd:COG1020 678 GALLSGATLVLAPPearRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALPSLRLV-LVGGEALPPELVRRWRARLP 756
|
170
....*....|..
gi 1007386236 341 PIRIWEVYGSTE 352
Cdd:COG1020 757 GARLVNLYGPTE 768
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
188-559 |
1.00e-09 |
|
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: 60.84 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 188 PSHPvPADLR-----AGITW------RSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSL-SGATADDVVYTVLPLyHV 255
Cdd:cd17649 69 PEYP-AERLRymledSGAGLllthhpRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAErYGLTPGDRELQFASF-NF 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 256 MGLVVGILGCLDLGATCVLAPK---FSTSCFWDDCRQHGVTVI----LYVGELLRYLCNIPQqpeDRTHTVRL--AMGNG 326
Cdd:cd17649 147 DGAHEQLLPPLICGACVVLRPDelwASADELAEMVRELGVTVLdlppAYLQQLAEEADRTGD---GRPPSLRLyiFGGEA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 327 LRADVWEtfQQRFGPIRIWEVYGSTEGNMGLVNYVGRCGA--LGKMSCLLRMLSPFELVQFDMEAAepvrdnqgfciPVG 404
Cdd:cd17649 224 LSPELLR--RWLKAPVRLFNAYGPTEATVTPLVWKCEAGAarAGASMPIGRPLGGRSAYILDADLN-----------PVP 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 405 LGEPGLLLtkVVSQQPFVGYRGPRELS-ERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEV 483
Cdd:cd17649 291 VGVTGELY--IGGEGLARGYLGRPELTaERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEI 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1007386236 484 EGVLSQVDFLQQVNVYGVCVPGCEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATP-HFIRIqDAMEVTSTFKL 559
Cdd:cd17649 369 EAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQPELRAQLRTALRASLPDYMVPaHLVFL-ARLPLTPNGKL 444
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
203-564 |
1.44e-09 |
|
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: 60.56 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 203 RSPALFIYTSGTTGLPKPAILTHERVLQMSKMLS--LSGATADDVVYTVLPlyhvMGLVVGILGCL----DLGAtCVLA- 275
Cdd:cd05928 174 QEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGryWLDLTASDIMWNTSD----TGWIKSAWSSLfepwIQGA-CVFVh 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 276 --PKFSTSCFWDDCRQHGVTVILYVGELLRYLCnipQQPEDRTHTVRL----AMGNGLRADVWETFQQRFGpIRIWEVYG 349
Cdd:cd05928 249 hlPRFDPLVILKTLSSYPITTFCGAPTVYRMLV---QQDLSSYKFPSLqhcvTGGEPLNPEVLEKWKAQTG-LDIYEGYG 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 350 STEGNMGLVNYVG---RCGALGKMScllrmlSPFElVQfdmeaaepVRDNQGFCIPVGlgEPGLLLTKVVSQQP---FVG 423
Cdd:cd05928 325 QTETGLICANFKGmkiKPGSMGKAS------PPYD-VQ--------IIDDNGNVLPPG--TEGDIGIRVKPIRPfglFSG 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 424 YRGPRElserKLVRNVRqsGDvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCV 503
Cdd:cd05928 388 YVDNPE----KTAATIR--GD-FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPD 460
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1007386236 504 PgCEGKVGMAAVQLAPG-QTFDGEKL----YQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:cd05928 461 P-IRGEVVKAFVVLAPQfLSHDPEQLtkelQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
205-564 |
3.39e-09 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 59.64 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSGA-----TADDVVYTVLPLYHVMGLvVGILGCLDLGATCVLAPKfS 279
Cdd:PRK05857 171 PLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKEGLnwvtwVVGETTYSPLPATHIGGL-WWILTCLMHGGLCVTGGE-N 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 280 TSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLR---ADVweTFQQRFGpIRIWEVYGSTE---- 352
Cdd:PRK05857 249 TTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRaiaADV--RFIEATG-VRTAQVYGLSEtgct 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 353 -----GNMGLVNYVgRCGALGKmscllrmlsPFELVQFDMEAAepvrDNQGFCIPVGLGEPGLLLTKVVSQQPFVGYRGP 427
Cdd:PRK05857 326 alclpTDDGSIVKI-EAGAVGR---------PYPGVDVYLAAT----DGIGPTAPGAGPSASFGTLWIKSPANMLGYWNN 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 428 RELSERKLVrnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCE 507
Cdd:PRK05857 392 PERTAEVLI-------DGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFG 464
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1007386236 508 GKVGMAAVQLAPGQTFDGEKLYQ----HVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:PRK05857 465 ALVGLAVVASAELDESAARALKHtiaaRFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
206-281 |
3.65e-09 |
|
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: 59.38 E-value: 3.65e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVL-QMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTS 281
Cdd:cd05914 92 ALINYTSGTTGNSKGVMLTYRNIVsNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSA 168
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
204-559 |
4.88e-09 |
|
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: 58.86 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 204 SPALFIYTSGTTGLPKPAILTHERVLQM-SKMLSLSGATADDVVYtvlpLYHVMGL---VVGILGCLDLGATCVLAPKF- 278
Cdd:cd17643 94 DLAYVIYTSGSTGRPKGVVVSHANVLALfAATQRWFGFNEDDVWT----LFHSYAFdfsVWEIWGALLHGGRLVVVPYEv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 279 --STSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGPIRIWEV--YGSTE 352
Cdd:cd17643 170 arSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLALRYVIfgGEALEAAMLRPWAGRFGLDRPQLVnmYGITE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 353 GNMgLVNYvgrcgalgkmscllRMLSPFELVQFDMEA-AEP-------VRDNQGfcIPVGLGEPGLLLtkVVSQQPFVGY 424
Cdd:cd17643 250 TTV-HVTF--------------RPLDAADLPAAAASPiGRPlpglrvyVLDADG--RPVPPGVVGELY--VSGAGVARGY 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 425 RGPRELSERKLVRN-VRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVyGVCV 503
Cdd:cd17643 311 LGRPELTAERFVANpFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAV-IVRE 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1007386236 504 PGCEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKL 559
Cdd:cd17643 390 DEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKL 445
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
206-487 |
4.94e-09 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 59.06 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVLQMSKM-LSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLA-----PKFS 279
Cdd:PRK06334 186 AVILFTSGTEKLPKGVPLTHANLLANQRAcLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVVFAynplyPKKI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 280 TScFWDDCRqhgVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGPIRIWEVYGSTEGNMgl 357
Cdd:PRK06334 266 VE-MIDEAK---VTFLGSTPVFFDYILKTAKKQESCLPSLRFVVigGDAFKDSLYQEALKTFPHIQLRQGYGTTECSP-- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 358 VNYVGRCGALGKMSCllrmlspfelVQFDMEAAEPVRDNQGFCIPVGLGEPGLLLTKVVSQqpFVGYrgpreLSERKLVR 437
Cdd:PRK06334 340 VITINTVNSPKHESC----------VGMPIRGMDVLIVSEETKVPVSSGETGLVLTRGTSL--FSGY-----LGEDFGQG 402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1007386236 438 NVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVL 487
Cdd:PRK06334 403 FVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESIL 452
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
206-564 |
8.25e-09 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 58.49 E-value: 8.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHE----RVLQMSKML--SLSGATADDVVYTV--LPLYHVMGLVVGILGCLDLGATCVLAPK 277
Cdd:PRK07059 207 AFLQYTGGTTGVSKGATLLHRnivaNVLQMEAWLqpAFEKKPRPDQLNFVcaLPLYHIFALTVCGLLGMRTGGRNILIPN 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 278 -FSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAMGNGL---RAdVWETFQQRFG-PIRiwEVYGSTE 352
Cdd:PRK07059 287 pRDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMavqRP-VAERWLEMTGcPIT--EGYGLSE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 353 gnmglVNYVGRCgalgkmscllrmlSPFELVQFDMEAAEP-------VRDNQGFCIPvgLGEPGLLLTKvvSQQPFVGYR 425
Cdd:PRK07059 364 -----TSPVATC-------------NPVDATEFSGTIGLPlpstevsIRDDDGNDLP--LGEPGEICIR--GPQVMAGYW 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 426 GPRELSERKLvrnvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPG 505
Cdd:PRK07059 422 NRPDETAKVM------TADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEH 495
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1007386236 506 CEGKVGMAAVQLAPGQTfdGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:PRK07059 496 SGEAVKLFVVKKDPALT--EEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
204-550 |
8.61e-09 |
|
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: 57.31 E-value: 8.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 204 SPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSGATADDVVY-TVLPLYHVmGLVVGILGCLDLGATCVLAPKFSTSC 282
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFlNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDAEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 283 FWDDCRQHGVTVILYVGELLRylcNIPQQPEDRTHTVRlamgnGLRADVweTFQQRFGPIRIWEV--------YGSTEGn 354
Cdd:cd17636 80 VLELIEAERCTHAFLLPPTID---QIVELNADGLYDLS-----SLRSSP--AAPEWNDMATVDTSpwgrkpggYGQTEV- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 355 MGLV--NYVGRC--GALGKMS--CLLRMLspfelvqfDMEAAEpvrdnqgfcipVGLGEPGllltKVVSQQPFV--GYRG 426
Cdd:cd17636 149 MGLAtfAALGGGaiGGAGRPSplVQVRIL--------DEDGRE-----------VPDGEVG----EIVARGPTVmaGYWN 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 427 PRELserklvrNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGC 506
Cdd:cd17636 206 RPEV-------NARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRW 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1007386236 507 EGKVgMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDA 550
Cdd:cd17636 279 AQSV-KAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADA 321
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
205-559 |
1.58e-08 |
|
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: 57.09 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHERVLQMskmlslsgataddvVYTVLPLYHVMGLVVGILG-------------CLDL--G 269
Cdd:cd17650 95 LAYVIYTSGTTGKPKGVMVEHRNVAHA--------------AHAWRREYELDSFPVRLLQmasfsfdvfagdfARSLlnG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 270 ATCVLAP---KFSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGP-IR 343
Cdd:cd17650 161 GTLVICPdevKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSAMRLLIvgSDGCKAQDFKTLAARFGQgMR 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 344 IWEVYGSTEGNMGLVNYVGRCGALGKmSCLLRMLSPFELVQFDM--EAAEPVrdnqgfciPVGL-GEPGLLLTKVVSqqp 420
Cdd:cd17650 241 IINSYGVTEATIDSTYYEEGRDPLGD-SANVPIGRPLPNTAMYVldERLQPQ--------PVGVaGELYIGGAGVAR--- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 421 fvGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVyg 500
Cdd:cd17650 309 --GYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVV-- 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1007386236 501 VCVPGCEGKVGMAAVqLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKL 559
Cdd:cd17650 385 AVREDKGGEARLCAY-VVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
191-519 |
2.19e-08 |
|
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: 57.08 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 191 PVPADLRAGITWRSPALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSGATADDVVYTV--LPLYHVMGLVVgILGCLDL 268
Cdd:cd17632 211 PPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITLnfMPMSHIAGRIS-LYGTLAR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 269 GATCVLAPKFSTSCFWDD---CRQHGVTVILYVGELL--RYlcnipQQPEDR---THTVRLAMGNGLRADVWE------- 333
Cdd:cd17632 290 GGTAYFAAASDMSTLFDDlalVRPTELFLVPRVCDMLfqRY-----QAELDRrsvAGADAETLAERVKAELRErvlggrl 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 334 ---------------TFQQRFGPIRIWEVYGSTEGNMGLVN-YVGRCGALGkmsclLRMLSPFELVQFDMEAAEPvrdnq 397
Cdd:cd17632 365 laavcgsaplsaemkAFMESLLDLDLHDGYGSTEAGAVILDgVIVRPPVLD-----YKLVDVPELGYFRTDRPHP----- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 398 gfcipvglgePGLLLTKvvSQQPFVGY-RGPRELSErklVRNvrqsGDVYYNTGDVLAM---DRegfLYFRDRLGDTFRW 473
Cdd:cd17632 435 ----------RGELLVK--TDTLFPGYyKRPEVTAE---VFD----EDGFYRTGDVMAElgpDR---LVYVDRRNNVLKL 492
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1007386236 474 -KGENVSTHEVEGVLSQVDFLQQVNVYG---------VCVPGCEGKVGMAAVQLAP 519
Cdd:cd17632 493 sQGEFVTVARLEAVFAASPLVRQIFVYGnserayllaVVVPTQDALAGEDTARLRA 548
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
206-564 |
3.81e-08 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 56.37 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTH-ERVLQMSKMLSLSGATADD----------VVYTVLPLYHVMGLVVGILGCLDLGATCVL 274
Cdd:PRK12492 210 AVLQYTGGTTGLAKGAMLTHgNLVANMLQVRACLSQLGPDgqplmkegqeVMIAPLPLYHIYAFTANCMCMMVSGNHNVL 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 275 A--PKfSTSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRL--AMGNGLRADVWETFQQRFGpIRIWEVYGS 350
Cdd:PRK12492 290 ItnPR-DIPGFIKELGKWRFSALLGLNTLFVALMDHPGFKDLDFSALKLtnSGGTALVKATAERWEQLTG-CTIVEGYGL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 351 TEgnmglVNYVGRCGALGKMSCLLRMLSPFElvqfdmEAAEPVRDNQGFCIPvgLGEPGLLLTKvvSQQPFVGYRGPREL 430
Cdd:PRK12492 368 TE-----TSPVASTNPYGELARLGTVGIPVP------GTALKVIDDDGNELP--LGERGELCIK--GPQVMKGYWQQPEA 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 431 SERKLvrnvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGKV 510
Cdd:PRK12492 433 TAEAL------DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAV 506
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1007386236 511 GMAAVQLAPGQTFdgEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:PRK12492 507 KLFVVARDPGLSV--EELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
203-550 |
5.92e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 55.66 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 203 RSP--ALFIYTSGTTGLPKPAILTHE--RVLQMSKMLSLSGATADD--------------VVYTVLPLYHVMGLvVGILG 264
Cdd:PRK07798 161 RSPddLYLLYTGGTTGMPKGVMWRQEdiFRVLLGGRDFATGEPIEDeeelakraaagpgmRRFPAPPLMHGAGQ-WAAFA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 265 CLDLGATCVLAP--KFSTSCFWDDCRQHGVTVILYVGE-----LLRYLcnipqQPEDRTHTVRL-AMGNG---LRADVWE 333
Cdd:PRK07798 240 ALFSGQTVVLLPdvRFDADEVWRTIEREKVNVITIVGDamarpLLDAL-----EARGPYDLSSLfAIASGgalFSPSVKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 334 TFQQRFGPIRIWEVYGSTE-GNMGLVNYVGRCGALGKMScllrmlspfelvqFDMEAAEPVRDNQGFCIPVGLGEPGLLl 412
Cdd:PRK07798 315 ALLELLPNVVLTDSIGSSEtGFGGSGTVAKGAVHTGGPR-------------FTIGPRTVVLDEDGNPVEPGSGEIGWI- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 413 tkvvSQQPFV--GYRGPRELSER--KLVRNVRqsgdvYYNTGDVLAMDREGF--LYFRDRL----GdtfrwkGENVSTHE 482
Cdd:PRK07798 381 ----ARRGHIplGYYKDPEKTAEtfPTIDGVR-----YAIPGDRARVEADGTitLLGRGSVcintG------GEKVFPEE 445
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1007386236 483 VEGVL-SQVDflqqvnVYGVCVPGCE----GKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDA 550
Cdd:PRK07798 446 VEEALkAHPD------VADALVVGVPderwGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDE 512
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
210-567 |
6.26e-08 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 55.59 E-value: 6.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 210 YTSGTTGLPKPAILTHERVL--------QMskmlslsGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVL-APKFS- 279
Cdd:PRK08315 206 YTSGTTGFPKGATLTHRNILnngyfigeAM-------KLTEEDRLCIPVPLYHCFGMVLGNLACVTHGATMVYpGEGFDp 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 280 ------------TSCfwddcrqHGV-TviLYVGELlrylcNIPQQPE-D----RThtvrlamgnGLRA------DVWETF 335
Cdd:PRK08315 279 latlaaveeercTAL-------YGVpT--MFIAEL-----DHPDFARfDlsslRT---------GIMAgspcpiEVMKRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 336 QQRFGPIRIWEVYGSTEGNMGL------------VNYVGRCGalgkmscllrmlsPF-ELVQFDMEAAEPVrdnqgfciP 402
Cdd:PRK08315 336 IDKMHMSEVTIAYGMTETSPVStqtrtddplekrVTTVGRAL-------------PHlEVKIVDPETGETV--------P 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 403 VglGEPGLLLTKvvsqqpfvGYrgprelserklvrNVRQSgdvYYN----------------TGDVLAMDREGFLYFRDR 466
Cdd:PRK08315 395 R--GEQGELCTR--------GY-------------SVMKG---YWNdpektaeaidadgwmhTGDLAVMDEEGYVNIVGR 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 467 LGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPgCE--GKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHF 544
Cdd:PRK08315 449 IKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVG--VP-DEkyGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRY 525
|
410 420
....*....|....*....|...
gi 1007386236 545 IRIQDAMEVTSTFKLMKTRLvRE 567
Cdd:PRK08315 526 IRFVDEFPMTVTGKIQKFKM-RE 547
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
206-564 |
6.33e-08 |
|
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: 55.48 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVLQMSKMLS--LSGATADDVVYTVLPLY----HVMGLVVGILGcldlGATCVLAP--- 276
Cdd:cd17648 97 AYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSerYFGRDNGDEAVLFFSNYvfdfFVEQMTLALLN----GQKLVVPPdem 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 277 KFSTSCFWDDCRQHGVTvilyvgellrYLCNIP---QQPE--DRTHTVR-LAMGNGLRADVWETFQQRFgPIRIWEVYGS 350
Cdd:cd17648 173 RFDPDRFYAYINREKVT----------YLSGTPsvlQQYDlaRLPHLKRvDAAGEEFTAPVFEKLRSRF-AGLIINAYGP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 351 TEgnmglvnyvgrcgalgkmSCLLRMLSPFELVQ-FDMEAAEPVRDNQGFC-------IPVG-LGE---------PGLLL 412
Cdd:cd17648 242 TE------------------TTVTNHKRFFPGDQrFDKSLGRPVRNTKCYVlndamkrVPVGaVGElylggdgvaRGYLN 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 413 TKVVSQQPFVgyRGP-RELSERKLVRNVRqsgdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVD 491
Cdd:cd17648 304 RPELTAERFL--PNPfQTEQERARGRNAR-----LYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYP 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 492 FLQQVNVygvcVPGCEGKVGMAAVQ--------LAPGqTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTR 563
Cdd:cd17648 377 GVRECAV----VAKEDASQAQSRIQkylvgyylPEPG-HVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRA 451
|
.
gi 1007386236 564 L 564
Cdd:cd17648 452 L 452
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
194-564 |
7.49e-08 |
|
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: 55.02 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 194 ADLRAGITWRS-PALFIYTSGTTGLPKPAILTHERVL-------------QMSKMLSLSGATADDVVYTV-LPLYHvmG- 257
Cdd:cd12115 95 AQARLVLTDPDdLAYVIYTSGSTGRPKGVAIEHRNAAaflqwaaaafsaeELAGVLASTSICFDLSVFELfGPLAT--Gg 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 258 ---LVVGILGCLDLGATCvlapkfstscfwddcrqhGVTVILYVGELLRYLCNIPQQPEDrTHTVRLAmGNGLRADVWET 334
Cdd:cd12115 173 kvvLADNVLALPDLPAAA------------------EVTLINTVPSAAAELLRHDALPAS-VRVVNLA-GEPLPRDLVQR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 335 FQQRFGPIRIWEVYGSTEGNMGLVNYVGRCGALGKMScLLRMLSPFELVQFDmeaaepvrdnqGFCIPVGLGEPGLLLT- 413
Cdd:cd12115 233 LYARLQVERVVNLYGPSEDTTYSTVAPVPPGASGEVS-IGRPLANTQAYVLD-----------RALQPVPLGVPGELYIg 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 414 -KVVSQqpfvGYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDf 492
Cdd:cd12115 301 gAGVAR----GYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIP- 375
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1007386236 493 lqQVN--VYGVCVPGCEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:cd12115 376 --GVReaVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
204-276 |
1.35e-07 |
|
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: 54.60 E-value: 1.35e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1007386236 204 SPALFIYTSGTTGLPKPAILTHERVLQMSKMLS-LSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAP 276
Cdd:cd05906 168 DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIqHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVP 241
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
206-564 |
1.98e-07 |
|
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: 53.87 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTSC--- 282
Cdd:cd17655 140 AYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDgqa 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 283 FWDDCRQHGVTVILYVGELLRYLCNIPQQPEdrtHTVR--LAMGNGLRADVWETFQQRFGP-IRIWEVYGSTEGNMGlvn 359
Cdd:cd17655 220 LTQYIRQNRITIIDLTPAHLKLLDAADDSEG---LSLKhlIVGGEALSTELAKKIIELFGTnPTITNAYGPTETTVD--- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 360 yvgrcgalgkmsCLLRMLSPFELVQFDMEAAEPVRDNQGFCI-----PVGLGEPGLLLtkVVSQQPFVGYRGPRELSERK 434
Cdd:cd17655 294 ------------ASIYQYEPETDQQVSVPIGKPLGNTRIYILdqygrPQPVGVAGELY--IGGEGVARGYLNRPELTAEK 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 435 LVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVygVCVPGCEGKVGMAA 514
Cdd:cd17655 360 FVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVV--IARKDEQGQNYLCA 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1007386236 515 VqLAPGQTFDGEKLYQHVRAWLPAYATP-HFIRIqDAMEVTSTFKLMKTRL 564
Cdd:cd17655 438 Y-IVSEKELPVAQLREFLARELPDYMIPsYFIKL-DEIPLTPNGKVDRKAL 486
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
205-549 |
2.15e-07 |
|
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: 53.62 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHER-VLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCL-DLGATC--VLAPKFst 280
Cdd:cd05910 87 PAAILFTSGSTGTPKGVVYRHGTfAAQIDALRQLYGIRPGEVDLATFPLFALFGPALGLTSVIpDMDPTRpaRADPQK-- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 281 scFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVR--LAMGNGLRADVWETFQQRFGP-IRIWEVYGSTE----- 352
Cdd:cd05910 165 --LVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRrvLSAGAPVPIALAARLRKMLSDeAEILTPYGATEalpvs 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 353 --GNMGLVNYVGRCGALGKMSCLLRMLSPFELVQFDMEAAEPVRDNQGFCIPVG-LGEpgLLLTKVVSQQPFVGyrgpRE 429
Cdd:cd05910 243 siGSRELLATTTAATSGGAGTCVGRPIPGVRVRIIEIDDEPIAEWDDTLELPRGeIGE--ITVTGPTVTPTYVN----RP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 430 LSERkLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCEGK 509
Cdd:cd05910 317 VATA-LAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLP 395
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1007386236 510 VGmaAVQLAPGQTFDGEKLYQHVRAWLPAYatPHFIRIQD 549
Cdd:cd05910 396 VL--CVEPLPGTITPRARLEQELRALAKDY--PHTQRIGR 431
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
204-559 |
2.56e-07 |
|
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: 53.41 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 204 SPALFIYTSGTTGLPKPAILTHERVLQMSKMLS-LSGATADDVVYTvlplYHVMGL---VVGILGCLDLGATCVLAPKFS 279
Cdd:cd17652 94 NLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIaAFDVGPGSRVLQ----FASPSFdasVWELLMALLAGATLVLAPAEE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 280 TSC---FWDDCRQHGVTVILYVGELLRYLcNIPQQPEDRTHTVrlaMGNGLRADVwetfQQRFGPIR-IWEVYGSTEGNM 355
Cdd:cd17652 170 LLPgepLADLLREHRITHVTLPPAALAAL-PPDDLPDLRTLVV---AGEACPAEL----VDRWAPGRrMINAYGPTETTV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 356 GLVnyVGRCGALGKMSCLLRMLSPFELVQFDmEAAEPVrdnqgfciPVG------LGEPGLLltkvvsqqpfVGYRGPRE 429
Cdd:cd17652 242 CAT--MAGPLPGGGVPPIGRPVPGTRVYVLD-ARLRPV--------PPGvpgelyIAGAGLA----------RGYLNRPG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 430 LSERKLVRN-VRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVnVYGVCVPGCEG 508
Cdd:cd17652 301 LTAERFVADpFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEA-VVVVRDDRPGD 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1007386236 509 KVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKL 559
Cdd:cd17652 380 KRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKL 430
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
206-490 |
4.66e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 52.79 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVL-QMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPK------- 277
Cdd:PRK08043 368 ALILFTSGSEGHPKGVVHSHKSLLaNVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSplhyriv 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 278 ------------FSTSCFWDDCRQHGVTvilYVGELLRYLCNIPQQPEDRTHTvrlamgnglradVWetfQQRFGpIRIW 345
Cdd:PRK08043 448 pelvydrnctvlFGTSTFLGNYARFANP---YDFARLRYVVAGAEKLQESTKQ------------LW---QDKFG-LRIL 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 346 EVYGSTEG------NMGLVNYVGRCGalgkmscllRMLSpfelvqfDMEAAepvrdnqgfCIPV-GLGEPGLLLTKvvsq 418
Cdd:PRK08043 509 EGYGVTECapvvsiNVPMAAKPGTVG---------RILP-------GMDAR---------LLSVpGIEQGGRLQLK---- 559
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1007386236 419 QPFV--GY-----RGPRELSERKLVRNVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQV 490
Cdd:PRK08043 560 GPNImnGYlrvekPGVLEVPTAENARGEMERG--WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGV 636
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
206-566 |
5.74e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.04 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVLQ-MSKMLSLSGATADDVVYTVLPlYHVMGLVVGILGCLDLGATCVLAPK--FSTSC 282
Cdd:PRK12316 2149 AYVIYTSGSTGLPKGVAVSHGALVAhCQAAGERYELSPADCELQFMS-FSFDGAHEQWFHPLLNGARVLIRDDelWDPEQ 2227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 283 FWDDCRQHGVTVILYVGELLRYLCNIPQQpEDRTHTVRLAM--GNGLRADVWETFQQRFGPIRIWEVYGSTEGNMGLVNY 360
Cdd:PRK12316 2228 LYDEMERHGVTILDFPPVYLQQLAEHAER-DGRPPAVRVYCfgGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLW 2306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 361 VGR----CGALG-KMSCLLRMLSPFEL-VQFDMEAaepvrdnQGFCIPVGLGEPGLLLtkvvsqqpfvGYRG-PRELSER 433
Cdd:PRK12316 2307 KCRpqdpCGAAYvPIGRALGNRRAYILdADLNLLA-------PGMAGELYLGGEGLAR----------GYLNrPGLTAER 2369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 434 KLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVygVCVPGCEGKVGMA 513
Cdd:PRK12316 2370 FVPDPFSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVV--VAQDGASGKQLVA 2447
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1007386236 514 AVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLVR 566
Cdd:PRK12316 2448 YVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
195-491 |
5.85e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 52.66 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 195 DLRAGITW----------------------RSPALFIYTSGTTGLPKPAILTHERVL-QMSKMLSLSGATADDVVYTVLP 251
Cdd:PRK06814 763 DVRAQIGLadkikgllagrfplvyfcnrdpDDPAVILFTSGSEGTPKGVVLSHRNLLaNRAQVAARIDFSPEDKVFNALP 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 252 LYHVMGLVVGILGCL-----------------------DLGATCVlapkFSTSCFWD---------DCRQhgvtvilyvg 299
Cdd:PRK06814 843 VFHSFGLTGGLVLPLlsgvkvflypsplhyriipeliyDTNATIL----FGTDTFLNgyaryahpyDFRS---------- 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 300 elLRYLcnipqqpedrthtvrLAMGNGLRADVWETFQQRFGpIRIWEVYGSTEG------NMGLVNyvgRCGALGKmscl 373
Cdd:PRK06814 909 --LRYV---------------FAGAEKVKEETRQTWMEKFG-IRILEGYGVTETapvialNTPMHN---KAGTVGR---- 963
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 374 lrmLSPfelvqfDMEAA-EPVRdnqgfcipvGLGEPGLLLTKvvsqQPFV--GY---RGPRELSERKlvrnvrqsgDVYY 447
Cdd:PRK06814 964 ---LLP------GIEYRlEPVP---------GIDEGGRLFVR----GPNVmlGYlraENPGVLEPPA---------DGWY 1012
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1007386236 448 NTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVD 491
Cdd:PRK06814 1013 DTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELW 1056
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
191-274 |
6.81e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 52.86 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 191 PVPADlragiTWRSPAL------FI-YTSGTTGLPKPAILTHERVLQMSKMLSLS---GATADDVVYTVLPLYHVMGLVV 260
Cdd:PRK05691 152 PALAE-----AWQEPALqpddiaFLqYTSGSTALPKGVQVSHGNLVANEQLIRHGfgiDLNPDDVIVSWLPLYHDMGLIG 226
|
90
....*....|....
gi 1007386236 261 GILGCLDLGATCVL 274
Cdd:PRK05691 227 GLLQPIFSGVPCVL 240
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
193-587 |
7.27e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 52.26 E-value: 7.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 193 PADlragiTWRSPALFiYTSGTTGLPKpAILTHERvlqMSKMLSLSGATADDV----VYT-VLPLYH--------VMGLV 259
Cdd:PRK08162 178 PAD-----EWDAIALN-YTSGTTGNPK-GVVYHHR---GAYLNALSNILAWGMpkhpVYLwTLPMFHcngwcfpwTVAAR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 260 VGILGCLDlgatcvlapKFSTSCFWDDCRQHGVTviLYVGE--LLRYLCNIPQQP-EDRTHTVR-LAMGNGLRADVWETF 335
Cdd:PRK08162 248 AGTNVCLR---------KVDPKLIFDLIREHGVT--HYCGApiVLSALINAPAEWrAGIDHPVHaMVAGAAPPAAVIAKM 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 336 QQRfgPIRIWEVYGSTEgnmglvNY--VGRCGALGKMSCL-------------LRMLSPFELVQFDMEAAEPV-RDNQGf 399
Cdd:PRK08162 317 EEI--GFDLTHVYGLTE------TYgpATVCAWQPEWDALplderaqlkarqgVRYPLQEGVTVLDPDTMQPVpADGET- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 400 cipvgLGE---PGLLLTKvvsqqpfvGYrgpreLSERKLVRNVRQSGdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGE 476
Cdd:PRK08162 388 -----IGEimfRGNIVMK--------GY-----LKNPKATEEAFAGG--WFHTGDLAVLHPDGYIKIKDRSKDIIISGGE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 477 NVSTHEVEGVLSQVDFLQQVNVygVCVPGCE-GKVGMAAVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIqDAMEVTS 555
Cdd:PRK08162 448 NISSIEVEDVLYRHPAVLVAAV--VAKPDPKwGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTS 524
|
410 420 430
....*....|....*....|....*....|..
gi 1007386236 556 TFKLMKtrlvregfnvgivvdplFVLDNRAQS 587
Cdd:PRK08162 525 TGKIQK-----------------FVLREQAKS 539
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
191-270 |
2.07e-06 |
|
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: 50.68 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 191 PVPADLragitwrspALFIYTSGTTGLPKPAILTHERVLQ----MSKML-SLSGATADDVVYTVLPLYHVMGLVVgILGC 265
Cdd:cd05927 111 PKPEDL---------ATICYTSGTTGNPKGVMLTHGNIVSnvagVFKILeILNKINPTDVYISYLPLAHIFERVV-EALF 180
|
....*
gi 1007386236 266 LDLGA 270
Cdd:cd05927 181 LYHGA 185
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
206-564 |
2.34e-06 |
|
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: 50.54 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHER-VLQMSKMLSLSGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPKFSTscFW 284
Cdd:cd05932 140 ATLIYTSGTTGQPKGVMLTFGSfAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESLDT--FV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 285 DDCRQHGVTVILYVGEL-----LRYLCNIPQQPEDRTHTV---------RLAMGNGLRA-------------DVWETFqQ 337
Cdd:cd05932 218 EDVQRARPTLFFSVPRLwtkfqQGVQDKIPQQKLNLLLKIpvvnslvkrKVLKGLGLDQcrlagcgsapvppALLEWY-R 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 338 RFGpIRIWEVYGSTEgNMGL--VNYVGR--CGALGKMScllrmlspfelvqfdmeaaepvrdnQGfcIPVGLGEPGLLLT 413
Cdd:cd05932 297 SLG-LNILEAYGMTE-NFAYshLNYPGRdkIGTVGNAG-------------------------PG--VEVRISEDGEILV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 414 KvvSQQPFVGYRGPRELSERKLvrnvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRW-KGENVSTHEVEGVLSQVDF 492
Cdd:cd05932 348 R--SPALMMGYYKDPEATAEAF------TADGFLRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDR 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 493 LQQVNVYGVCVPGCEGKVGMAAVQLAPGQTFDGEKLYQHVRAWLP---AYATPH-----FIRIQDAMEV-----TSTFKL 559
Cdd:cd05932 420 VEMVCVIGSGLPAPLALVVLSEEARLRADAFARAELEASLRAHLArvnSTLDSHeqlagIVVVKDPWSIdngilTPTLKI 499
|
....*
gi 1007386236 560 MKTRL 564
Cdd:cd05932 500 KRNVL 504
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
206-500 |
2.44e-06 |
|
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: 50.44 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVL-QMSKMLSLSGATADDVVYTVLPLYHVMGLVVG--ILGCldlGATCVLApkfSTSC 282
Cdd:cd17640 91 ATIIYTSGTTGNPKGVMLTHANLLhQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEyfIFAC---GCSQAYT---SIRT 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 283 FWDDCRQHGVTVILYVGELLRYLCN-----IPQQPEDRTHTVRLAM----------GNGLRADVWETFQQRFGpIRIWEV 347
Cdd:cd17640 165 LKDDLKRVKPHYIVSVPRLWESLYSgiqkqVSKSSPIKQFLFLFFLsggifkfgisGGGALPPHVDTFFEAIG-IEVLNG 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 348 YGSTEGNMGLV------NYVGRCGAlgkmscllrmlsPFELVQFDmeaaepVRDNQGfCIPVGLGEPGLLLTKvvSQQPF 421
Cdd:cd17640 244 YGLTETSPVVSarrlkcNVRGSVGR------------PLPGTEIK------IVDPEG-NVVLPPGEKGIVWVR--GPQVM 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 422 VGYRGPRELSERKLvrnvrqSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWK-GENVSTHEVEGVLSQVDFLQQVNVYG 500
Cdd:cd17640 303 KGYYKNPEATSKVL------DSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
206-271 |
2.89e-06 |
|
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: 50.29 E-value: 2.89e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVLQ----MSKMLSlSGATADDVVYTVLPLYHVMGLVVGILgCLDLGAT 271
Cdd:cd17639 91 ACIMYTSGSTGNPKGVMLTHGNLVAgiagLGDRVP-ELLGPDDRYLAYLPLAHIFELAAENV-CLYRGGT 158
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
205-353 |
3.09e-06 |
|
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: 49.96 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHE----RVLQMSKMLSLsgaTADDVVYTVLPLYHVMGlVVGILGCLDLGATCVLAP--KF 278
Cdd:cd12114 128 LAYVIFTSGSTGTPKGVMISHRaalnTILDINRRFAV---GPDDRVLALSSLSFDLS-VYDIFGALSAGATLVLPDeaRR 203
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1007386236 279 STSCFW-DDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVRLAM--GNGLRADVWETFQQRFGPIRIWEVYGSTEG 353
Cdd:cd12114 204 RDPAHWaELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSLRLVLlsGDWIPLDLPARLRALAPDARLISLGGATEA 281
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
206-564 |
3.43e-06 |
|
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: 49.86 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVLQM-SKMLSLSGATADD--VVYTVLPLYhvmGLVVGILGCLDLGATCVLAP---KFS 279
Cdd:cd17645 107 AYVIYTSGSTGLPKGVMIEHHNLVNLcEWHRPYFGVTPADksLVYASFSFD---ASAWEIFPHLTAGAALHVVPserRLD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 280 TSCFWDDCRQHGVTVILyvgeLLRYLCNipQQPEDRTHTVRLAMGNGlraDVWETFQQRfgPIRIWEVYGSTEGNMglvn 359
Cdd:cd17645 184 LDALNDYFNQEGITISF----LPTGAAE--QFMQLDNQSLRVLLTGG---DKLKKIERK--GYKLVNNYGPTENTV---- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 360 yvgrcgalgkmscllrMLSPFELvqfDMEAAEpvrdnqgfcIPVG----------LGEPGLLLTKVVSQQPFV------- 422
Cdd:cd17645 249 ----------------VATSFEI---DKPYAN---------IPIGkpidntrvyiLDEALQLQPIGVAGELCIageglar 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 423 GYRGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVygVC 502
Cdd:cd17645 301 GYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAV--LA 378
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1007386236 503 VPGCEGKVGMAAVQLAPgQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:cd17645 379 KEDADGRKYLVAYVTAP-EEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
206-545 |
4.49e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.96 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVLQ-MSKMLSLSGATADDVVYTVLPlYHVMGLVVGILGCLDLGATCVLAPkfstSCFW 284
Cdd:PRK12316 4697 AYVIYTSGSTGRPKGVAVSHGSLVNhLHATGERYELTPDDRVLQFMS-FSFDGSHEGLYHPLINGASVVIRD----DSLW 4771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 285 DDCR------QHGVTVILYVGELLRYLCNIPQQPEDRTHTVRL-----AMGNGLRADVWETFQqrfgPIRIWEVYGSTEG 353
Cdd:PRK12316 4772 DPERlyaeihEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYcfggeAVAQASYDLAWRALK----PVYLFNGYGPTET 4847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 354 NMGLVNYVGR----CGA----LGKmscLLRMLSPFELvqfdmeaaepvrDNQGFCIPVGLGEPGLLLTKVVSQqpfvGY- 424
Cdd:PRK12316 4848 TVTVLLWKARdgdaCGAaympIGT---PLGNRSGYVL------------DGQLNPLPVGVAGELYLGGEGVAR----GYl 4908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 425 RGPRELSERKLVRNVRQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVygVCVP 504
Cdd:PRK12316 4909 ERPALTAERFVPDPFGAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVV--IAQE 4986
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1007386236 505 GCEGKVGMAAV-----QLAPGQTFDGE---KLYQHVRAWLPAYATP-HFI 545
Cdd:PRK12316 4987 GAVGKQLVGYVvpqdpALADADEAQAElrdELKAALRERLPEYMVPaHLV 5036
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
210-569 |
7.05e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 48.93 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 210 YTSGTTGLPKPAILTHErvlqmSKMLSLSGA--------TADDVVYTVLPLYHVMGLvvGI-LGCLDLGATCVL-APKFS 279
Cdd:PRK07008 183 YTSGTTGNPKGALYSHR-----STVLHAYGAalpdamglSARDAVLPVVPMFHVNAW--GLpYSAPLTGAKLVLpGPDLD 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 280 TSCFWDDCRQHGVTVILYVGELLRYLCNIPQQPEDRTHTVR--LAMGNGLRADVWETFQQRFGpIRIWEVYGSTEgnmgl 357
Cdd:PRK07008 256 GKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRrtVIGGSACPPAMIRTFEDEYG-VEVIHAWGMTE----- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 358 vnyvgrCGALGKMSCLLrmlspFELVQFDMEAAEPVRDNQGFCIpVGL-----GEPGllltkvvSQQPFVG-------YR 425
Cdd:PRK07008 330 ------MSPLGTLCKLK-----WKHSQLPLDEQRKLLEKQGRVI-YGVdmkivGDDG-------RELPWDGkafgdlqVR 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 426 GPRELSerklvRNVRQSG----DVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLsqvdflqqVNVYGV 501
Cdd:PRK07008 391 GPWVID-----RYFRGDAsplvDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVA--------VAHPAV 457
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1007386236 502 CVPGCegkVGMA----------AVQLAPGQTFDGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLvREGF 569
Cdd:PRK07008 458 AEAAC---IACAhpkwderpllVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKL-REQF 531
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
200-566 |
8.24e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 48.74 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 200 ITW---RSPALFIYTSGTTGLPKPAILTHERVLQMskmlSLSGATA----DDVVY--TVLPLYhVMGLVVGILGCLDLGA 270
Cdd:PRK04319 199 IEWtdrEDGAILHYTSGSTGKPKGVLHVHNAMLQH----YQTGKYVldlhEDDVYwcTADPGW-VTGTSYGIFAPWLNGA 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 271 T-CVLAPKFSTSCFWDDCRQHGVTV-----------------------------ILYVGEllrylcniPQQPEdrthTVR 320
Cdd:PRK04319 274 TnVIDGGRFSPERWYRILEDYKVTVwytaptairmlmgagddlvkkydlsslrhILSVGE--------PLNPE----VVR 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 321 LAMgnglradvwETFQQrfgpiRIWEVYGSTE--GNMgLVNYVG---RCGALGKmscllrmlsPFELVqfdmEAAepVRD 395
Cdd:PRK04319 342 WGM---------KVFGL-----PIHDNWWMTEtgGIM-IANYPAmdiKPGSMGK---------PLPGI----EAA--IVD 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 396 NQGFCIPVglGEPGLLLTKVVSQQPFVGYRGPRELSERKLVrnvrqsGDvYYNTGDVLAMDREGFLYFRDRLGDTFRWKG 475
Cdd:PRK04319 392 DQGNELPP--NRMGNLAIKKGWPSMMRGIWNNPEKYESYFA------GD-WYVSGDSAYMDEDGYFWFQGRVDDVIKTSG 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 476 ENVSTHEVEGVLSQVDFLQQVNVYGVCVPgCEGKVGMAAVQLAPGQTFDGE---KLYQHVRAWLPAYATPHFIRIQDAME 552
Cdd:PRK04319 463 ERVGPFEVESKLMEHPAVAEAGVIGKPDP-VRGEIIKAFVALRPGYEPSEElkeEIRGFVKKGLGAHAAPREIEFKDKLP 541
|
410
....*....|....
gi 1007386236 553 VTSTFKLMKtRLVR 566
Cdd:PRK04319 542 KTRSGKIMR-RVLK 554
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
205-283 |
1.08e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 48.22 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHERVLQ----MSKMLSLSGATadDVVYTVLPLYHVMGLVVGILGCLDlGATCVLAPK--F 278
Cdd:PRK05851 154 PAVLQGTAGSTGTPRTAILSPGAVLSnlrgLNARVGLDAAT--DVGCSWLPLYHDMGLAFLLTAALA-GAPLWLAPTtaF 230
|
....*
gi 1007386236 279 STSCF 283
Cdd:PRK05851 231 SASPF 235
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
203-577 |
1.73e-05 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 47.86 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 203 RSPALFIYTSGTTGLPKPAILTHeRVLQMSkmlSLSGATADDVVYT-------VLPLYHVMGLVVGILGCLDlGATCVL- 274
Cdd:PRK05620 181 TTAAAICYSTGTTGAPKGVVYSH-RSLYLQ---SLSLRTTDSLAVThgesflcCVPIYHVLSWGVPLAAFMS-GTPLVFp 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 275 -----APKFSTSCFWDDCRQ-HGVTViLYVGELLRYLCNIPQQPEDRTHTVRLAMGNGLRADVWEtfqQRFGpIRIWEVY 348
Cdd:PRK05620 256 gpdlsAPTLAKIIATAMPRVaHGVPT-LWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWE---ERYG-VDVVHVW 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 349 GSTEgnMGLVNYVGR--CGALGKMSCLLRMLS---PFEL---VQFDMEAAEPVRDNQGFcIPVglgePGLLLTKVVSQQP 420
Cdd:PRK05620 331 GMTE--TSPVGTVARppSGVSGEARWAYRVSQgrfPASLeyrIVNDGQVMESTDRNEGE-IQV----RGNWVTASYYHSP 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 421 FVGYRGPRELSERKLVRNVRQS--GDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNV 498
Cdd:PRK05620 404 TEEGGGAASTFRGEDVEDANDRftADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAV 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 499 YGVCVPGCeGKVGMAAVQLAPG-----QTfdGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL---VREG-F 569
Cdd:PRK05620 484 IGYPDDKW-GERPLAVTVLAPGieptrET--AERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLrqhLADGdF 560
|
....*...
gi 1007386236 570 NVGIVVDP 577
Cdd:PRK05620 561 EIIKLKGP 568
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
204-274 |
1.82e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 47.63 E-value: 1.82e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1007386236 204 SPALFIYTSGTTGLPKPAILTHERVLQ-----MSKMLSLSG--ATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVL 274
Cdd:PRK05850 161 STAYLQYTSGSTRTPAGVMVSHRNVIAnfeqlMSDYFGDTGgvPPPDTTVVSWLPFYHDMGLVLGVCAPILGGCPAVL 238
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
188-258 |
3.09e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 47.03 E-value: 3.09e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1007386236 188 PSHPVPADLragitwrspALFIYTSGTTGLPKPAILTHERVLQM--SKMLSLSGATADDVVYTVLPLYHVMGL 258
Cdd:PLN02387 244 PDLPSPNDI---------AVIMYTSGSTGLPKGVMMTHGNIVATvaGVMTVVPKLGKNDVYLAYLPLAHILEL 307
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
209-271 |
4.10e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 46.76 E-value: 4.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1007386236 209 IYTSGTTGLPKPAILTHE----RVLQMSKMLSLSG--ATADDVVYTVLPLYHVMGLVVGILgCLDLGAT 271
Cdd:PLN02861 226 MYTSGTTGEPKGVILTNRaiiaEVLSTDHLLKVTDrvATEEDSYFSYLPLAHVYDQVIETY-CISKGAS 293
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
205-563 |
4.70e-05 |
|
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: 46.54 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILT---HERVLQMSkMLSLSGATADDVVYTVLPlyhvMGLVVG----ILGCLDLGATCVL--- 274
Cdd:cd05967 232 PLYILYTSGTTGKPKGVVRDnggHAVALNWS-MRNIYGIKPGDVWWAASD----VGWVVGhsyiVYGPLLHGATTVLyeg 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 275 APKFSTSC--FWDDCRQHGVTVILYVGELLRYlcnIPQQPEDRTH-------TVRLAMGNGLRADVwETF---QQRFGpI 342
Cdd:cd05967 307 KPVGTPDPgaFWRVIEKYQVNALFTAPTAIRA---IRKEDPDGKYikkydlsSLRTLFLAGERLDP-PTLewaENTLG-V 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 343 RIWEVYGSTE------GN-MGLVNYVGRCGALGKmscllrmlsP-----FELVQFDMEAAEPvrDNQGF-CIPVGLgEPG 409
Cdd:cd05967 382 PVIDHWWQTEtgwpitANpVGLEPLPIKAGSPGK---------PvpgyqVQVLDEDGEPVGP--NELGNiVIKLPL-PPG 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 410 LLLTKVVSQQPFV-GYrgpreLSERKLvrnvrqsgdvYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLS 488
Cdd:cd05967 450 CLLTLWKNDERFKkLY-----LSKFPG----------YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVL 514
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1007386236 489 QVDFLQQVNVYGVcVPGCEGKVGMAAVQLAPGQTFDGEK----LYQHVRAWLPAYATPHfiriqdamEVTSTFKLMKTR 563
Cdd:cd05967 515 SHPAVAECAVVGV-RDELKGQVPLGLVVLKEGVKITAEElekeLVALVREQIGPVAAFR--------LVIFVKRLPKTR 584
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
205-564 |
6.04e-05 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 46.17 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHE--RVLQMSKMLSLSGATADDVVYTvLPLYHVMGLVVgILGCLDLGATCVLAPKFSTSC 282
Cdd:PLN03102 188 PISLNYTSGTTADPKGVVISHRgaYLSTLSAIIGWEMGTCPVYLWT-LPMFHCNGWTF-TWGTAARGGTSVCMRHVTAPE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 283 FWDDCRQHGVTVILYVGELLRYLC---NIPQQPedRTHTVRLAMGNGLRADVWETFQQRFGpIRIWEVYGSTEGNmGLVN 359
Cdd:PLN03102 266 IYKNIEMHNVTHMCCVPTVFNILLkgnSLDLSP--RSGPVHVLTGGSPPPAALVKKVQRLG-FQVMHAYGLTEAT-GPVL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 360 YVGRCGALGKMScllrmlspfELVQFDMEAAEPVRDnqgfcipVGLGEPGLLLTKVVSQQPfvgyRGPRELSE------- 432
Cdd:PLN03102 342 FCEWQDEWNRLP---------ENQQMELKARQGVSI-------LGLADVDVKNKETQESVP----RDGKTMGEivikgss 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 433 --RKLVRNVRQSGDVY----YNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPgC 506
Cdd:PLN03102 402 imKGYLKNPKATSEAFkhgwLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHP-T 480
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1007386236 507 EGKVGMAAVQLAPGQTFDGEK----------LYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRL 564
Cdd:PLN03102 481 WGETPCAFVVLEKGETTKEDRvdklvtrerdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
207-566 |
7.45e-05 |
|
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: 45.63 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 207 LFI-YTSGTTGLPKP-----------AILTHERVLQMsKMLSLSGATADdvvytvlplyhvMGLVVG----ILGCLDLGA 270
Cdd:cd05966 234 LFIlYTSGSTGKPKGvvhttggyllyAATTFKYVFDY-HPDDIYWCTAD------------IGWITGhsyiVYGPLANGA 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 271 TCVL---APKFST-SCFWDDCRQHGVTvILY-----VGELLRYLCNIPQQpEDRThTVRL--AMGNGLRADVWETFQQRF 339
Cdd:cd05966 301 TTVMfegTPTYPDpGRYWDIVEKHKVT-IFYtaptaIRALMKFGDEWVKK-HDLS-SLRVlgSVGEPINPEAWMWYYEVI 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 340 GPIR--IWEVYGSTEGNMGLVNYVGRCGALGKMSCLLrmlsPFelvqFDMEAAepVRDNQGfcIPVGLGEPGLLLTKvvs 417
Cdd:cd05966 378 GKERcpIVDTWWQTETGGIMITPLPGATPLKPGSATR----PF----FGIEPA--ILDEEG--NEVEGEVEGYLVIK--- 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 418 qQPFVG-----YRGPrelsERKLVRNVRQSGDVYYnTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDF 492
Cdd:cd05966 443 -RPWPGmartiYGDH----ERYEDTYFSKFPGYYF-TGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPA 516
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1007386236 493 LQQVNVYGVCVPgCEGKVGMAAVQLAPGQTFDGE---KLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKtRLVR 566
Cdd:cd05966 517 VAEAAVVGRPHD-IKGEAIYAFVTLKDGEEPSDElrkELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMR-RILR 591
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
206-256 |
9.40e-05 |
|
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: 45.49 E-value: 9.40e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVLQMSK-MLSLSGATADDVVYTVLPLYHVM 256
Cdd:cd17641 161 AVLCTTSGTTGKPKLAMLSHGNFLGHCAaYLAADPLGPGDEYVSVLPLPWIG 212
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
194-259 |
1.60e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 44.60 E-value: 1.60e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1007386236 194 ADLRAG-------ITWRSPALFIYTSGTTGLPKPAILTHER-VLQMSKMLSLSGATAD-DVVYTVLPLYHVMGLV 259
Cdd:PRK07768 136 ADLLAAdpidpveTGEDDLALMQLTSGSTGSPKAVQITHGNlYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMV 210
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
205-487 |
1.67e-04 |
|
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: 44.48 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 205 PALFIYTSGTTGLPKPAILTHER--VLQMSKMLSLsGATADDVVYTVLPLYHVMGLVVGILGCLDLGATCVL--APKFST 280
Cdd:cd05974 87 PMLLYFTSGTTSKPKLVEHTHRSypVGHLSTMYWI-GLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLfnYARFDA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 281 SCFWDDCRQHGVTVILYVGELLRYLCnipQQPEDRTHT-VRLAMGNG--LRADVWETFQQRFGpIRIWEVYGSTEGNMGL 357
Cdd:cd05974 166 KRVLAALVRYGVTTLCAPPTVWRMLI---QQDLASFDVkLREVVGAGepLNPEVIEQVRRAWG-LTIRDGYGQTETTALV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 358 VNYVGRCGALGKMScllRMLSPFELVQFDMEAAePVRDNQgFCIPVGLGEPGLLLTkvvsqqpfvGYRG-PRELSErklv 436
Cdd:cd05974 242 GNSPGQPVKAGSMG---RPLPGYRVALLDPDGA-PATEGE-VALDLGDTRPVGLMK---------GYAGdPDKTAH---- 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1007386236 437 rnvrQSGDVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVL 487
Cdd:cd05974 304 ----AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVL 350
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
206-266 |
1.99e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 44.58 E-value: 1.99e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1007386236 206 ALFIYTSGTTGLPKPAILTH----ERVLQMS-KMLSLSGATADDVVYTV-LPLYHVMGL-VVGIL---GCL 266
Cdd:PTZ00216 267 ALIMYTSGTTGDPKGVMHTHgsltAGILALEdRLNDLIGPPEEDETYCSyLPLAHIMEFgVTNIFlarGAL 337
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
208-276 |
2.09e-04 |
|
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: 44.02 E-value: 2.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1007386236 208 FI-YTSGTTGLPKPAILTHERVLqmSKMLSLSGATA---DDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAP 276
Cdd:cd05908 110 FIqFSSGSTGDPKGVMLTHENLV--HNMFAILNSTEwktKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMP 180
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
209-256 |
2.99e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 43.65 E-value: 2.99e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1007386236 209 IYTSGTTGLPKPAILTHERVLQMSKMLSL------SGATADDVVYTVLPLYHVM 256
Cdd:PLN02430 226 MYTSGTSGDPKGVVLTHEAVATFVRGVDLfmeqfeDKMTHDDVYLSFLPLAHIL 279
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
151-263 |
3.30e-04 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 43.32 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 151 LEEILPKLqaeNIRCFYLSHTSPTPGVGALGAALDAAPSHPVPADLRAgitwrsPALFIYTSGTTGLPKPAILTHERVLQ 230
Cdd:PRK09029 92 LEELLPSL---TLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQR------LATMTLTSGSTGLPKAAVHTAQAHLA 162
|
90 100 110
....*....|....*....|....*....|....
gi 1007386236 231 MSK-MLSLSGATADDVVYTVLPLYHVMGLvvGIL 263
Cdd:PRK09029 163 SAEgVLSLMPFTAQDSWLLSLPLFHVSGQ--GIV 194
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
444-569 |
4.03e-04 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 43.20 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 444 DVYYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGVCVPGCeGKVGMAAVQLAPGQTF 523
Cdd:PRK06018 409 DGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKW-DERPLLIVQLKPGETA 487
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1007386236 524 DGEKLYQHVRAWLPAYATPHFIRIQDAMEVTSTFKLMKTRLvREGF 569
Cdd:PRK06018 488 TREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL-REQF 532
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
192-263 |
6.17e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 42.79 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 192 VPADLraGITWRSP-------ALFIYTSGTTGLPKPAILTHE----RVLQMskMLSLSGATADDVVyTVLPLYHVMGLVV 260
Cdd:PRK07769 164 VPDEV--GATWVPPeanedtiAYLQYTSGSTRIPAGVQITHLnlptNVLQV--IDALEGQEGDRGV-SWLPFFHDMGLIT 238
|
...
gi 1007386236 261 GIL 263
Cdd:PRK07769 239 VLL 241
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
207-294 |
1.01e-03 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 42.09 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 207 LFI-YTSGTTGLPKPAILTHERV-LQMSKMLSL-SGATADDVV--YT----VLPLYHVMGLVVgilgcldlGATCVL--- 274
Cdd:PRK03584 266 LWIlYSSGTTGLPKCIVHGHGGIlLEHLKELGLhCDLGPGDRFfwYTtcgwMMWNWLVSGLLV--------GATLVLydg 337
|
90 100
....*....|....*....|...
gi 1007386236 275 ---APKFSTscFWDDCRQHGVTV 294
Cdd:PRK03584 338 spfYPDPNV--LWDLAAEEGVTV 358
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
409-500 |
1.04e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 42.01 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 409 GLLLTKvvSQQPFVGYRGPRELSERKLVRnvrqsgDVYYNTGDVLAMDREGFLYFRDRLGDTFRW-KGENVSTHEVEGVL 487
Cdd:PTZ00342 542 GELLIK--SDSIFSGYFLEKEQTKNAFTE------DGYFKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIETDMLNNLY 613
|
90
....*....|...
gi 1007386236 488 SQVDFLQQVNVYG 500
Cdd:PTZ00342 614 SQISFINFCVVYG 626
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
191-255 |
1.47e-03 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 41.62 E-value: 1.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1007386236 191 PVPADLragitwrspALFIYTSGTTGLPKPAILTHERVLQmskmlSLSGATAD------DVVYTVLPLYHV 255
Cdd:PLN02736 218 PKPEDV---------ATICYTSGTTGTPKGVVLTHGNLIA-----NVAGSSLStkfypsDVHISYLPLAHI 274
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
206-277 |
3.00e-03 |
|
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: 40.42 E-value: 3.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1007386236 206 ALFIYTSGTTGLPKPAILTHERVL----QMSKMLSLSGAT-ADDVVYTVLPLYHVMGLVVGILGCLDLGATCVLAPK 277
Cdd:cd05933 153 CTLIYTSGTTGMPKGVMLSHDNITwtakAASQHMDLRPATvGQESVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQP 229
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
446-549 |
4.82e-03 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 39.59 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1007386236 446 YYNTGDVLAMDREGFLYFRDRLGDTFRWKGENVSTHEVEGVLSQVDFLQQVNVYGvcVPGCE-GKVGMAAVQLAPGQtFD 524
Cdd:PRK07445 325 IFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLG--LPDPHwGEVVTAIYVPKDPS-IS 401
|
90 100
....*....|....*....|....*.
gi 1007386236 525 GEKLYQHVRAWLPAYATP-HFIRIQD 549
Cdd:PRK07445 402 LEELKTAIKDQLSPFKQPkHWIPVPQ 427
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
197-271 |
7.99e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 39.26 E-value: 7.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1007386236 197 RAGITWRSPALFIYTSGTTGLPKPAILTHER---VLQMSKMLSLSGATAD-DVVYTVLPLYHVMGLVVGILGCLDLGAT 271
Cdd:PRK12582 214 IAAITPDTVAKYLFTSGSTGMPKAVINTQRMmcaNIAMQEQLRPREPDPPpPVSLDWMPWNHTMGGNANFNGLLWGGGT 292
|
|
| |
