|
Name |
Accession |
Description |
Interval |
E-value |
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
90-623 |
0e+00 |
|
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: 651.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 90 RAAIRADHKSYGFVQLISSALDVHNILCtkndgdsssikgiDGTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLA 169
Cdd:cd05941 2 RIAIVDDGDSITYADLVARAARLANRLL-------------ALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLN 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 170 LSYPEVELLHVMNDSDISMVLstkehheimesistkcstgysllpsvesippkiesqeplsseltssvssllaeidnlkk 249
Cdd:cd05941 69 PSYPLAELEYVITDSEPSLVL----------------------------------------------------------- 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 250 ikgdDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKF 329
Cdd:cd05941 90 ----DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKF 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 330 SVRGVWQRwresypsgvsKSNDAITVFTGVPTVYTRLLQGYDTMNPDEQSACSYAAKQLRLMMCGSSALPSPLMKRWEEV 409
Cdd:cd05941 166 DPKEVAIS----------RLMPSITVFMGVPTIYTRLLQYYEAHFTDPQFARAAAAERLRLMVSGSAALPVPTLEEWEAI 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 410 TGHRLLERYGMTEFVMALSNPLHGPRKEGTVGKPLPRVEAKIIMDDGTETKAG--VGELCIRSPSLFREYWKRPEVTEES 487
Cdd:cd05941 236 TGHTLLERYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVDEETGEPLPRgeVGEIQVRGPSVFKEYWNKPEATKEE 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 488 FIDGGFFKTGDTVTIDEDGYFKILGRTNADIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKED 567
Cdd:cd05941 316 FTDDGWFKTGDLGVVDEDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAG 395
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2212542879 568 VkeraeqasePALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKK 623
Cdd:cd05941 396 A---------AALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
134-626 |
8.42e-138 |
|
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: 409.59 E-value: 8.42e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLStkehheimesistkcstgysll 213
Cdd:COG0318 45 GVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT---------------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 214 psvesippkiesqeplsseltssvssllaeidnlkkikgddpALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQS 293
Cdd:COG0318 103 ------------------------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 294 EDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGVWQ---RWResypsgvsksndaITVFTGVPTVYTRLLQgy 370
Cdd:COG0318 141 GDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLElieRER-------------VTVLFGVPTMLARLLR-- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 371 dtmNPDeqsACSYAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTE-FVMALSNPL-HGPRKEGTVGKPLPRVE 448
Cdd:COG0318 206 ---HPE---FARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTEtSPVVTVNPEdPGERRPGSVGRPLPGVE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 449 AKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFIDgGFFKTGDTVTIDEDGYFKILGRTnADIMKVGGYKLS 527
Cdd:COG0318 280 VRIVDEDGRELPPGeVGEIVVRGPNVMKGYWNDPEATAEAFRD-GWLRTGDLGRLDEDGYLYIVGRK-KDMIISGGENVY 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 528 ALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDvkeraeqasePALTLQALTSWSKDKLAPYKIPTRLYLWDS 607
Cdd:COG0318 358 PAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPG----------AELDAEELRAFLRERLARYKVPRRVEFVDE 427
|
490
....*....|....*....
gi 2212542879 608 LPRNAMGKVNKKELKKLLQ 626
Cdd:COG0318 428 LPRTASGKIDRRALRERYA 446
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
132-622 |
1.32e-121 |
|
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: 368.43 E-value: 1.32e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 132 GTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVlstkehhEIMESISTKCSTGYS 211
Cdd:cd05936 43 NLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKAL-------IVAVSFTDLLAAGAP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 212 LLPSVEsippkiesqeplsseltssvssllaeidnlkkIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQIlTEAW-- 289
Cdd:cd05936 116 LGERVA--------------------------------LTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQ-IKAWle 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 290 -GYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGVWQrwresypsGVSKSNdaITVFTGVPTVYTRLLQ 368
Cdd:cd05936 163 dLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGVLK--------EIRKHR--VTIFPGVPTMYIALLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 369 gydtmNPDEQSacsYAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEF--VMALsNPLHGPRKEGTVGKPLPR 446
Cdd:cd05936 233 -----APEFKK---RDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETspVVAV-NPLDGPRKPGSIGIPLPG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 447 VEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFIDGgFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYK 525
Cdd:cd05936 304 TEVKIVDDDGEELPPGeVGELWVRGPQVMKGYWNRPEETAEAFVDG-WLRTGDIGYMDEDGYFFIVDRKK-DMIIVGGFN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 526 LSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDvkeraeqasePALTLQALTSWSKDKLAPYKIPTRLYLW 605
Cdd:cd05936 382 VYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEG----------ASLTEEEIIAFCREQLAGYKVPRQVEFR 451
|
490
....*....|....*..
gi 2212542879 606 DSLPRNAMGKVNKKELK 622
Cdd:cd05936 452 DELPKSAVGKILRRELR 468
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
136-622 |
8.69e-108 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 333.11 E-value: 8.69e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 136 LRGA-RIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHeimesistkcstgyslLP 214
Cdd:PRK07787 42 VAGArRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGPAPDD----------------PA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 215 SVESIPPKIESQEPLSSeltssvssllAEIDNlkkikgDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSE 294
Cdd:PRK07787 106 GLPHVPVRLHARSWHRY----------PEPDP------DAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 295 DQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGVWqrwRESYPSGvsksndaiTVFTGVPTVYTRLLQgydtmN 374
Cdd:PRK07787 170 DVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTPEAYA---QALSEGG--------TLYFGVPTVWSRIAA-----D 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 375 PDEQSACSYAakqlRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHGPRKEGTVGKPLPRVEAKIIMD 454
Cdd:PRK07787 234 PEAARALRGA----RLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 455 DGTETKAG---VGELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNADIMKVGGYKLSALEI 531
Cdd:PRK07787 310 DGGPVPHDgetVGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRESTDLIKSGGYRIGAGEI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 532 EAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKEraeqasepaltlQALTSWSKDKLAPYKIPTRLYLWDSLPRN 611
Cdd:PRK07787 390 ETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAA------------DELIDFVAQQLSVHKRPREVRFVDALPRN 457
|
490
....*....|.
gi 2212542879 612 AMGKVNKKELK 622
Cdd:PRK07787 458 AMGKVLKKQLL 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
254-616 |
4.77e-105 |
|
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: 321.16 E-value: 4.77e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 254 DPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFnALFAPLYSGSVVEFMPKFSVRG 333
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 334 VWQRWREsypsgvsksnDAITVFTGVPTVYTRLLQGYDTMNPDeQSAcsyaakqLRLMMCGSSALPSPLMKRWEEVTGHR 413
Cdd:cd04433 80 ALELIER----------EKVTILLGVPTLLARLLKAPESAGYD-LSS-------LRALVSGGAPLPPELLERFEEAPGIK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 414 LLERYGMTE--FVMALSNPLHGPRKEGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFID 490
Cdd:cd04433 142 LVNGYGLTEtgGTVATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGeIGELVVRGPSVMKGYWNNPEATAAVDED 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 491 gGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEdvke 570
Cdd:cd04433 222 -GWYRTGDLGRLDEDGYLYIVGRLK-DMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRP---- 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2212542879 571 raeqasEPALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKV 616
Cdd:cd04433 296 ------GADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
138-622 |
5.16e-104 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 324.52 E-value: 5.16e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 138 GARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKCSTGY------- 210
Cdd:PRK07514 53 GDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDPANFAWLSKIAAAAGAPHvetldad 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 211 ---SLLPSVESIPPKIESQEplsseltssvssllaeidnlkkIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTE 287
Cdd:PRK07514 133 gtgSLLEAAAAAPDDFETVP----------------------RGADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 288 AWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGVWQRWRESypsgvsksndaiTVFTGVPTVYTRLL 367
Cdd:PRK07514 191 YWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLALMPRA------------TVMMGVPTFYTRLL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 368 QGyDTMNPDeqsacsyAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHGPRKEGTVGKPLPRV 447
Cdd:PRK07514 259 QE-PRLTRE-------AAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNPYDGERRAGTVGFPLPGV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 448 EAKII-MDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRtNADIMKVGGYK 525
Cdd:PRK07514 331 SLRVTdPETGAELPPGeIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGR-GKDLIISGGYN 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 526 LSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAkedvkeRAEQASEPALTLQALtswsKDKLAPYKIPTRLYLW 605
Cdd:PRK07514 410 VYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVP------KPGAALDEAAILAAL----KGRLARFKQPKRVFFV 479
|
490
....*....|....*..
gi 2212542879 606 DSLPRNAMGKVNKKELK 622
Cdd:PRK07514 480 DELPRNTMGKVQKNLLR 496
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
72-622 |
5.90e-97 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 306.73 E-value: 5.90e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 72 TFMDVVREvfkHSSAHGARAAIRADHKSYGFVQLISSALDVHNILctkndgDSSSIKGidgtgflrGARIGIVAKPSAEF 151
Cdd:PRK06187 7 TIGRILRH---GARKHPDKEAVYFDGRRTTYAELDERVNRLANAL------RALGVKK--------GDRVAVFDWNSHEY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 152 VAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESIStkcstgySLLPSVESIppKIESQEPLSS 231
Cdd:PRK06187 70 LEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAIL-------PQLPTVRTV--IVEGDGPAAP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 232 ELTSSVS-----SLLAEIDNLKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHV 306
Cdd:PRK06187 141 LAPEVGEyeellAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 307 HGLfNALFAPLYSGSVVEFMPKFSVRGVWQRWREsypsgvsksnDAITVFTGVPTVYTRLLQgydtmNPDeqsACSYAAK 386
Cdd:PRK06187 221 HAW-GLPYLALMAGAKQVIPRRFDPENLLDLIET----------ERVTFFFAVPTIWQMLLK-----APR---AYFVDFS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 387 QLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTE----FVMALSNP--LHGPRKEGTVGKPLPRVEAKIIMDDGTETK 460
Cdd:PRK06187 282 SLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTEtspvVSVLPPEDqlPGQWTKRRSAGRPLPGVEARIVDDDGDELP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 461 AG---VGELCIRSPSLFREYWKRPEVTEEsFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLE 537
Cdd:PRK06187 362 PDggeVGEIIVRGPWLMQGYWNRPEATAE-TIDGGWLHTGDVGYIDEDGYLYITDRIK-DVIISGGENIYPRELEDALYG 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 538 HDTILECAVLGLPDEAYGEVICAIIVAKEDvkeraEQASEpaltlQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVN 617
Cdd:PRK06187 440 HPAVAEVAVIGVPDEKWGERPVAVVVLKPG-----ATLDA-----KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKIL 509
|
....*
gi 2212542879 618 KKELK 622
Cdd:PRK06187 510 KRVLR 514
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
132-618 |
5.29e-95 |
|
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: 298.76 E-value: 5.29e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 132 GTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPL--ALSYPEVEllHVMNDSDISMVLstkehheimesistkcstg 209
Cdd:cd17631 39 ALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLnfRLTPPEVA--YILADSGAKVLF------------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 210 ysllpsvesippkiesqeplsseltssvssllaeidnlkkikgDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAW 289
Cdd:cd17631 98 -------------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAAL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 290 GYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGVWQRWRESypsgvsksndAITVFTGVPTVYTRLLQG 369
Cdd:cd17631 135 DLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERH----------RVTSFFLVPTMIQALLQH 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 370 YDTMNPDEQSacsyaakqLRLMMCGSSALPSPLMKRWEEvTGHRLLERYGMTEFVMALS--NPLHGPRKEGTVGKPLPRV 447
Cdd:cd17631 205 PRFATTDLSS--------LRAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTETSPGVTflSPEDHRRKLGSAGRPVFFV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 448 EAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFIDgGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKL 526
Cdd:cd17631 276 EVRIVDPDGREVPPGeVGEIVVRGPHVMAGYWNRPEATAAAFRD-GWFHTGDLGRLDEDGYLYIVDRKK-DMIISGGENV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 527 SALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKERAEQasepaltlqaLTSWSKDKLAPYKIPTRLYLWD 606
Cdd:cd17631 354 YPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDE----------LIAHCRERLARYKIPKSVEFVD 423
|
490
....*....|..
gi 2212542879 607 SLPRNAMGKVNK 618
Cdd:cd17631 424 ALPRNATGKILK 435
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
134-623 |
8.98e-95 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 300.00 E-value: 8.98e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTK-EHHEIMESISTK------- 205
Cdd:cd05926 35 GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPKgELGPASRAASKLglailel 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 206 --CSTGYSLLPSVESIPPKIEsqeplsseltssvssLLAEIDNLKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQ 283
Cdd:cd05926 115 alDVGVLIRAPSAESLSNLLA---------------DKKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASAT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 284 ILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGVWQrWRESYpsgvsksndAITVFTGVPTVY 363
Cdd:cd05926 180 NITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWP-DVRDY---------NATWYTAVPTIH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 364 TRLLQgydtmnpDEQSACSYAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFV--MAlSNPL-HGPRKEGTV 440
Cdd:cd05926 250 QILLN-------RPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMT-SNPLpPGPRKPGSV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 441 GKPLPrVEAKIIMDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIM 519
Cdd:cd05926 322 GKPVG-VEVRILDEDGEILPPGVvGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIK-ELI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 520 KVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDvkeraeqasePALTLQALTSWSKDKLAPYKIP 599
Cdd:cd05926 400 NRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREG----------ASVTEEELRAFCRKHLAAFKVP 469
|
490 500
....*....|....*....|....
gi 2212542879 600 TRLYLWDSLPRNAMGKVNKKELKK 623
Cdd:cd05926 470 KKVYFVDELPKTATGKIQRRKVAE 493
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
134-522 |
9.60e-93 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 292.29 E-value: 9.60e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVL--STKEHHEIMESISTKCSTGYS 211
Cdd:pfam00501 42 GVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLItdDALKLEELLEALGKLEVVKLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 212 LLPSVESIPPKIESQEPLSSELTSSVSSllaeidnlKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQV----QILTE 287
Cdd:pfam00501 122 LVLDRDPVLKEEPLPEEAKPADVPPPPP--------PPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVlsikRVRPR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 288 AWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGVWQRWREsypsgVSKSNdaITVFTGVPTVYTRLL 367
Cdd:pfam00501 194 GFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPALDPAALLEL-----IERYK--VTVLYGVPTLLNMLL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 368 QGYDTMNPDEQSacsyaakqLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTE---FVMALSNPLHGPRKEGTVGKPL 444
Cdd:pfam00501 267 EAGAPKRALLSS--------LRLVLSGGAPLPPELARRFRELFGGALVNGYGLTEttgVVTTPLPLDEDLRSLGSVGRPL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 445 PRVEAKIIMDDGTETKA--GVGELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVG 522
Cdd:pfam00501 339 PGTEVKIVDDETGEPVPpgEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKK-DQIKLG 417
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
134-623 |
7.62e-92 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 292.96 E-value: 7.62e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKcstgyslL 213
Cdd:PRK07656 51 GIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTR-------L 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 214 PSVESI---PPKIESQEPLSSELTSSVSSLLAEIDNLKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWG 290
Cdd:PRK07656 124 PALEHVvicETEEDDPHTEKMKTFTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 291 YQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGVWQRWREsypsgvsksnDAITVFTGVPTVYTRLLQgy 370
Cdd:PRK07656 204 LTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEVFRLIET----------ERITVLPGPPTMYNSLLQ-- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 371 dtmNPDeqsACSYAAKQLRLMMCGSSALPSPLMKRWEEVTG-HRLLERYGMTEFV-MALSNPLHGPRKE--GTVGKPLPR 446
Cdd:PRK07656 272 ---HPD---RSAEDLSSLRLAVTGAASMPVALLERFESELGvDIVLTGYGLSEASgVTTFNRLDDDRKTvaGTIGTAIAG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 447 VEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESfIDG-GFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGY 524
Cdd:PRK07656 346 VENKIVNELGEEVPVGeVGELLVRGPNVMKGYYDDPEATAAA-IDAdGWLHTGDLGRLDEEGYLYIVDRKK-DMFIVGGF 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 525 KLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDvkeraeqasePALTLQALTSWSKDKLAPYKIPTRLYL 604
Cdd:PRK07656 424 NVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG----------AELTEEELIAYCREHLAKYKVPRSIEF 493
|
490
....*....|....*....
gi 2212542879 605 WDSLPRNAMGKVNKKELKK 623
Cdd:PRK07656 494 LDELPKNATGKVLKRALRE 512
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
137-626 |
5.72e-88 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 284.31 E-value: 5.72e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 137 RGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTK--CSTGYSLLP 214
Cdd:COG0365 63 KGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKekVDEALEELP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 215 SVESIppkIESQEPLSSELTSSVSSLLAEIDNL------KKIKGDDPALILYTSGTTGKPKGVVHTHKGILsqVQILTEA 288
Cdd:COG0365 143 SLEHV---IVVGRTGADVPMEGDLDWDELLAAAsaefepEPTDADDPLFILYTSGTTGKPKGVVHTHGGYL--VHAATTA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 289 ---WGYQSEDQFLhCLP-LHHVHGLFNALFAPLYSGSVVeFM----PKFSVRGVWqrWR--ESYpsgvsksndAITVFTG 358
Cdd:COG0365 218 kyvLDLKPGDVFW-CTAdIGWATGHSYIVYGPLLNGATV-VLyegrPDFPDPGRL--WEliEKY---------GVTVFFT 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 359 VPTVYtRLLqgydtMNPDEQSACSYAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHG-PRKE 437
Cdd:COG0365 285 APTAI-RAL-----MKAGDEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGlPVKP 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 438 GTVGKPLPRVEAKIIMDDGTETKAG-VGELCIRS--PSLFREYWKRPEVTEESFID--GGFFKTGDTVTIDEDGYFKILG 512
Cdd:COG0365 359 GSMGKPVPGYDVAVVDEDGNPVPPGeEGELVIKGpwPGMFRGYWNDPERYRETYFGrfPGWYRTGDGARRDEDGYFWILG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 513 RTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKERAEQASEpaltlqaLTSWSKDK 592
Cdd:COG0365 439 RSD-DVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSDELAKE-------LQAHVREE 510
|
490 500 510
....*....|....*....|....*....|....
gi 2212542879 593 LAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLLQ 626
Cdd:COG0365 511 LGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAE 544
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
134-617 |
5.66e-81 |
|
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: 263.69 E-value: 5.66e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKCSTGysll 213
Cdd:cd05911 31 GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDPDGLEKVKEAAKELGPK---- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 214 PSVESIPPKIESQEPLSSELTSSVSSLLAEIDNLKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWG--Y 291
Cdd:cd05911 107 DKIIVLDDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYgnD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 292 QSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVeFMPKFSVrgvwqrwrESYPSGVSKSNdaITVFTGVPTVYTRLLQgyd 371
Cdd:cd05911 187 GSNDVILGFLPLYHIYGLFTTLASLLNGATVI-IMPKFDS--------ELFLDLIEKYK--ITFLYLVPPIAAALAK--- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 372 tmNPDEQSacsYAAKQLRLMMCGSSalpsPLMKRWEE-----VTGHRLLERYGMTEFVMALSNPLHGPRKEGTVGKPLPR 446
Cdd:cd05911 253 --SPLLDK---YDLSSLRVILSGGA----PLSKELQEllakrFPNATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 447 VEAKIIMDDGTETKA--GVGELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGY 524
Cdd:cd05911 324 VEAKIVDDDGKDSLGpnEPGEICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKK-ELIKYKGF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 525 KLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDvkeraeqasePALTLQALTSWSKDKLAPYKiptRL-- 602
Cdd:cd05911 403 QVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPG----------EKLTEKEVKDYVAKKVASYK---QLrg 469
|
490
....*....|....*..
gi 2212542879 603 --YLWDSLPRNAMGKVN 617
Cdd:cd05911 470 gvVFVDEIPKSASGKIL 486
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
244-626 |
2.35e-78 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 259.55 E-value: 2.35e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 244 IDNLKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVqILTEAW----GYQSEdQFLHCLPLHHVHGL-FNALFAPLY 318
Cdd:PRK05605 210 DVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANA-AQGKAWvpglGDGPE-RVLAALPMFHAYGLtLCLTLAVSI 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 319 SGSVVeFMPKFSVRGVWQRWRESYPsgvsksndaiTVFTGVPTVYTRLLQGYDTMNPDEQSacsyaakqLRLMMCGSSAL 398
Cdd:PRK05605 288 GGELV-LLPAPDIDLILDAMKKHPP----------TWLPGVPPLYEKIAEAAEERGVDLSG--------VRNAFSGAMAL 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 399 PSPLMKRWEEVTGHRLLERYGMTEFV-MALSNPLHGPRKEGTVGKPLPRVEAKII--------MDDGTEtkagvGELCIR 469
Cdd:PRK05605 349 PVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVRIVdpedpdetMPDGEE-----GELLVR 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 470 SPSLFREYWKRPEVTEESFIDgGFFKTGDTVTIDEDGYFKILGRTNADIMkVGGYKLSALEIEAVLLEHDTILECAVLGL 549
Cdd:PRK05605 424 GPQVFKGYWNRPEETAKSFLD-GWFRTGDVVVMEEDGFIRIVDRIKELII-TGGFNVYPAEVEEVLREHPGVEDAAVVGL 501
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2212542879 550 PDEAYGEVICAIIVAKEDVkeraeqasepALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLLQ 626
Cdd:PRK05605 502 PREDGSEEVVAAVVLEPGA----------ALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELL 568
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
134-622 |
7.75e-76 |
|
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: 248.36 E-value: 7.75e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLStkehheimesistkcstgysll 213
Cdd:cd05934 24 GIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV---------------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 214 psvesippkiesqeplsseltssvssllaeidnlkkikgdDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQS 293
Cdd:cd05934 82 ----------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 294 EDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGVWQRWREsypSGVsksndaiTVFTGVPTVYTRLLQGYDTM 373
Cdd:cd05934 122 DDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWSDVRR---YGA-------TVTNYLGAMLSYLLAQPPSP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 374 NPdeqsacsyAAKQLRLmmCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHGPRKEGTVGKPLPRVEAKIIM 453
Cdd:cd05934 192 DD--------RAHRLRA--AYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 454 DDGTETKAG-VGELCIRS---PSLFREYWKRPEVTEESFiDGGFFKTGDTVTIDEDGYFKILGRTnADIMKVGGYKLSAL 529
Cdd:cd05934 262 DDGQELPAGePGELVIRGlrgWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRK-KDMIRRRGENISSA 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 530 EIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKeraeqasepaLTLQALTSWSKDKLAPYKIPTRLYLWDSLP 609
Cdd:cd05934 340 EVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGET----------LDPEELFAFCEGQLAYFKVPRYIRFVDDLP 409
|
490
....*....|...
gi 2212542879 610 RNAMGKVNKKELK 622
Cdd:cd05934 410 KTPTEKVAKAQLR 422
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
129-621 |
7.81e-76 |
|
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: 248.55 E-value: 7.81e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 129 GIDGTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHheimesistkcst 208
Cdd:cd05935 17 FLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSEL------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 209 gysllpsvesippkiesqeplsseltssvssllaeidnlkkikgDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEA 288
Cdd:cd05935 84 --------------------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVW 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 289 WGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMpkfsvrgvwQRW-RESYPSGVSKSNdaITVFTGVPTVYTRLL 367
Cdd:cd05935 120 TGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLM---------ARWdRETALELIEKYK--VTFWTNIPTMLVDLL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 368 QgydtmNPDEQSACsyaAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEfVMALS--NPLHGPrKEGTVGKPLP 445
Cdd:cd05935 189 A-----TPEFKTRD---LSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTE-TMSQThtNPPLRP-KLQCLGIP*F 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 446 RVEAKII-MDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFI-DGG--FFKTGDTVTIDEDGYFKILGRTNaDIMK 520
Cdd:cd05935 259 GVDARVIdIETGRELPPNeVGEIVVRGPQIFKGYWNRPEETEESFIeIKGrrFFRTGDLGYMDEEGYFFFVDRVK-RMIN 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 521 VGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKERAeqasepalTLQALTSWSKDKLAPYKIPT 600
Cdd:cd05935 338 VSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKV--------TEEDIIEWAREQMAAYKYPR 409
|
490 500
....*....|....*....|.
gi 2212542879 601 RLYLWDSLPRNAMGKVNKKEL 621
Cdd:cd05935 410 EVEFVDELPRSASGKILWRLL 430
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
150-623 |
1.29e-73 |
|
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: 243.06 E-value: 1.29e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 150 EFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHeimesistkcSTGYSLLPsvesippkiesqepl 229
Cdd:cd05903 38 EFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPERFR----------QFDPAAMP--------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 230 sseltssvssllaeidnlkkikgDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGL 309
Cdd:cd05903 93 -----------------------DAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 310 FNALFAPLYSGSVVEFMPKFSVRGVWQRWREsypsgvsksnDAITVFTGVPTVYTRLLQGydtmnPDEQSAcsyAAKQLR 389
Cdd:cd05903 150 VYGFTLPLLLGAPVVLQDIWDPDKALALMRE----------HGVTFMMGATPFLTDLLNA-----VEEAGE---PLSRLR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 390 LMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHGP--RKEGTVGKPLPRVEAKIIMDDGTETKAG-VGEL 466
Cdd:cd05903 212 TFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedRRLYTDGRPLPGVEIKVVDDTGATLAPGvEGEL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 467 CIRSPSLFREYWKRPEVTEESFiDGGFFKTGDTVTIDEDGYFKILGRtNADIMKVGGYKLSALEIEAVLLEHDTILECAV 546
Cdd:cd05903 292 LSRGPSVFLGYLDRPDLTADAA-PEGWFRTGDLARLDEDGYLRITGR-SKDIIIRGGENIPVLEVEDLLLGHPGVIEAAV 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2212542879 547 LGLPDEAYGEVICAIIVAKedvkeraeqaSEPALTLQALTSW-SKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKK 623
Cdd:cd05903 370 VALPDERLGERACAVVVTK----------SGALLTFDELVAYlDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
137-626 |
4.40e-71 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 237.84 E-value: 4.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 137 RGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKCStgysLLPSV 216
Cdd:PRK06839 52 KGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSY----VQRVI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 217 ESIPPKIESQeplsseltssvssllAEIDNLKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQ 296
Cdd:PRK06839 128 SITSLKEIED---------------RKIDNFVEKNESASFIICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 297 FLHCLPLHHVHGLFNALFAPLYSGSVV----EFMPKFSVRGVwqrwresypsgvskSNDAITVFTGVPTVYTRLLQGYDT 372
Cdd:PRK06839 193 SIVLLPLFHIGGIGLFAFPTLFAGGVIivprKFEPTKALSMI--------------EKHKVTVVMGVPTIHQALINCSKF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 373 MNPDEQSacsyaakqLRLMMCGSSALPSPLMKRWEEvTGHRLLERYGMTE-----FVMALSNplhGPRKEGTVGKPLPRV 447
Cdd:PRK06839 259 ETTNLQS--------VRWFYNGGAPCPEELMREFID-RGFLFGQGFGMTEtsptvFMLSEED---ARRKVGSIGKPVLFC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 448 EAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESfIDGGFFKTGDTVTIDEDGYFKILGRTNADIMKvGGYKL 526
Cdd:PRK06839 327 DYELIDENKNKVEVGeVGELLIRGPNVMKEYWNRPDATEET-IQDGWLCTGDLARVDEDGFVYIVGRKKEMIIS-GGENI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 527 SALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAK-------EDVKERAEQasepaltlqaltswskdKLAPYKIP 599
Cdd:PRK06839 405 YPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKsssvlieKDVIEHCRL-----------------FLAKYKIP 467
|
490 500
....*....|....*....|....*..
gi 2212542879 600 TRLYLWDSLPRNAMGKVNKKELKKLLQ 626
Cdd:PRK06839 468 KEIVFLKELPKNATGKIQKAQLVNQLK 494
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
132-623 |
1.47e-70 |
|
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: 234.54 E-value: 1.47e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 132 GTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEhheimesistkcstgys 211
Cdd:cd05972 19 KLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDAE----------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 212 llpsvesippkiesqeplsseltssvssllaeidnlkkikgdDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGY 291
Cdd:cd05972 82 ------------------------------------------DPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 292 QSEDQFLHCLPLHHVHGLFNALFAPLYSGS--VVEFMPKFSVRgVWQRWRESYPsgvsksndaITVFTGVPTVYTRLLQg 369
Cdd:cd05972 120 RPDDIHWNIADPGWAKGAWSSFFGPWLLGAtvFVYEGPRFDAE-RILELLERYG---------VTSFCGPPTAYRMLIK- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 370 ydtmnpdeQSACSYAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHGPRKEGTVGKPLPRVEA 449
Cdd:cd05972 189 --------QDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 450 KIIMDDGTETKAG-VGELCIR--SPSLFREYWKRPEVTEESFIdGGFFKTGDTVTIDEDGYFKILGRtNADIMKVGGYKL 526
Cdd:cd05972 261 AIIDDDGRELPPGeEGDIAIKlpPPGLFLGYVGDPEKTEASIR-GDYYLTGDRAYRDEDGYFWFVGR-ADDIIKSSGYRI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 527 SALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKERAEQASEpaltLQALTswsKDKLAPYKIPTRLYLWD 606
Cdd:cd05972 339 GPFEVESALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEE----LQGHV---KKVLAPYKYPREIEFVE 411
|
490
....*....|....*..
gi 2212542879 607 SLPRNAMGKVNKKELKK 623
Cdd:cd05972 412 ELPKTISGKIRRVELRD 428
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
77-622 |
4.29e-70 |
|
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: 235.73 E-value: 4.29e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 77 VREVFKHS-SAHGARAAIRADHKSYGFVQLISSALDVHNILCTKndgdsssikgidgtGFLRGARIGIVAKPSAEFVAGI 155
Cdd:cd05959 6 ATLVDLNLnEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRAL--------------GVKREERVLLIMLDTVDFPTAF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 156 FGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKCSTGYSLLPSVESIPPKiesqepLSSELTS 235
Cdd:cd05959 72 LGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPE------AGALLLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 236 SVSSLLAEIDNLKKIKGDDPALILYTSGTTGKPKGVVHTHKGI-----LSQVQILteawGYQSEDQFLHCLPLHHVHGLF 310
Cdd:cd05959 146 ELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIywtaeLYARNVL----GIREDDVCFSAAKLFFAYGLG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 311 NALFAPLYSGSVVEFMPKF-SVRGVWQRWRESYPsgvsksndaiTVFTGVPTVYTRLLQgydtmNPDeqsACSYAAKQLR 389
Cdd:cd05959 222 NSLTFPLSVGATTVLMPERpTPAAVFKRIRRYRP----------TVFFGVPTLYAAMLA-----APN---LPSRDLSSLR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 390 LMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFV-MALSNpLHGPRKEGTVGKPLPRVEAKIIMDDGTETKAG-VGELC 467
Cdd:cd05959 284 LCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLhIFLSN-RPGRVRYGTTGKPVPGYEVELRDEDGGDVADGePGELY 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 468 IRSPSLFREYWKRPEVTEESFiDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVL 547
Cdd:cd05959 363 VRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRAD-DMLKVSGIWVSPFEVESALVQHPAVLEAAVV 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2212542879 548 GLPDEAYGEVICAIIVAKEDVKERAEQASEpaltlqaLTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:cd05959 441 GVEDEDGLTKPKAFVVLRPGYEDSEALEEE-------LKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
134-621 |
6.34e-70 |
|
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: 233.19 E-value: 6.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTkehheimesistkcstgysll 213
Cdd:cd05930 33 GVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVLTD--------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 214 psvesippkiesqeplsseltssvssllaeidnlkkikGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQS 293
Cdd:cd05930 92 --------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 294 EDQFLHCLPLHHVHGLFNaLFAPLYSGSVVEFMPKFSVRGVWQ--RWRESYpsgvsksndAITVFTGVPTVYTRLLQ-GY 370
Cdd:cd05930 134 GDRVLQFTSFSFDVSVWE-IFGALLAGATLVVLPEEVRKDPEAlaDLLAEE---------GITVLHLTPSLLRLLLQeLE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 371 DTMNPDeqsacsyaakqLRLMMCGSSALPSPLMKRWEEV-TGHRLLERYGMTEF-VMALSNPLHGPRKEG---TVGKPLP 445
Cdd:cd05930 204 LAALPS-----------LRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEAtVDATYYRVPPDDEEDgrvPIGRPIP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 446 RVEAKIIMDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGFF------KTGDTVTIDEDGYFKILGRTnADI 518
Cdd:cd05930 273 NTRVYVLDENLRPVPPGVpGELYIGGAGLARGYLNRPELTAERFVPNPFGpgermyRTGDLVRWLPDGNLEFLGRI-DDQ 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 519 MKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDvkeraeqasePALTLQALTSWSKDKLAPYKI 598
Cdd:cd05930 352 VKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEG----------GELDEEELRAHLAERLPDYMV 421
|
490 500
....*....|....*....|...
gi 2212542879 599 PTRLYLWDSLPRNAMGKVNKKEL 621
Cdd:cd05930 422 PSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
137-621 |
7.83e-70 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 236.01 E-value: 7.83e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 137 RGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKCSTGYSLL--- 213
Cdd:PRK08314 60 KGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIVaqy 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 214 ------PSVESIPPKIESQEPLSSELTSSVSSLLAEIDNLK-----KIKGDDPALILYTSGTTGKPKGVVHTHKGILSQV 282
Cdd:PRK08314 140 sdylpaEPEIAVPAWLRAEPPLQALAPGGVVAWKEALAAGLappphTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 283 qILTEAW-GYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPkfsvrgvwqRW-RESYPSGVSKSNdaITVFTGVP 360
Cdd:PRK08314 220 -VGSVLWsNSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMP---------RWdREAAARLIERYR--VTHWTNIP 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 361 TVYTRLLqgydtMNPDEQsacSYAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEfVMA--LSNPLHGPRKEg 438
Cdd:PRK08314 288 TMVVDFL-----ASPGLA---ERDLSSLRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAqtHSNPPDRPKLQ- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 439 TVGKPLPRVEAKII-MDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFI--DGG-FFKTGDTVTIDEDGYFKILGR 513
Cdd:PRK08314 358 CLGIPTFGVDARVIdPETLEELPPGeVGEIVVHGPQVFKGYWNRPEATAEAFIeiDGKrFFRTGDLGRMDEEGYFFITDR 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 514 TNADImKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKERAeqasepalTLQALTSWSKDKL 593
Cdd:PRK08314 438 LKRMI-NASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEARGKT--------TEEEIIAWAREHM 508
|
490 500
....*....|....*....|....*...
gi 2212542879 594 APYKIPTRLYLWDSLPRNAMGKVNKKEL 621
Cdd:PRK08314 509 AAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
133-623 |
2.35e-69 |
|
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: 230.70 E-value: 2.35e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 133 TGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMvlstkehheimesistkcstgysl 212
Cdd:cd05912 21 LGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL------------------------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 213 lpsvesippkiesqeplsseltssvssllaeidnlkkikgDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQ 292
Cdd:cd05912 77 ----------------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLT 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 293 SEDQFLHCLPLHHVHGLfNALFAPLYSGSVVEFMPKFSVRGVWQRWRESypsgvsksndAITVFTGVPTVYTRLLQGYDT 372
Cdd:cd05912 117 EDDNWLCALPLFHISGL-SILMRSVIYGMTVYLVDKFDAEQVLHLINSG----------KVTIISVVPTMLQRLLEILGE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 373 MNPDEqsacsyaakqLRLMMCGSSALPSPLMKRWEEvTGHRLLERYGMTEF---VMALsNPLHGPRKEGTVGKPLPRVEA 449
Cdd:cd05912 186 GYPNN----------LRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTETcsqIVTL-SPEDALNKIGSAGKPLFPVEL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 450 KIIMDDGTetKAGVGELCIRSPSLFREYWKRPEVTEESFIDGgFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSAL 529
Cdd:cd05912 254 KIEDDGQP--PYEVGEILLKGPNVTKGYLNRPDATEESFENG-WFKTGDIGYLDEEGFLYVLDRRS-DLIISGGENIYPA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 530 EIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVkeraeqasepalTLQALTSWSKDKLAPYKIPTRLYLWDSLP 609
Cdd:cd05912 330 EIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPI------------SEEELIAYCSEKLAKYKVPKKIYFVDELP 397
|
490
....*....|....
gi 2212542879 610 RNAMGKVNKKELKK 623
Cdd:cd05912 398 RTASGKLLRHELKQ 411
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
132-623 |
9.03e-69 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 232.52 E-value: 9.03e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 132 GTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKCSTGYS 211
Cdd:PRK08316 55 DLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 212 LLPSVESIPPKIESQEPLSSELTSSVSSLLAEIdnlkkIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGY 291
Cdd:PRK08316 135 ILSLVLGGREAPGGWLDFADWAEAGSVAEPDVE-----LADDDLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDM 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 292 QSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGVWQRwresypsgVSKsnDAITVFTGVPTVYTRLLQGYD 371
Cdd:PRK08316 210 SADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELILRT--------IEA--ERITSFFAPPTVWISLLRHPD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 372 TMNPDEQSacsyaakqLRLMMCGSSALPSPLMKRWEE-VTGHRLLERYGMTEfvMAlsnPLH---GP----RKEGTVGKP 443
Cdd:PRK08316 280 FDTRDLSS--------LRKGYYGASIMPVEVLKELRErLPGLRFYNCYGQTE--IA---PLAtvlGPeehlRRPGSAGRP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 444 LPRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFiDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVG 522
Cdd:PRK08316 347 VLNVETRVVDDDGNDVAPGeVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKK-DMIKTG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 523 GYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVkeraeqasepALTLQALTSWSKDKLAPYKIPTRL 602
Cdd:PRK08316 425 GENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGA----------TVTEDELIAHCRARLAGFKVPKRV 494
|
490 500
....*....|....*....|.
gi 2212542879 603 YLWDSLPRNAMGKVNKKELKK 623
Cdd:PRK08316 495 IFVDELPRNPSGKILKRELRE 515
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
250-622 |
1.36e-64 |
|
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: 218.87 E-value: 1.36e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 250 IKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQIL-TEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPK 328
Cdd:cd05919 88 TSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMaREALGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 329 fsvrgvwqrWRESYPSGVSKSNDAITVFTGVPTVYTRLLqgydtmnpDEQSACSYAAKQLRLMMCGSSALPSPLMKRWEE 408
Cdd:cd05919 168 ---------WPTAERVLATLARFRPTVLYGVPTFYANLL--------DSCAGSPDALRSLRLCVSAGEALPRGLGERWME 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 409 VTGHRLLERYGMTE-FVMALSNPLhGPRKEGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEE 486
Cdd:cd05919 231 HFGGPILDGIGATEvGHIFLSNRP-GAWRLGSTGRPVPGYEIRLVDEEGHTIPPGeEGDLLVRGPSAAVGYWNNPEKSRA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 487 SFiDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKE 566
Cdd:cd05919 310 TF-NGGWYRTGDKFCRDADGWYTHAGRAD-DMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKS 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2212542879 567 dvkeraEQASEPALtLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:cd05919 388 ------PAAPQESL-ARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
134-622 |
2.59e-64 |
|
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: 218.53 E-value: 2.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESistkcstgysll 213
Cdd:cd05969 21 GVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEELYERTDP------------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 214 psvesippkiesqeplsseltssvssllaeidnlkkikgDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQS 293
Cdd:cd05969 89 ---------------------------------------EDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHP 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 294 EDQFLHCLPLHHVHGLFNALFAPLYSG-SVVEFMPKFSVRgvwqRWRESYPSgvsksnDAITVFTGVPTVYTRLlqgydt 372
Cdd:cd05969 130 DDIYWCTADPGWVTGTVYGIWAPWLNGvTNVVYEGRFDAE----SWYGIIER------VKVTVWYTAPTAIRML------ 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 373 MNPDEQSACSYAAKQLRLMMCGSSALpSPLMKRW-EEVTGHRLLERYGMTEF-VMALSNPLHGPRKEGTVGKPLPRVEAK 450
Cdd:cd05969 194 MKEGDELARKYDLSSLRFIHSVGEPL-NPEAIRWgMEVFGVPIHDTWWQTETgSIMIANYPCMPIKPGSMGKPLPGVKAA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 451 IIMDDGTETKAG-VGELCIRS--PSLFREYWKRPEVTEESFIDGgFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLS 527
Cdd:cd05969 273 VVDENGNELPPGtKGILALKPgwPSMFRGIWNDEERYKNSFIDG-WYLTGDLAYRDEDGYFWFVGRAD-DIIKTSGHRVG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 528 ALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKERAEQASEpaltlqaLTSWSKDKLAPYKIPTRLYLWDS 607
Cdd:cd05969 351 PFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEE-------IINFVRQKLGAHVAPREIEFVDN 423
|
490
....*....|....*
gi 2212542879 608 LPRNAMGKVNKKELK 622
Cdd:cd05969 424 LPKTRSGKIMRRVLK 438
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
130-626 |
5.39e-63 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 217.99 E-value: 5.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 130 IDGTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKCS-- 207
Cdd:PRK06178 75 LRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETSlr 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 208 ----TGYS-LLPSVESIPPKIESQEPLSSELtssvssllAEIDNLKKIKG------------DDPALILYTSGTTGKPKG 270
Cdd:PRK06178 155 hvivTSLAdVLPAEPTLPLPDSLRAPRLAAA--------GAIDLLPALRActapvplpppalDALAALNYTGGTTGMPKG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 271 VVHTHKGIlsqvqILTEAWGY------QSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMpkfsvrgvwQRWresyps 344
Cdd:PRK06178 227 CEHTQRDM-----VYTAAAAYavavvgGEDSVFLSFLPEFWIAGENFGLLFPLFSGATLVLL---------ARW------ 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 345 gvsksnDAITVFTGVP----TVYTRLLQGYDTMNpDEQSACSYAAKQLRLMMCGS--SALPSPLMKRWEEVTGHRLLE-R 417
Cdd:PRK06178 287 ------DAVAFMAAVEryrvTRTVMLVDNAVELM-DHPRFAEYDLSSLRQVRVVSfvKKLNPDYRQRWRALTGSVLAEaA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 418 YGMTE------FVMALSNPLHGPRKEGT-VGKPLPRVEAKII-MDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESF 488
Cdd:PRK06178 360 WGMTEthtcdtFTAGFQDDDFDLLSQPVfVGLPVPGTEFKICdFETGELLPLGAeGEIVVRTPSLLKGYWNKPEATAEAL 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 489 IDgGFFKTGDTVTIDEDGYFKILGRtNADIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDV 568
Cdd:PRK06178 440 RD-GWLHTGDIGKIDEQGFLHYLGR-RKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGA 517
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2212542879 569 KERAEqasepaltlqALTSWSKDKLAPYKIPTrLYLWDSLPRNAMGKVNKKELKKLLQ 626
Cdd:PRK06178 518 DLTAA----------ALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDLQALAE 564
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
130-546 |
1.22e-62 |
|
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: 212.90 E-value: 1.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 130 IDGTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKCST- 208
Cdd:TIGR01733 17 RAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRLAGLVLPVILl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 209 GYSLLPSVESIPPKIESQEPLsseltssvssllaeidnlkkiKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEA 288
Cdd:TIGR01733 97 DPLELAALDDAPAPPPPDAPS---------------------GPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 289 WGYQSEDQFLHCLPLHHVHGLFnALFAPLYSGSVVEFMPKFSVR---GVWQRWRESYPsgvsksndaITVFTGVPTVYTR 365
Cdd:TIGR01733 156 YGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPEDEERddaALLAALIAEHP---------VTVLNLTPSLLAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 366 LLQGYDTMNPDeqsacsyaakqLRLMMCGSSALPSPLMKRWEEVTGH-RLLERYGMTE---FVMALSNPLHGPRKEGTV- 440
Cdd:TIGR01733 226 LAAALPPALAS-----------LRLVILGGEALTPALVDRWRARGPGaRLINLYGPTEttvWSTATLVDPDDAPRESPVp 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 441 -GKPLPRVEAKIIMDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGF--------FKTGDTVTIDEDGYFKI 510
Cdd:TIGR01733 295 iGRPLANTRLYVLDDDLRPVPVGVvGELYIGGPGVARGYLNRPELTAERFVPDPFaggdgarlYRTGDLVRYLPDGNLEF 374
|
410 420 430
....*....|....*....|....*....|....*.
gi 2212542879 511 LGRTNADImKVGGYKLSALEIEAVLLEHDTILECAV 546
Cdd:TIGR01733 375 LGRIDDQV-KIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
249-621 |
1.56e-62 |
|
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: 215.18 E-value: 1.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 249 KIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQS--EDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFM 326
Cdd:cd05904 154 VIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSdsEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVM 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 327 PKFSVRGVW---QRWResypsgvsksndaITVFTGVPTVYTRLlqgydTMNPDEQSacsYAAKQLRLMMCGSSALPSPLM 403
Cdd:cd05904 234 PRFDLEELLaaiERYK-------------VTHLPVVPPIVLAL-----VKSPIVDK---YDLSSLRQIMSGAAPLGKELI 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 404 KRWEEVTGH-RLLERYGMTE---FVMALSNPLHGPRKEGTVGKPLPRVEAKII-MDDGTETKAG-VGELCIRSPSLFREY 477
Cdd:cd05904 293 EAFRAKFPNvDLGQGYGMTEstgVVAMCFAPEKDRAKYGSVGRLVPNVEAKIVdPETGESLPPNqTGELWIRGPSIMKGY 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 478 WKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEV 557
Cdd:cd05904 373 LNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLK-ELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEV 451
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2212542879 558 ICAIIVAKedvkeraeqaSEPALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 621
Cdd:cd05904 452 PMAFVVRK----------PGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
134-585 |
6.93e-62 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 216.12 E-value: 6.93e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVL-STKEHHEIMESISTKCstgysl 212
Cdd:COG1022 61 GVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFvEDQEQLDKLLEVRDEL------ 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 213 lPSVESIP---PKIESQEPLSSE-----LTSSVSSLLAEIDNLK-KIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQ 283
Cdd:COG1022 135 -PSLRHIVvldPRGLRDDPRLLSldellALGREVADPAELEARRaAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNAR 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 284 ILTEAWGYQSEDQFLHCLPLHHVHGLFNALFApLYSGSVVEFMPkfSVRGVWQRWRESYPsgvsksndaiTVFTGVP--- 360
Cdd:COG1022 214 ALLERLPLGPGDRTLSFLPLAHVFERTVSYYA-LAAGATVAFAE--SPDTLAEDLREVKP----------TFMLAVPrvw 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 361 -TVYTRLLQGYDTMNPDEQSACSYAAK----------------------------------------QLRLMMCGSSALP 399
Cdd:COG1022 281 eKVYAGIQAKAEEAGGLKRKLFRWALAvgrryararlagkspslllrlkhaladklvfsklrealggRLRFAVSGGAALG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 400 SPLMkRWEEVTGHRLLERYGMTE-FVMALSNPLHGPRKeGTVGKPLPRVEAKIimddgtetkAGVGELCIRSPSLFREYW 478
Cdd:COG1022 361 PELA-RFFRALGIPVLEGYGLTEtSPVITVNRPGDNRI-GTVGPPLPGVEVKI---------AEDGEILVRGPNVMKGYY 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 479 KRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKV-GGYKLSALEIEAVLLEHDTILECAVLGlPDEAYgev 557
Cdd:COG1022 430 KNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKK-DLIVTsGGKNVAPQPIENALKASPLIEQAVVVG-DGRPF--- 504
|
490 500
....*....|....*....|....*....
gi 2212542879 558 ICAIIV-AKEDVKERAEQASEPALTLQAL 585
Cdd:COG1022 505 LAALIVpDFEALGEWAEENGLPYTSYAEL 533
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
90-625 |
7.72e-62 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 212.90 E-value: 7.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 90 RAAIRADHKSYGFVQLISSAldvhNILCTKndgdsssikgIDGTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLA 169
Cdd:PRK03640 18 RTAIEFEEKKVTFMELHEAV----VSVAGK----------LAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 170 LSYPEVELLHVMNDSDISMVLSTKEhheIMESISTKCSTGYSLLPSVESIPPKIESQEPLsseltssvssllaeidnlkk 249
Cdd:PRK03640 84 TRLSREELLWQLDDAEVKCLITDDD---FEAKLIPGISVKFAELMNGPKEEAEIQEEFDL-------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 250 ikgDDPALILYTSGTTGKPKGVVHTHK-----GILSQVQIlteawGYQSEDQFLHCLPLHHVHGLfNALFAPLYSGSVVE 324
Cdd:PRK03640 141 ---DEVATIMYTSGTTGKPKGVIQTYGnhwwsAVGSALNL-----GLTEDDCWLAAVPIFHISGL-SILMRSVIYGMRVV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 325 FMPKFSVRGVWQrwresypsgvSKSNDAITVFTGVPTVYTRLLQGYdtmnPDEqsacSYAAKqLRLMMCGSSALPSPLMK 404
Cdd:PRK03640 212 LVEKFDAEKINK----------LLQTGGVTIISVVSTMLQRLLERL----GEG----TYPSS-FRCMLLGGGPAPKPLLE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 405 RWEEvTGHRLLERYGMTEF---VMALSnPLHGPRKEGTVGKPLPRVEAKIiMDDGTETKAG-VGELCIRSPSLFREYWKR 480
Cdd:PRK03640 273 QCKE-KGIPVYQSYGMTETasqIVTLS-PEDALTKLGSAGKPLFPCELKI-EKDGVVVPPFeEGEIVVKGPNVTKGYLNR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 481 PEVTEESFIDGgFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICA 560
Cdd:PRK03640 350 EDATRETFQDG-WFKTGDIGYLDEEGFLYVLDRRS-DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVA 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2212542879 561 IIVAKEDVKEraeqasepaltlQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLL 625
Cdd:PRK03640 428 FVVKSGEVTE------------EELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
90-622 |
1.68e-61 |
|
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: 210.80 E-value: 1.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 90 RAAIRADHKSYGFVQLISSALDVHNILctkndgdsssikgIDGTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPla 169
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVL-------------VGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVA-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 170 lSYPevellhvmndsdismVLSTKEHHEIMEsistKCSTGYSLLPSVESippkiesqeplsseltssvssllaeidnlkk 249
Cdd:cd05958 66 -TMP---------------LLRPKELAYILD----KARITVALCAHALT------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 250 iKGDDPALILYTSGTTGKPKGVVHTHKGILS-----QVQILteawGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVE 324
Cdd:cd05958 95 -ASDDICILAFTSGTTGAPKATMHFHRDPLAsadryAVNVL----RLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGV 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 325 FMPkfsvrgvwqrwrESYPSGVSK--SNDAITVFTGVPTVYTRLLQGYDTMNPDEQSacsyaakqLRLMMCGSSALPSPL 402
Cdd:cd05958 170 LLE------------EATPDLLLSaiARYKPTVLFTAPTAYRAMLAHPDAAGPDLSS--------LRKCVSAGEALPAAL 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 403 MKRWEEVTGHRLLERYGMTE-FVMALSNPlHGPRKEGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPSLfreYWKR 480
Cdd:cd05958 230 HRAWKEATGIPIIDGIGSTEmFHIFISAR-PGDARPGATGKPVPGYEAKVVDDEGNPVPDGtIGRLAVRGPTG---CRYL 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 481 PEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICA 560
Cdd:cd05958 306 ADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSD-DMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKA 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2212542879 561 IIVAkedvkeRAEQASEPALtLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:cd05958 385 FVVL------RPGVIPGPVL-ARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
253-622 |
2.08e-61 |
|
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: 207.90 E-value: 2.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFM-PKFSV 331
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPsPSFDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 332 RGVWQrwresypsgvSKSNDAITVFTGVPTVYTRLLQGYDTMNPDEQSacsyaakqLRLMMCGSSALPSPLMKRWEEVTG 411
Cdd:cd05917 82 LAVLE----------AIEKEKCTALHGVPTMFIAELEHPDFDKFDLSS--------LRTGIMAGAPCPPELMKRVIEVMN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 412 HR-LLERYGMTEF--VMALSNPLHGP-RKEGTVGKPLPRVEAKII-MDDGTETKAGV-GELCIRSPSLFREYWKRPEVTE 485
Cdd:cd05917 144 MKdVTIAYGMTETspVSTQTRTDDSIeKRVNTVGRIMPHTEAKIVdPEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 486 ESfIDG-GFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVA 564
Cdd:cd05917 224 EA-IDGdGWLHTGDLAVMDEDGYCRIVGRIK-DMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRL 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2212542879 565 KEDVKERAEQasepaltlqaLTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:cd05917 302 KEGAELTEED----------IKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
129-623 |
2.42e-60 |
|
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: 209.79 E-value: 2.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 129 GIDGTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDS-------DISMV---------LST 192
Cdd:cd12119 41 ALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAedrvvfvDRDFLplleaiaprLPT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 193 KEHHEIMESISTKCSTGYSLLPSVESIppkIESQEPLSseltssvssllaeidNLKKIKGDDPALILYTSGTTGKPKGVV 272
Cdd:cd12119 121 VEHVVVMTDDAAMPEPAGVGVLAYEEL---LAAESPEY---------------DWPDFDENTAAAICYTSGTTGNPKGVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 273 HTHKG-ILSQVQIL-TEAWGYQSEDQFLHCLPLHHVHGlFNALFAPLYSGSvvefmpKFSVRGVwqrwresYPSGVSKSN 350
Cdd:cd12119 183 YSHRSlVLHAMAALlTDGLGLSESDVVLPVVPMFHVNA-WGLPYAAAMVGA------KLVLPGP-------YLDPASLAE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 351 ----DAITVFTGVPTVYTRLLQGYDTMNPDEQSacsyaakqLRLMMCGSSALPSPLMKRWEEVtGHRLLERYGMTEF--- 423
Cdd:cd12119 249 lierEGVTFAAGVPTVWQGLLDHLEANGRDLSS--------LRRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTETspl 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 424 -VMALSNPLHGPRKEG-------TVGKPLPRVEAKIIMDDGTETKA---GVGELCIRSPSLFREYWKRPEVTEESFiDGG 492
Cdd:cd12119 320 gTVARPPSEHSNLSEDeqlalraKQGRPVPGVELRIVDDDGRELPWdgkAVGELQVRGPWVTKSYYKNDEESEALT-EDG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 493 FFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKERA 572
Cdd:cd12119 399 WLRTGDVATIDEDGYLTITDRSK-DVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTA 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2212542879 573 EqasepaltlqALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKK 623
Cdd:cd12119 478 E----------ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
128-624 |
4.45e-59 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 207.32 E-value: 4.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 128 KGIDGTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLS-----TKEHHEIMESI 202
Cdd:PRK12583 60 RGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICadafkTSDYHAMLQEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 203 STKCSTGYSLLPSVESIPP--KIESQEPLSSELTSSVSSLLAEIDNLKK---------IKGDDPALILYTSGTTGKPKGV 271
Cdd:PRK12583 140 LPGLAEGQPGALACERLPElrGVVSLAPAPPPGFLAWHELQARGETVSRealaerqasLDRDDPINIQYTSGTTGFPKGA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 272 VHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVV-----EFMPKFSVRGVwqrwresypsgv 346
Cdd:PRK12583 220 TLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGACLvypneAFDPLATLQAV------------ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 347 skSNDAITVFTGVPTVYTRLLQGYDTMNPDEQSacsyaakqLRLMMCGSSALPSPLMKR-WEEVTGHRLLERYGMTE--- 422
Cdd:PRK12583 288 --EEERCTALYGVPTMFIAELDHPQRGNFDLSS--------LRTGIMAGAPCPIEVMRRvMDEMHMAEVQIAYGMTEtsp 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 423 --FVMALSNPLhgPRKEGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDT 499
Cdd:PRK12583 358 vsLQTTAADDL--ERRVETVGRTQPHLEVKVVDPDGATVPRGeIGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDL 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 500 VTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDvkeraEQASEpa 579
Cdd:PRK12583 436 ATMDEQGYVRIVGRSK-DMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPG-----HAASE-- 507
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2212542879 580 ltlQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKL 624
Cdd:PRK12583 508 ---EELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREI 549
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
134-621 |
6.42e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 207.19 E-value: 6.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVL--------------STKEHHEIM 199
Cdd:PRK06710 70 GVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcldlvfprvtnvqsATKIEHVIV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 200 ESISTKCSTGYSLL-PSVE----SIPPKIESQEplsseLTSSVSSLLAEIDNLKKIKGD---DPALILYTSGTTGKPKGV 271
Cdd:PRK06710 150 TRIADFLPFPKNLLyPFVQkkqsNLVVKVSESE-----TIHLWNSVEKEVNTGVEVPCDpenDLALLQYTGGTTGFPKGV 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 272 VHTHKGILSQVqILTEAWGY---QSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGVWQRWRESypsgvsk 348
Cdd:PRK06710 225 MLTHKNLVSNT-LMGVQWLYnckEGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKMVFEAIKKH------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 349 sndAITVFTGVPTVYTRLLQgydtmNPDEQSacsYAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFV-MAL 427
Cdd:PRK06710 297 ---KVTLFPGAPTIYIALLN-----SPLLKE---YDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSpVTH 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 428 SNPLHGPRKEGTVGKPLPRVEAKII-MDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFIDGgFFKTGDTVTIDED 505
Cdd:PRK06710 366 SNFLWEKRVPGSIGVPWPDTEAMIMsLETGEALPPGeIGEIVVKGPQIMKGYWNKPEETAAVLQDG-WLHTGDVGYMDED 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 506 GYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDvkeraEQASEpaltlQAL 585
Cdd:PRK06710 445 GFFYVKDRKK-DMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEG-----TECSE-----EEL 513
|
490 500 510
....*....|....*....|....*....|....*.
gi 2212542879 586 TSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 621
Cdd:PRK06710 514 NQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
248-624 |
1.06e-58 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 207.89 E-value: 1.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 248 KKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMP 327
Cdd:PRK07529 208 RPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLAT 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 328 KFSVRG------VW---QRWResypsgvsksndaITVFTGVPTVYTRLLQgydtMNPDEQSACSyaakqLRLMMCGSSAL 398
Cdd:PRK07529 288 PQGYRGpgvianFWkivERYR-------------INFLSGVPTVYAALLQ----VPVDGHDISS-----LRYALCGAAPL 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 399 PSPLMKRWEEVTGHRLLERYGMTEFVMALS-NPLHGPRKEGTVGKPLPRVEAKIIMDDGTET------KAGVGELCIRSP 471
Cdd:PRK07529 346 PVEVFRRFEAATGVRIVEGYGLTEATCVSSvNPPDGERRIGSVGLRLPYQRVRVVILDDAGRylrdcaVDEVGVLCIAGP 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 472 SLFREYwKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNADIMKvGGYKLSALEIEAVLLEHDTILECAVLGLPD 551
Cdd:PRK07529 426 NVFSGY-LEAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLIIR-GGHNIDPAAIEEALLRHPAVALAAAVGRPD 503
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2212542879 552 EAYGEVICAIIVAKEDVkeraeqasepALTLQALTSWSKDKLA-PYKIPTRLYLWDSLPRNAMGKVNKKELKKL 624
Cdd:PRK07529 504 AHAGELPVAYVQLKPGA----------SATEAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALRRD 567
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
253-622 |
2.45e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 204.45 E-value: 2.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGlfnALFAP-LYSGSVVEFMPKFSV 331
Cdd:PRK06188 168 PDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGG---AFFLPtLLRGGTVIVLAKFDP 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 332 RGVWQRWREsypsgvsksnDAITVFTGVPTVYTRLLQGYDTMNPDEQSacsyaakqLRLMMCGSSAL-PSPL---MKRWe 407
Cdd:PRK06188 245 AEVLRAIEE----------QRITATFLVPTMIYALLDHPDLRTRDLSS--------LETVYYGASPMsPVRLaeaIERF- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 408 evtGHRLLERYGMTEFVMALS------NPLHGPRKEGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKR 480
Cdd:PRK06188 306 ---GPIFAQYYGQTEAPMVITylrkrdHDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGeVGEICVRGPLVMDGYWNR 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 481 PEVTEESFiDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICA 560
Cdd:PRK06188 383 PEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKK-DMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTA 460
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2212542879 561 IIVAKEDVKERAEQasepaltLQALTswsKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:PRK06188 461 VVVLRPGAAVDAAE-------LQAHV---KERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
254-625 |
1.56e-57 |
|
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: 196.78 E-value: 1.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 254 DPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFnALFAPLYSGSVVEFMPKfsvrg 333
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLA-ILVRSLLAGAELVLLER----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 334 vwqRWresyPSGVSKSNDAITVFTGVPTVYTRLLqgydtmnpdEQSACSYAAKQLRLMMCGSSALPSPLMKRWEEvTGHR 413
Cdd:cd17630 75 ---NQ----ALAEDLAPPGVTHVSLVPTQLQRLL---------DSGQGPAALKSLRAVLLGGAPIPPELLERAAD-RGIP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 414 LLERYGMTEFVMALSNPLHGPRKEGTVGKPLPRVEAKIIMDdgtetkagvGELCIRSPSLFREYWKRPEVTEesFIDGGF 493
Cdd:cd17630 138 LYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVED---------GEIWVGGASLAMGYLRGQLVPE--FNEDGW 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 494 FKTGDTVTIDEDGYFKILGRtnADIMKV-GGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVakedvkera 572
Cdd:cd17630 207 FTTKDLGELHADGRLTVLGR--ADNMIIsGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIV--------- 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2212542879 573 eqaSEPALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLL 625
Cdd:cd17630 276 ---GRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
250-622 |
7.65e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 201.53 E-value: 7.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 250 IKGDDPALILYTSGTTGKPKGVVHTHKGILS---QVQILTEAWGYQSEDQFLHCLPLHHVHGL-FNALFAPLYSGSVVEF 325
Cdd:PRK05677 204 PQADDVAVLQYTGGTTGVAKGAMLTHRNLVAnmlQCRALMGSNLNEGCEILIAPLPLYHIYAFtFHCMAMMLIGNHNILI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 326 -----MPKFsVRgVWQRWResypsgvsksndaITVFTGVPTVYTRLLQGYDTMNPDeqsacsYAAkqLRLMMCGSSALPS 400
Cdd:PRK05677 284 snprdLPAM-VK-ELGKWK-------------FSGFVGLNTLFVALCNNEAFRKLD------FSA--LKLTLSGGMALQL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 401 PLMKRWEEVTGHRLLERYGMTEFV-MALSNPLHGPRKeGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYW 478
Cdd:PRK05677 341 ATAERWKEVTGCAICEGYGMTETSpVVSVNPSQAIQV-GTIGIPVPSTLCKVIDDDGNELPLGeVGELCVKGPQVMKGYW 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 479 KRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVI 558
Cdd:PRK05677 420 QRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKK-DMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAI 498
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2212542879 559 CAIIVAKedvkeraeqaSEPALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:PRK05677 499 KVFVVVK----------PGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELR 552
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
149-623 |
2.26e-56 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 199.59 E-value: 2.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 149 AEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLS-TKEHHEIMESISTKCSTGYSLL----------PSVE 217
Cdd:PRK06087 85 CEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFApTLFKQTRPVDLILPLQNQLPQLqqivgvdklaPATS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 218 SIPPK--IESQEPLSSELTssvssllaeidnlkkIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSED 295
Cdd:PRK06087 165 SLSLSqiIADYEPLTTAIT---------------THGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQD 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 296 QFLHCLPLHHVHGLFNALFAP-LYSGSVV---EFMPKFSVRgVWQRWRESYPSGVSksndaitvftgvPTVytrllqgYD 371
Cdd:PRK06087 230 VFMMPAPLGHATGFLHGVTAPfLIGARSVlldIFTPDACLA-LLEQQRCTCMLGAT------------PFI-------YD 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 372 TMNPDEQSACSYAAkqLRLMMCGSSALPSPLMKRWEEvTGHRLLERYGMTE----FVMALSNPLhgPRKEGTVGKPLPRV 447
Cdd:PRK06087 290 LLNLLEKQPADLSA--LRFFLCGGTTIPKKVARECQQ-RGIKLLSVYGSTEssphAVVNLDDPL--SRFMHTDGYAAAGV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 448 EAKIIMDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKL 526
Cdd:PRK06087 365 EIKVVDEARKTLPPGCeGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKK-DIIVRGGENI 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 527 SALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKedvkeraeqASEPALTLQALTSW-SKDKLAPYKIPTRLYLW 605
Cdd:PRK06087 444 SSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLK---------APHHSLTLEEVVAFfSRKRVAKYKYPEHIVVI 514
|
490
....*....|....*...
gi 2212542879 606 DSLPRNAMGKVNKKELKK 623
Cdd:PRK06087 515 DKLPRTASGKIQKFLLRK 532
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
128-582 |
2.51e-56 |
|
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: 197.05 E-value: 2.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 128 KGIDGTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLstkehheimesistkcs 207
Cdd:cd05907 20 KGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF----------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 208 tgysllpsVEsippkiesqeplsseltssvssllaeidnlkkiKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTE 287
Cdd:cd05907 83 --------VE---------------------------------DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 288 AWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPkfSVRGVWQRWRESYPsgvsksndaiTVFTGVPTVYTRLl 367
Cdd:cd05907 122 RLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFAS--SAETLLDDLSEVRP----------TVFLAVPRVWEKV- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 368 qgYDTMNPDEQSACSYA------AKQLRLMMCGSSALPSPLMKRWEEVtGHRLLERYGMTEFVMALS-NPLHGPRkEGTV 440
Cdd:cd05907 189 --YAAIKVKAVPGLKRKlfdlavGGRLRFAASGGAPLPAELLHFFRAL-GIPVYEGYGLTETSAVVTlNPPGDNR-IGTV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 441 GKPLPRVEAKIIMDdgtetkagvGELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMK 520
Cdd:cd05907 265 GKPLPGVEVRIADD---------GEILVRGPNVMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKK-DLII 334
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2212542879 521 V-GGYKLSALEIEAVLLEHDTILECAVLGlpdEAYGEVICAIIVAKEDVKERAEQASEPALTL 582
Cdd:cd05907 335 TsGGKNISPEPIENALKASPLISQAVVIG---DGRPFLVALIVPDPEALEAWAEEHGIAYTDV 394
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
132-623 |
1.70e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 197.31 E-value: 1.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 132 GTGFlrGARIGIVAKPSAEFVAGIFGTWLSGGVAVPL--ALSYPEVELLhvMNDSDISMVLS-------TKEHHEIMESI 202
Cdd:PRK07786 63 GVGF--GDRVLILMLNRTEFVESVLAANMLGAIAVPVnfRLTPPEIAFL--VSDCGAHVVVTeaalapvATAVRDIVPLL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 203 STKCSTGYSLLPSVESIPPKIESQEPLSseltssvssllAEIDnlkkIKGDDPALILYTSGTTGKPKGVVHTHKGILSQV 282
Cdd:PRK07786 139 STVVVAGGSSDDSVLGYEDLLAEAGPAH-----------APVD----IPNDSPALIMYTSGTTGRPKGAVLTHANLTGQA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 283 QILTEAWGYQSEDQFLHC-LPLHHVHGLFNALFAPLYSGSVV-----EFMPKfSVRGVWQRWResypsgvsksndAITVF 356
Cdd:PRK07786 204 MTCLRTNGADINSDVGFVgVPLFHIAGIGSMLPGLLLGAPTViyplgAFDPG-QLLDVLEAEK------------VTGIF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 357 TgVPTVYTRLLqgydtmnpDEQSAcsyAAKQLRLMMCGSSALPSP--LMKRWEEV-TGHRLLERYGMTEF--VMALSNPL 431
Cdd:PRK07786 271 L-VPAQWQAVC--------AEQQA---RPRDLALRVLSWGAAPASdtLLRQMAATfPEAQILAAFGQTEMspVTCMLLGE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 432 HGPRKEGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFiDGGFFKTGDTVTIDEDGYFKI 510
Cdd:PRK07786 339 DAIRKLGSVGKVIPTVAARVVDENMNDVPVGeVGEIVYRAPTLMSGYWNNPEATAEAF-AGGWFHSGDLVRQDEEGYVWV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 511 LGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKedvkeraeqASEPALTLQALTSWSK 590
Cdd:PRK07786 418 VDRKK-DMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVR---------NDDAALTLEDLAEFLT 487
|
490 500 510
....*....|....*....|....*....|...
gi 2212542879 591 DKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKK 623
Cdd:PRK07786 488 DRLARYKHPKALEIVDALPRNPAGKVLKTELRE 520
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
134-623 |
8.50e-55 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 194.29 E-value: 8.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKcstgyslL 213
Cdd:TIGR02262 51 GVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGK-------S 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 214 PSVESIppKIESQEPLSSELTSSVSSLLAEIDNLKKIKGDDPALILYTSGTTGKPKGVVHTHkgilSQVQILTEAW---- 289
Cdd:TIGR02262 124 PHLEHR--VVVGRPEAGEVQLAELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTH----SNPYWTAELYarnt 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 290 -GYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMP-KFSVRGVWQRWRESYPsgvsksndaiTVFTGVPTVYTRLL 367
Cdd:TIGR02262 198 lGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGeRPTPDAVFDRLRRHQP----------TIFYGVPTLYAAML 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 368 QgydtmNPDEQSacsyaAKQLRLMMCGSS--ALPSPLMKRWEEVTGHRLLERYGMTEFV-MALSNpLHGPRKEGTVGKPL 444
Cdd:TIGR02262 268 A-----DPNLPS-----EDQVRLRLCTSAgeALPAEVGQRWQARFGVDIVDGIGSTEMLhIFLSN-LPGDVRYGTSGKPV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 445 PRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFIdGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGG 523
Cdd:TIGR02262 337 PGYRLRLVGDGGQDVADGePGELLISGPSSATMYWNNRAKSRDTFQ-GEWTRSGDKYVRNDDGSYTYAGRTD-DMLKVSG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 524 YKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKERAEQasepaltlqaLTSWSKDKLAPYKIPTRLY 603
Cdd:TIGR02262 415 IYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQTALETE----------LKEHVKDRLAPYKYPRWIV 484
|
490 500
....*....|....*....|
gi 2212542879 604 LWDSLPRNAMGKVNKKELKK 623
Cdd:TIGR02262 485 FVDDLPKTATGKIQRFKLRE 504
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
252-624 |
9.23e-55 |
|
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: 190.38 E-value: 9.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 252 GDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSV 331
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 332 RG------VW---QRWResypsgvsksndaITVFTGVPTVYTRLLQgydtmNPDEQSACSyaakqLRLMMCGSSALPSPL 402
Cdd:cd05944 81 RNpglfdnFWklvERYR-------------ITSLSTVPTVYAALLQ-----VPVNADISS-----LRFAMSGAAPLPVEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 403 MKRWEEVTGHRLLERYGMTEFVMALS-NPLHGPRKEGTVGKPLPRVEAKIIMDDGTET---KAG---VGELCIRSPSLFR 475
Cdd:cd05944 138 RARFEDATGLPVVEGYGLTEATCLVAvNPPDGPKRPGSVGLRLPYARVRIKVLDGVGRllrDCApdeVGEICVAGPGVFG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 476 EYWKRpEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYG 555
Cdd:cd05944 218 GYLYT-EGNKNAFVADGWLNTGDLGRLDADGYLFITGRAK-DLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAG 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 556 EVICAIIVAKEDVKeraeqasepaLTLQALTSWSKDKLAPY-KIPTRLYLWDSLPRNAMGKVNKKELKKL 624
Cdd:cd05944 296 ELPVAYVQLKPGAV----------VEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALRAD 355
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
254-618 |
2.72e-54 |
|
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: 188.09 E-value: 2.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 254 DPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRG 333
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 334 VWQRwresypsgvsKSNDAITVFTGVPTVYTRLLQGYDTMNPDEQSacsyaakqLRLMMCGSSALPSPLMKRW-EEVTGH 412
Cdd:cd17638 81 ILEA----------IERERITVLPGPPTLFQSLLDHPGRKKFDLSS--------LRAAVTGAATVPVELVRRMrSELGFE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 413 RLLERYGMTEFVMA-LSNPLHGPRK-EGTVGKPLPRVEAKIimddgtetkAGVGELCIRSPSLFREYWKRPEVTEESFID 490
Cdd:cd17638 143 TVLTAYGLTEAGVAtMCRPGDDAETvATTCGRACPGFEVRI---------ADDGEVLVRGYNVMQGYLDDPEATAEAIDA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 491 GGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVke 570
Cdd:cd17638 214 DGWLHTGDVGELDERGYLRITDRLK-DMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGV-- 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2212542879 571 raeqasepALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNK 618
Cdd:cd17638 291 --------TLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
249-622 |
6.38e-54 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 193.31 E-value: 6.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 249 KIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVqILTEAW---GYQSEDQ-----FLHCLPLHHVHGL-FNALFApLYS 319
Cdd:PRK07059 200 KLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANV-LQMEAWlqpAFEKKPRpdqlnFVCALPLYHIFALtVCGLLG-MRT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 320 GSVVEFMPkfSVRGVwqrwresypSGVSK--SNDAITVFTGVPTVYTRLLQgydtmNPD-EQSACSyaakQLRLMMCGSS 396
Cdd:PRK07059 278 GGRNILIP--NPRDI---------PGFIKelKKYQVHIFPAVNTLYNALLN-----NPDfDKLDFS----KLIVANGGGM 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 397 ALPSPLMKRWEEVTGHRLLERYGMTEFV-MALSNPLHGPRKEGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPSLF 474
Cdd:PRK07059 338 AVQRPVAERWLEMTGCPITEGYGLSETSpVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGePGEICIRGPQVM 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 475 REYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAY 554
Cdd:PRK07059 418 AGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIVDRKK-DMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHS 496
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2212542879 555 GEVICAIIVAKedvkeraeqasEPALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:PRK07059 497 GEAVKLFVVKK-----------DPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
134-624 |
1.51e-53 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 191.64 E-value: 1.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVL--STKEHHEIMESI---STKCST 208
Cdd:PRK05852 64 GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLidADGPHDRAEPTTrwwPLTVNV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 209 GYSLLPSVESIPPKIE-SQEPLSSELTSsvssllaeiDNLkkikGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTE 287
Cdd:PRK05852 144 GGDSGPSGGTLSVHLDaATEPTPATSTP---------EGL----RPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIIT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 288 AWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVeFMP---KFSVRGVWQRWRESypsgvsksndAITVFTGVPTVYT 364
Cdd:PRK05852 211 GYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAV-LLPargRFSAHTFWDDIKAV----------GATWYTAVPTIHQ 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 365 RLLQgydtmNPDEQSACSYAAKqLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSNP-------LHGPRKE 437
Cdd:PRK05852 280 ILLE-----RAATEPSGRKPAA-LRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTqiegigqTENPVVS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 438 -GTVGKPlPRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFIDgGFFKTGDTVTIDEDGYFKILGRTN 515
Cdd:PRK05852 354 tGLVGRS-TGAQIRIVGSDGLPLPAGaVGEVWLRGTTVVRGYLGDPTITAANFTD-GWLRTGDLGSLSAAGDLSIRGRIK 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 516 aDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVkeraeqasepALTLQALTSWSKDKLAP 595
Cdd:PRK05852 432 -ELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESA----------PPTAEELVQFCRERLAA 500
|
490 500
....*....|....*....|....*....
gi 2212542879 596 YKIPTRLYLWDSLPRNAMGKVNKKELKKL 624
Cdd:PRK05852 501 FEIPASFQEASGLPHTAKGSLDRRAVAEQ 529
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
141-621 |
1.95e-53 |
|
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: 190.23 E-value: 1.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 141 IGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEhheimesistkcstgysllpsvesIP 220
Cdd:cd17655 50 VGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQSH------------------------LQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 221 PKIESQEPLSSELTSSVSSLLAEidNLKKI-KGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAwGYQSE-DQFL 298
Cdd:cd17655 106 PPIAFIGLIDLLDEDTIYHEESE--NLEPVsKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKV-IYQGEhLRVA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 299 HCLPLHhvhglFNA----LFAPLYSGSVVEFMPKFSVRGVwQRWRESYpsgvskSNDAITVFTGVPTVytrlLQGYDTMN 374
Cdd:cd17655 183 LFASIS-----FDAsvteIFASLLSGNTLYIVRKETVLDG-QALTQYI------RQNRITIIDLTPAH----LKLLDAAD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 375 PDEQSacsyaakQLRLMMCGSSALPSPLMKRWEEVTGH--RLLERYGMTEFVMALSNPLHGPRKEGTV----GKPLPRVE 448
Cdd:cd17655 247 DSEGL-------SLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETTVDASIYQYEPETDQQVsvpiGKPLGNTR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 449 AKIIMDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGF------FKTGDTVTIDEDGYFKILGRTNADImKV 521
Cdd:cd17655 320 IYILDQYGRPQPVGVaGELYIGGEGVARGYLNRPELTAEKFVDDPFvpgermYRTGDLARWLPDGNIEFLGRIDHQV-KI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 522 GGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDvkeraeqasepaLTLQALTSWSKDKLAPYKIPTR 601
Cdd:cd17655 399 RGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKE------------LPVAQLREFLARELPDYMIPSY 466
|
490 500
....*....|....*....|
gi 2212542879 602 LYLWDSLPRNAMGKVNKKEL 621
Cdd:cd17655 467 FIKLDEIPLTPNGKVDRKAL 486
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
134-622 |
2.32e-53 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 190.66 E-value: 2.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEImesistkcstgYSLL 213
Cdd:PRK08008 58 GIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQFYPM-----------YRQI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 214 PSVESIPPK-------IESQEPLSSELTSSVSSLLAEIDNLKKIKGDDPALILYTSGTTGKPKGVVHTH-----KGILSQ 281
Cdd:PRK08008 127 QQEDATPLRhicltrvALPADDGVSSFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHynlrfAGYYSA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 282 VQI-LTEawgyqsEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGVWQRWREsYPSGVSKSndaitvftgVP 360
Cdd:PRK08008 207 WQCaLRD------DDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSARAFWGQVCK-YRATITEC---------IP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 361 -TVYTRLLQgydTMNPDEQSACsyaakqLRLMMcgsSALP-SPLMKR-WEEVTGHRLLERYGMTE-FVMALSNPLHGPRK 436
Cdd:PRK08008 271 mMIRTLMVQ---PPSANDRQHC------LREVM---FYLNlSDQEKDaFEERFGVRLLTSYGMTEtIVGIIGDRPGDKRR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 437 EGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIR---SPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILG 512
Cdd:PRK08008 339 WPSIGRPGFCYEAEIRDDHNRPLPAGeIGEICIKgvpGKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVD 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 513 RtNADIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKeraeqasepaLTLQALTSWSKDK 592
Cdd:PRK08008 419 R-RCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGET----------LSEEEFFAFCEQN 487
|
490 500 510
....*....|....*....|....*....|
gi 2212542879 593 LAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:PRK08008 488 MAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
253-622 |
3.91e-53 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 191.19 E-value: 3.91e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQ----------FLHCLPLHHVHGLFNALFAPLYSGS- 321
Cdd:PRK12492 207 DDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGqplmkegqevMIAPLPLYHIYAFTANCMCMMVSGNh 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 322 -VVEFMPKfSVRGV---WQRWResypsgvsksndaITVFTGVPTVYTRLlqgydtMNPDEQSACSYAAkqLRLMMCGSSA 397
Cdd:PRK12492 287 nVLITNPR-DIPGFikeLGKWR-------------FSALLGLNTLFVAL------MDHPGFKDLDFSA--LKLTNSGGTA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 398 LPSPLMKRWEEVTGHRLLERYGMTEFV-MALSNPLHGPRKEGTVGKPLPRVEAKIIMDDGTETKAGV-GELCIRSPSLFR 475
Cdd:PRK12492 345 LVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGErGELCIKGPQVMK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 476 EYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYG 555
Cdd:PRK12492 425 GYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKK-DLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSG 503
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2212542879 556 EVICAIIVAKedvkeraeqasEPALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:PRK12492 504 EAVKLFVVAR-----------DPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
134-625 |
4.67e-53 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 189.25 E-value: 4.67e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPL--ALSYPEVELLhvMNDSDISMVLStkehheimesiSTKCSTGYS 211
Cdd:PRK09088 43 GCVDGERLAVLARNSVWLVALHFACARVGAIYVPLnwRLSASELDAL--LQDAEPRLLLG-----------DDAVAAGRT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 212 LLPSVESIPPKIESQEPlsseltssvssllaeiDNLKKIKGDDPALILYTSGTTGKPKGVVHTHKGiLSQVQILTEAWGY 291
Cdd:PRK09088 110 DVEDLAAFIASADALEP----------------ADTPSIPPERVSLILFTSGTSGQPKGVMLSERN-LQQTAHNFGVLGR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 292 -QSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGVWQRwresypsgVSKSNDAITVFTGVPTVYTRLLQgy 370
Cdd:PRK09088 173 vDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGR--------LGDPALGITHYFCVPQMAQAFRA-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 371 dtmNPDEQSAcsyAAKQLRLMMCGSSALPSPLMKRWEEvTGHRLLERYGMTEFVMALSNPLHGPR---KEGTVGKPLPRV 447
Cdd:PRK09088 243 ---QPGFDAA---ALRHLTALFTGGAPHAAEDILGWLD-DGIPMVDGFGMSEAGTVFGMSVDCDViraKAGAAGIPTPTV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 448 EAKIIMDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRtNADIMKVGGYKL 526
Cdd:PRK09088 316 QTRVVDDQGNDCPAGVpGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDR-KKDMFISGGENV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 527 SALEIEAVLLEHDTILECAVLGLPDEAYGEV-ICAIIVAKEDvkeraeqasepALTLQALTSWSKDKLAPYKIPTRLYLW 605
Cdd:PRK09088 395 YPAEIEAVLADHPGIRECAVVGMADAQWGEVgYLAIVPADGA-----------PLDLERIRSHLSTRLAKYKVPKHLRLV 463
|
490 500
....*....|....*....|
gi 2212542879 606 DSLPRNAMGKVNKKELKKLL 625
Cdd:PRK09088 464 DALPRTASGKLQKARLRDAL 483
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
138-624 |
5.19e-53 |
|
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: 189.08 E-value: 5.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 138 GARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKE------HHEIMEsISTKCSTGYs 211
Cdd:cd05909 31 GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQfieklkLHHLFD-VEYDARIVY- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 212 llpsVESIPPKIESQEP-LSSELTSSVSSLLAEIDNLKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWG 290
Cdd:cd05909 109 ----LEDLRAKISKADKcKAFLAGKFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 291 YQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMP-----KFSVRGVWQRwresypsgvsksndAITVFTGVPTvytr 365
Cdd:cd05909 185 PNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPnpldyKKIPELIYDK--------------KATILLGTPT---- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 366 LLQGYdtmnpdEQSACSYAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEF--VMALSNPlHGPRKEGTVGKP 443
Cdd:cd05909 247 FLRGY------ARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECspVISVNTP-QSPNKEGTVGRP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 444 LPRVEAKII-MDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDgGFFKTGDTVTIDEDGYFKILGRTNAdIMKV 521
Cdd:cd05909 320 LPGMEVKIVsVETHEEVPIGEgGLLLVRGPNVMLGYLNEPELTSFAFGD-GWYDTGDIGKIDGEGFLTITGRLSR-FAKI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 522 GGYKLSALEIEAVLLEHDTI-LECAVLGLPDEAYGEVICAIIV----AKEDVKERAEQASEPALTlqaltswskdklapy 596
Cdd:cd05909 398 AGEMVSLEAIEDILSEILPEdNEVAVVSVPDGRKGEKIVLLTTttdtDPSSLNDILKNAGISNLA--------------- 462
|
490 500
....*....|....*....|....*...
gi 2212542879 597 kIPTRLYLWDSLPRNAMGKVNKKELKKL 624
Cdd:cd05909 463 -KPSYIHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
134-622 |
5.97e-53 |
|
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: 190.01 E-value: 5.97e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHhEIMESISTKCSTGYSLL 213
Cdd:cd05970 68 GIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAED-NIPEEIEKAAPECPSKP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 214 PSVESIPPKIESQEplsseltssvsSLLAEIDNLKKI----------KGDDPALILYTSGTTGKPKGVVHTHKGILSQvq 283
Cdd:cd05970 147 KLVWVGDPVPEGWI-----------DFRKLIKNASPDferptansypCGEDILLVYFSSGTTGMPKMVEHDFTYPLGH-- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 284 ILTEAWGYQSEDQFLHcLPLHHVhGLFNALFAPLY----SGSVVeF---MPKFSVRGVWQRwresypsgVSKSNdaITVF 356
Cdd:cd05970 214 IVTAKYWQNVREGGLH-LTVADT-GWGKAVWGKIYgqwiAGAAV-FvydYDKFDPKALLEK--------LSKYG--VTTF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 357 TGVPTVYTRLLQgydtmnpdeQSACSYAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSN-PLHGPr 435
Cdd:cd05970 281 CAPPTIYRFLIR---------EDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIATfPWMEP- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 436 KEGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPS-----LFREYWKRPEVTEESFIDGgFFKTGDTVTIDEDGYFK 509
Cdd:cd05970 351 KPGSMGKPAPGYEIDLIDREGRSCEAGeEGEIVIRTSKgkpvgLFGGYYKDAEKTAEVWHDG-YYHTGDAAWMDEDGYLW 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 510 ILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVkeraeQASEpALTlQALTSWS 589
Cdd:cd05970 430 FVGRTD-DLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGY-----EPSE-ELK-KELQDHV 501
|
490 500 510
....*....|....*....|....*....|...
gi 2212542879 590 KDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:cd05970 502 KKVTAPYKYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
253-626 |
7.65e-53 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 189.88 E-value: 7.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSvvefmpkfsvR 332
Cdd:PRK13295 197 DDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGA----------T 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 333 GVWQRWRESYPSGVSKSNDAITvFTGVPTVYTrllqgYDTMNPDEQSAcsYAAKQLRLMMCGSSALPSPLMKRWEEVTGH 412
Cdd:PRK13295 267 AVLQDIWDPARAAELIRTEGVT-FTMASTPFL-----TDLTRAVKESG--RPVSSLRTFLCAGAPIPGALVERARAALGA 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 413 RLLERYGMTE----FVMALSNPLHgpRKEGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEES 487
Cdd:PRK13295 339 KIVSAWGMTEngavTLTKLDDPDE--RASTTDGCPLPGVEVRVVDADGAPLPAGqIGRLQVRGCSNFGGYLKRPQLNGTD 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 488 FidGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKed 567
Cdd:PRK13295 417 A--DGWFDTGDLARIDADGYIRISGRSK-DVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPR-- 491
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 568 vkeraeqASEPaLTLQALTSWSKD-KLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLLQ 626
Cdd:PRK13295 492 -------PGQS-LDFEEMVEFLKAqKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLR 543
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
253-622 |
8.64e-53 |
|
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: 187.25 E-value: 8.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKGILsqvqilteawGYQSEDQFLH-CLPLHH-----------VHGLFNALFAPLYSG 320
Cdd:cd05971 88 DDPALIIYTSGTTGPPKGALHAHRVLL----------GHLPGVQFPFnLFPRDGdlywtpadwawIGGLLDVLLPSLYFG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 321 -SVVEF-MPKFSVRGVWQrwresypsgVSKSNDAITVFTgVPTVYTRLLQGYDTMNPdeqsacsyAAKQLRLMMCGSSAL 398
Cdd:cd05971 158 vPVLAHrMTKFDPKAALD---------LMSRYGVTTAFL-PPTALKMMRQQGEQLKH--------AQVKLRAIATGGESL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 399 PSPLMKRWEEVTGHRLLERYGMTEFVMALSN-PLHGPRKEGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPS--LF 474
Cdd:cd05971 220 GEELLGWAREQFGVEVNEFYGQTECNLVIGNcSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGeVGEIAVELPDpvAF 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 475 REYWKRPEVTEESFIdGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAY 554
Cdd:cd05971 300 LGYWNNPSATEKKMA-GDWLLTGDLGRKDSDGYFWYVGRDD-DVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIR 377
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2212542879 555 GEVICAIIVAKEDVKERAEQASEpaltLQALTswsKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:cd05971 378 GEIVKAFVVLNPGETPSDALARE----IQELV---KTRLAAHEYPREIEFVNELPRTATGKIRRRELR 438
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
134-622 |
1.00e-52 |
|
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: 187.65 E-value: 1.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGG----VAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKCS-T 208
Cdd:cd05922 14 GGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPdP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 209 GYSLlpSVESIPPK---IESQEPLsseltssvssllaeidnlkkikGDDPALILYTSGTTGKPKGVVHTHKGILSQVQIL 285
Cdd:cd05922 94 GTVL--DADGIRAArasAPAHEVS----------------------HEDLALLLYTSGSTGSPKLVRLSHQNLLANARSI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 286 TEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVV---EFMPKfsvRGVWQRWRESypsgvsksndAITVFTGVPTV 362
Cdd:cd05922 150 AEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVltnDGVLD---DAFWEDLREH----------GATGLAGVPST 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 363 YTRLLQ-GYDTMnpdeqsacsyAAKQLRLMMCGSSALPSPLMKRWEEV-TGHRLLERYGMTEF--VMALSNPLHGPRKEG 438
Cdd:cd05922 217 YAMLTRlGFDPA----------KLPSLRYLTQAGGRLPQETIARLRELlPGAQVYVMYGQTEAtrRMTYLPPERILEKPG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 439 TVGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRtNAD 517
Cdd:cd05922 287 SIGLAIPGGEFEILDDDGTPTPPGePGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGR-RDR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 518 IMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAyGE--VICAIIVAKEDVKERAEQASEpaltlqaltswskdKLAP 595
Cdd:cd05922 366 MIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPL-GEklALFVTAPDKIDPKDVLRSLAE--------------RLPP 430
|
490 500
....*....|....*....|....*..
gi 2212542879 596 YKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:cd05922 431 YKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
129-623 |
1.60e-52 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 188.45 E-value: 1.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 129 GIDGTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPL--ALSYPEVEllHVMNDSDISMVLSTKEHHEIMESISTKC 206
Cdd:TIGR03098 41 GLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPInpLLKAEQVA--HILADCNVRLLVTSSERLDLLHPALPGC 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 207 STGYSLLPSVEsiPPKIESQEPLSSELTSSVSSLLAEIDNLKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILT 286
Cdd:TIGR03098 119 HDLRTLIIVGD--PAHASEGHPGEEPASWPKLLALGDADPPHPVIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 287 EAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVV--EF-MPKFSVRGVWQrwresypsgvsksnDAITVFTGVPTVY 363
Cdd:TIGR03098 197 TYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVlhDYlLPRDVLKALEK--------------HGITGLAAVPPLW 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 364 TRLLQgyDTMNPDeqsacsyAAKQLRLMMCGSSALPSPLMKRWEE-VTGHRLLERYGMTE-FVMALSNPLHGPRKEGTVG 441
Cdd:TIGR03098 263 AQLAQ--LDWPES-------AAPSLRYLTNSGGAMPRATLSRLRSfLPNARLFLMYGLTEaFRSTYLPPEEVDRRPDSIG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 442 KPLPRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESF-----------IDGGFFKTGDTVTIDEDGYFK 509
Cdd:TIGR03098 334 KAIPNAEVLVLREDGSECAPGeEGELVHRGALVAMGYWNDPEKTAERFrplppfpgelhLPELAVWSGDTVRRDEEGFLY 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 510 ILGRTNADImKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVkeraeqasepALTLQALTSWS 589
Cdd:TIGR03098 414 FVGRRDEMI-KTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGE----------ELDRAALLAEC 482
|
490 500 510
....*....|....*....|....*....|....
gi 2212542879 590 KDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKK 623
Cdd:TIGR03098 483 RARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
253-626 |
1.79e-52 |
|
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: 188.82 E-value: 1.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHvhglfNA------LFAPLYSGSVVEFM 326
Cdd:COG1021 184 DDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAH-----NFplsspgVLGVLYAGGTVVLA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 327 PKFSVRGVW---QRWResypsgvsksndaITVFTGVPTVYTRLLQgydtmnpdEQSACSYAAKQLRLMMCGSSALPSPLM 403
Cdd:COG1021 259 PDPSPDTAFpliERER-------------VTVTALVPPLALLWLD--------AAERSRYDLSSLRVLQVGGAKLSPELA 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 404 KRWEEVTGHRLLERYGMTEfvmALSN--PLHGPRK--EGTVGKPL-PRVEAKIIMDDGTETKAG-VGELCIRSPSLFREY 477
Cdd:COG1021 318 RRVRPALGCTLQQVFGMAE---GLVNytRLDDPEEviLTTQGRPIsPDDEVRIVDEDGNPVPPGeVGELLTRGPYTIRGY 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 478 WKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEV 557
Cdd:COG1021 395 YRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAK-DQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGER 473
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 558 ICAIIVAKedvkeraeqasEPALTLQALTSWSKDK-LAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLLQ 626
Cdd:COG1021 474 SCAFVVPR-----------GEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAALA 532
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
148-623 |
2.59e-52 |
|
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: 185.80 E-value: 2.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 148 SAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLStkehheimesistkcstgysllpsvesippkiesqe 227
Cdd:cd05973 35 TPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT------------------------------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 228 plsseltssvssllaEIDNLKKIKgDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVH 307
Cdd:cd05973 79 ---------------DAANRHKLD-SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADPGWAY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 308 GLFNALFAPLYSGSVVEFMP-KFSVRGVWQRWRESypsgvsksndAITVFTGVPTVYTRLLQGydtmnpdeqSACSYAAK 386
Cdd:cd05973 143 GLYYAITGPLALGHPTILLEgGFSVESTWRVIERL----------GVTNLAGSPTAYRLLMAA---------GAEVPARP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 387 QLRLMMCGSSALP-SPLMKRWEEVT-GHRLLERYGMTEFVMALSNPlHG---PRKEGTVGKPLPRVEAKIIMDDGTETKA 461
Cdd:cd05973 204 KGRLRRVSSAGEPlTPEVIRWFDAAlGVPIHDHYGQTELGMVLANH-HAlehPVHAGSAGRAMPGWRVAVLDDDGDELGP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 462 GV-GELCI---RSPSL-FREYWKRPEVTeesfIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLL 536
Cdd:cd05973 283 GEpGRLAIdiaNSPLMwFRGYQLPDTPA----IDGGYYLTGDTVEFDPDGSFSFIGRAD-DVITMSGYRIGPFDVESALI 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 537 EHDTILECAVLGLPDEAYGEVICAIIVAKEDVKERAEQASEpaltlqaLTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKV 616
Cdd:cd05973 358 EHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADE-------LQLHVKKRLSAHAYPRTIHFVDELPKTPSGKI 430
|
....*..
gi 2212542879 617 NKKELKK 623
Cdd:cd05973 431 QRFLLRR 437
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
249-622 |
6.24e-52 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 187.95 E-value: 6.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 249 KIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVqiLTEAWGYQSedqFLH--------CLPLHHVHGL-FNAL-FAPLY 318
Cdd:PRK08974 202 ELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANL--EQAKAAYGP---LLHpgkelvvtALPLYHIFALtVNCLlFIELG 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 319 SGSVVEFMPKfSVRGVWQRWREsYPsgvsksndaITVFTGVPTVYTRLLqgydtmNPDEQSACSYAAkqLRLMMCGSSAL 398
Cdd:PRK08974 277 GQNLLITNPR-DIPGFVKELKK-YP---------FTAITGVNTLFNALL------NNEEFQELDFSS--LKLSVGGGMAV 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 399 PSPLMKRWEEVTGHRLLERYGMTE---FVMAlsNPLHGPRKEGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPSLF 474
Cdd:PRK08974 338 QQAVAERWVKLTGQYLLEGYGLTEcspLVSV--NPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGePGELWVKGPQVM 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 475 REYWKRPEVTEEsFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAY 554
Cdd:PRK08974 416 LGYWQRPEATDE-VIKDGWLATGDIAVMDEEGFLRIVDRKK-DMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVS 493
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2212542879 555 GEVICAIIVAKedvkeraeqasEPALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:PRK08974 494 GEAVKIFVVKK-----------DPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELR 550
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
134-622 |
2.11e-51 |
|
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: 183.72 E-value: 2.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLStkeHHeimesistkcstgysll 213
Cdd:cd17649 33 GVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLLLT---HH----------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 214 psvesippkiesqeplsseltssvssllaeidnlkkikGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQS 293
Cdd:cd17649 93 --------------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 294 EDQFLHCLPLhHVHGLFNALFAPLYSGSVVEFMPKfsvrgvwQRWRESYPSGVSKSNDAITVfTGVPTVYTR-LLQGYDT 372
Cdd:cd17649 135 GDRELQFASF-NFDGAHEQLLPPLICGACVVLRPD-------ELWASADELAEMVRELGVTV-LDLPPAYLQqLAEEADR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 373 MNPDEQSAcsyaakqLRLMMCGSSALPSPLMKRWeEVTGHRLLERYGMTEFVMAlsnPL--HGPRKEGT------VGKPL 444
Cdd:cd17649 206 TGDGRPPS-------LRLYIFGGEALSPELLRRW-LKAPVRLFNAYGPTEATVT---PLvwKCEAGAARagasmpIGRPL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 445 PRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFIDGGFF-------KTGDTVTIDEDGYFKILGRTNA 516
Cdd:cd17649 275 GGRSAYILDADLNPVPVGvTGELYIGGEGLARGYLGRPELTAERFVPDPFGapgsrlyRTGDLARWRDDGVIEYLGRVDH 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 517 DImKVGGYKLSALEIEAVLLEHDTILECAVLGLPDeAYGEVICAIIVAKEDvkeraeqASEPALtLQALTSWSKDKLAPY 596
Cdd:cd17649 355 QV-KIRGFRIELGEIEAALLEHPGVREAAVVALDG-AGGKQLVAYVVLRAA-------AAQPEL-RAQLRTALRASLPDY 424
|
490 500
....*....|....*....|....*.
gi 2212542879 597 KIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:cd17649 425 MVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
130-621 |
4.68e-50 |
|
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: 180.14 E-value: 4.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 130 IDGTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTkehheimesistkcstg 209
Cdd:cd05945 33 LASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIAD----------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 210 ysllpsvesippkiesqeplsseltssvssllaeidnlkkikGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAW 289
Cdd:cd05945 96 ------------------------------------------GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 290 GYQSEDQFLHCLPLH---HVHGLFNALFAplySGSVVefmpkfSVRGVWQRWRESYPSGVSKSndAITVFTGVPTVYTRL 366
Cdd:cd05945 134 PLGPGDVFLNQAPFSfdlSVMDLYPALAS---GATLV------PVPRDATADPKQLFRFLAEH--GITVWVSTPSFAAMC 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 367 LQgydtmnpdEQSACSYAAKQLRLMM-CGSsALPSPLMKRWEEVT-GHRLLERYGMTEFVMALSnpLHGPRKEG------ 438
Cdd:cd05945 203 LL--------SPTFTPESLPSLRHFLfCGE-VLPHKTARALQQRFpDARIYNTYGPTEATVAVT--YIEVTPEVldgydr 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 439 -TVGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESF--IDG-GFFKTGDTVTIDEDGYFKILGR 513
Cdd:cd05945 272 lPIGYAKPGAKLVILDEDGRPVPPGeKGELVISGPSVSKGYLNNPEKTAAAFfpDEGqRAYRTGDLVRLEADGLLFYRGR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 514 TNADImKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEdvkeraeqASEPALTLqALTSWSKDKL 593
Cdd:cd05945 352 LDFQV-KLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKP--------GAEAGLTK-AIKAELAERL 421
|
490 500
....*....|....*....|....*...
gi 2212542879 594 APYKIPTRLYLWDSLPRNAMGKVNKKEL 621
Cdd:cd05945 422 PPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
253-623 |
5.55e-50 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 182.31 E-value: 5.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALfAPLYSGSVVEFMPKFSVR 332
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSAL-AMLMVGACHVLLPKFDAK 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 333 GVWQrwresypsgVSKSNDaITVFTGVPTVYTRLLQ-GYDTMNPDEQsacsyaaKQLRLMMCGSSALPSPLMKRWEEV-T 410
Cdd:PLN02860 251 AALQ---------AIKQHN-VTSMITVPAMMADLISlTRKSMTWKVF-------PSVRKILNGGGSLSSRLLPDAKKLfP 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 411 GHRLLERYGMTE------FvMALSNP-----------------LHGPRKEGT-VGKPLPRVEAKIIMDDGTEtkagVGEL 466
Cdd:PLN02860 314 NAKLFSAYGMTEacssltF-MTLHDPtlespkqtlqtvnqtksSSVHQPQGVcVGKPAPHVELKIGLDESSR----VGRI 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 467 CIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNADImKVGGYKLSALEIEAVLLEHDTILECAV 546
Cdd:PLN02860 389 LTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRI-KTGGENVYPEEVEAVLSQHPGVASVVV 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 547 LGLPDEAYGEVICAIIVAKED----VKERAEQASEPALTLQALTSW-SKDKLAPYKIPTRLYLW-DSLPRNAMGKVNKKE 620
Cdd:PLN02860 468 VGVPDSRLTEMVVACVRLRDGwiwsDNEKENAKKNLTLSSETLRHHcREKNLSRFKIPKLFVQWrKPFPLTTTGKIRRDE 547
|
...
gi 2212542879 621 LKK 623
Cdd:PLN02860 548 VRR 550
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
249-623 |
6.31e-50 |
|
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: 181.51 E-value: 6.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 249 KIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAW-GYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVV--EF 325
Cdd:cd05928 170 ETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWlDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVfvHH 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 326 MPKFSVRGVWQRWrESYPsgvsksndaITVFTGVPTVYTRLLQgydtmnpdeQSACSYAAKQLRLMMCGSSALPSPLMKR 405
Cdd:cd05928 250 LPRFDPLVILKTL-SSYP---------ITTFCGAPTVYRMLVQ---------QDLSSYKFPSLQHCVTGGEPLNPEVLEK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 406 WEEVTGHRLLERYGMTEFVMALSNPLHGPRKEGTVGKPLPRVEAKIIMDDG------TETKAGVGELCIRSPSLFREYWK 479
Cdd:cd05928 311 WKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGnvlppgTEGDIGIRVKPIRPFGLFSGYVD 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 480 RPEVTEESfIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVIC 559
Cdd:cd05928 391 NPEKTAAT-IRGDFYLTGDRGIMDEDGYFWFMGRAD-DVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVK 468
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2212542879 560 AIIVAKEDVKERAEQasepALTLQaLTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKK 623
Cdd:cd05928 469 AFVVLAPQFLSHDPE----QLTKE-LQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
254-621 |
1.31e-49 |
|
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: 179.45 E-value: 1.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 254 DPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHH-----VHGLFNALFAplySGSVV----- 323
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHnfplaCPGVLGTLLA---GGRVVlapdp 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 324 ---EFMPKFSVRGVwqrwresypsgvsksndaiTVFTGVPTVYTRLLQGYDTMNPDEQSacsyaakqLRLMMCGSSALPS 400
Cdd:cd05920 217 spdAAFPLIEREGV-------------------TVTALVPALVSLWLDAAASRRADLSS--------LRLLQVGGARLSP 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 401 PLMKRWEEVTGHRLLERYGMTEFVM---ALSNPlhGPRKEGTVGKPL-PRVEAKIIMDDGTETKAG-VGELCIRSPSLFR 475
Cdd:cd05920 270 ALARRVPPVLGCTLQQVFGMAEGLLnytRLDDP--DEVIIHTQGRPMsPDDEIRVVDEEGNPVPPGeEGELLTRGPYTIR 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 476 EYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYG 555
Cdd:cd05920 348 GYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIK-DQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLG 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2212542879 556 EVICAIIVAKedvkeraeqasEPALTLQALTSWSKDK-LAPYKIPTRLYLWDSLPRNAMGKVNKKEL 621
Cdd:cd05920 427 ERSCAFVVLR-----------DPPPSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
137-622 |
1.67e-49 |
|
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: 186.22 E-value: 1.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 137 RGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKCstgysLLPSV 216
Cdd:COG1020 525 PGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPV-----LALDA 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 217 ESIppkieSQEPLSSELTSsvssllaeidnlkkIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQ 296
Cdd:COG1020 600 LAL-----AAEPATNPPVP--------------VTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDR 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 297 FLHCLPLHhvhglFNA----LFAPLYSGSVVEFMPKFSVRGV--WQRWRESYpsgvsksndAITVFTGVPTVYTRLLQgy 370
Cdd:COG1020 661 VLQFASLS-----FDAsvweIFGALLSGATLVLAPPEARRDPaaLAELLARH---------RVTVLNLTPSLLRALLD-- 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 371 dtmnpdeqsACSYAAKQLRLMMCGSSALPSPLMKRWEEVTGH-RLLERYGMTEF-VMALSNPLHGPRKEG---TVGKPLP 445
Cdd:COG1020 725 ---------AAPEALPSLRLVLVGGEALPPELVRRWRARLPGaRLVNLYGPTETtVDSTYYEVTPPDADGgsvPIGRPIA 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 446 RVEAKIIMDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGF-------FKTGDTVTIDEDGYFKILGRtNAD 517
Cdd:COG1020 796 NTRVYVLDAHLQPVPVGVpGELYIGGAGLARGYLNRPELTAERFVADPFgfpgarlYRTGDLARWLPDGNLEFLGR-ADD 874
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 518 IMKVGGYK--LSalEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAkedvkeRAEQASEPALTLQALtswsKDKLAP 595
Cdd:COG1020 875 QVKIRGFRieLG--EIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVP------EAGAAAAAALLRLAL----ALLLPP 942
|
490 500
....*....|....*....|....*..
gi 2212542879 596 YKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:COG1020 943 YMVPAAVVLLLPLPLTGNGKLDRLALP 969
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
249-622 |
2.28e-48 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 177.76 E-value: 2.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 249 KIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQ-----ILTEAWGYQSEDQFLHCLPLHHVHGLF-NALFAPLYSG-- 320
Cdd:PRK08751 204 QIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQqahqwLAGTGKLEEGCEVVITALPLYHIFALTaNGLVFMKIGGcn 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 321 ---SVVEFMPKFsVRGVwQRWResypsgvsksndaITVFTGVPTVYTRLLQ--GYDTMNpdeqsacsyaAKQLRLMMCGS 395
Cdd:PRK08751 284 hliSNPRDMPGF-VKEL-KKTR-------------FTAFTGVNTLFNGLLNtpGFDQID----------FSSLKMTLGGG 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 396 SALPSPLMKRWEEVTGHRLLERYGMTEFV-MALSNPLHGPRKEGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPSL 473
Cdd:PRK08751 339 MAVQRSVAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGeIGELCIKGPQV 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 474 FREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEA 553
Cdd:PRK08751 419 MKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKK-DMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEK 497
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2212542879 554 YGEVICAIIVAKedvkeraeqasEPALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:PRK08751 498 SGEIVKVVIVKK-----------DPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
254-618 |
3.15e-48 |
|
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: 171.68 E-value: 3.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 254 DPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLfNALFAPLYSG--SVVefMPKFSv 331
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGL-NLALATFHAGgaNVV--MEKFD- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 332 rgvwqrwresyPSGVSKSNDA--ITVFTGVPTVYTRLLqgydtmnpDEQSACSYAAKQLRLMmcgsSALPSP-LMKRWEE 408
Cdd:cd17637 77 -----------PAEALELIEEekVTLMGSFPPILSNLL--------DAAEKSGVDLSSLRHV----LGLDAPeTIQRFEE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 409 VTGHRLLERYGMTE---FV-MALSNplhgpRKEGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEV 483
Cdd:cd17637 134 TTGATFWSLYGQTEtsgLVtLSPYR-----ERPGSAGRPGPLVRVRIVDDNDRPVPAGeTGEIVVRGPLVFQGYWNLPEL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 484 TEESFiDGGFFKTGDTVTIDEDGYFKILGRTNA-DIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAII 562
Cdd:cd17637 209 TAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKPEkELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVC 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2212542879 563 VAKEdvkeraeqasEPALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNK 618
Cdd:cd17637 288 VLKP----------GATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
70-625 |
8.22e-48 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 176.19 E-value: 8.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 70 SHTFMDVVREVFKHSSAHGARAAIRAdhkSYGFVqlISSAlDVHNILctkndgdSSSIKGIDGTGFLRGARIGIVAKPSA 149
Cdd:PLN02574 36 SDPNLDAVSFIFSHHNHNGDTALIDS---STGFS--ISYS-ELQPLV-------KSMAAGLYHVMGVRQGDVVLLLLPNS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 150 EFVAGIFGTWLS-GGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTkcstgysllpSVESIPPKIESQEp 228
Cdd:PLN02574 103 VYFPVIFLAVLSlGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLGV----------PVIGVPENYDFDS- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 229 LSSELTSSVSSLLAEIDNLKK--IKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILT--EAWGYQ---SEDQFLHCL 301
Cdd:PLN02574 172 KRIEFPKFYELIKEDFDFVPKpvIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVrfEASQYEypgSDNVYLAAL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 302 PLHHVHGLfnALFAP--LYSGSVVEFMPKFSVR---GVWQRWResypsgvsksndaITVFTGVPTVYTRLLQGydtmnpd 376
Cdd:PLN02574 252 PMFHIYGL--SLFVVglLSLGSTIVVMRRFDASdmvKVIDRFK-------------VTHFPVVPPILMALTKK------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 377 EQSACSYAAKQLRLMMCGSSALPSPLMKRWEEVTGH-RLLERYGMTEFVMALSNPLHGP--RKEGTVGKPLPRVEAKII- 452
Cdd:PLN02574 310 AKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHvDFIQGYGMTESTAVGTRGFNTEklSKYSSVGLLAPNMQAKVVd 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 453 MDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEI 531
Cdd:PLN02574 390 WSTGCLLPPGnCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLK-EIIKYKGFQIAPADL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 532 EAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKedvkeraeqaSEPALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRN 611
Cdd:PLN02574 469 EAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRR----------QGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKS 538
|
570
....*....|....
gi 2212542879 612 AMGKVNKKELKKLL 625
Cdd:PLN02574 539 PAGKILRRELKRSL 552
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
253-625 |
1.52e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 174.84 E-value: 1.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHkGILSQVqiLTEAW-----GYQSEDQFLHCLPLHH---VHGLFNALFAplySGSVVE 324
Cdd:PRK07470 163 DDPCWFFFTSGTTGRPKAAVLTH-GQMAFV--ITNHLadlmpGTTEQDASLVVAPLSHgagIHQLCQVARG---AATVLL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 325 FMPKFSVRGVWQ---RWRESypsgvsksndaiTVFTgVPTVYTRLLQGYDTMNPDEQS--------ACSYAAKQlrlmmc 393
Cdd:PRK07470 237 PSERFDPAEVWAlveRHRVT------------NLFT-VPTILKMLVEHPAVDRYDHSSlryviyagAPMYRADQ------ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 394 gssalpsplmKRWEEVTGHRLLERYGMTEF---VMALSNPLH----GPR-KEGTVGKPLPRVEAKIIMDDGTETKAG-VG 464
Cdd:PRK07470 298 ----------KRALAKLGKVLVQYFGLGEVtgnITVLPPALHdaedGPDaRIGTCGFERTGMEVQIQDDEGRELPPGeTG 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 465 ELCIRSPSLFREYWKRPEVTEESFIDgGFFKTGDTVTIDEDGYFKILGRTnADIMKVGGYKLSALEIEAVLLEHDTILEC 544
Cdd:PRK07470 368 EICVIGPAVFAGYYNNPEANAKAFRD-GWFRTGDLGHLDARGFLYITGRA-SDMYISGGSNVYPREIEEKLLTHPAVSEV 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 545 AVLGLPDEAYGEVICAIIVAKEDVkeraeqasepALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKL 624
Cdd:PRK07470 446 AVLGVPDPVWGEVGVAVCVARDGA----------PVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
.
gi 2212542879 625 L 625
Cdd:PRK07470 516 L 516
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
134-622 |
2.20e-47 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 174.95 E-value: 2.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFG-TWLsGGVAVPLALSYPEVELLHVMNDSDISMVlstkehheIMESistkcstgySL 212
Cdd:PRK06155 67 GVKRGDRVALMCGNRIEFLDVFLGcAWL-GAIAVPINTALRGPQLEHILRNSGARLL--------VVEA---------AL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 213 LPSVESIPPKIESQEPLSSELTSSVSSLLAEIDNLK-----------KIKGDDPALILYTSGTTGKPKGVVHTHK----- 276
Cdd:PRK06155 129 LAALEAADPGDLPLPAVWLLDAPASVSVPAGWSTAPlppldapapaaAVQPGDTAAILYTSGTTGPSKGVCCPHAqfyww 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 277 GILSqvqilTEAWGYQSEDQFLHCLPLHHVHGLfNALFAPLYSGSVVEFMPKFSVRGVWQRWRESypsgvsksNDAITVF 356
Cdd:PRK06155 209 GRNS-----AEDLEIGADDVLYTTLPLFHTNAL-NAFFQALLAGATYVLEPRFSASGFWPAVRRH--------GATVTYL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 357 TG--VPTVYTRllqgydTMNPDEQsacsyaAKQLRLMMCGssALPSPLMKRWEEVTGHRLLERYGMTE--FVMALSnplH 432
Cdd:PRK06155 275 LGamVSILLSQ------PARESDR------AHRVRVALGP--GVPAALHAAFRERFGVDLLDGYGSTEtnFVIAVT---H 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 433 GPRKEGTVGKPLPRVEAKIIMDDGTETKAGV-GELCIRS--PSLFRE-YWKRPEVTEESFIDGgFFKTGDTVTIDEDGYF 508
Cdd:PRK06155 338 GSQRPGSMGRLAPGFEARVVDEHDQELPDGEpGELLLRAdePFAFATgYFGMPEKTVEAWRNL-WFHTGDRVVRDADGWF 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 509 KILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDE-AYGEVICAIIVakedvkeRAEQASEPaltlQALTS 587
Cdd:PRK06155 417 RFVDRIK-DAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSElGEDEVMAAVVL-------RDGTALEP----VALVR 484
|
490 500 510
....*....|....*....|....*....|....*
gi 2212542879 588 WSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:PRK06155 485 HCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLR 519
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
138-621 |
3.10e-47 |
|
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: 172.86 E-value: 3.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 138 GARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEhheIMESISTKCSTgysLLPSVE 217
Cdd:cd12116 37 GDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTDDA---LPDRLPAGLPV---LLLALA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 218 SIPPKIESQEPLSSeltssvssllaeidnlkkikGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQF 297
Cdd:cd12116 111 AAAAAPAAPRTPVS--------------------PDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 298 LHCL-PLHHVHGLfnALFAPLYSGSVVEFMPKFSVRGvwqrwresyPSGVSK--SNDAITVFTGVPTVYTRLLQ-GYDtm 373
Cdd:cd12116 171 LAVTtYAFDISLL--ELLLPLLAGARVVIAPRETQRD---------PEALARliEAHSITVMQATPATWRMLLDaGWQ-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 374 npdeqsacsyAAKQLRLMmCGSSALPSPLMKRWEEVTGhRLLERYGMTE-FVMALSNPLHGPRKEGTVGKPLPRVEAKII 452
Cdd:cd12116 238 ----------GRAGLTAL-CGGEALPPDLAARLLSRVG-SLWNLYGPTEtTIWSTAARVTAAAGPIPIGRPLANTQVYVL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 453 MDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGF-------FKTGDTVTIDEDGYFKILGRTNADImKVGGY 524
Cdd:cd12116 306 DAALRPVPPGVpGELYIGGDGVAQGYLGRPALTAERFVPDPFagpgsrlYRTGDLVRRRADGRLEYLGRADGQV-KIRGH 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 525 KLSALEIEAVLLEHDTILECAVLGLPDEAyGEVICAIIVAKEDvkeraeqasePALTLQALTSWSKDKLAPYKIPTRLYL 604
Cdd:cd12116 385 RIELGEIEAALAAHPGVAQAAVVVREDGG-DRRLVAYVVLKAG----------AAPDAAALRAHLRATLPAYMVPSAFVR 453
|
490
....*....|....*..
gi 2212542879 605 WDSLPRNAMGKVNKKEL 621
Cdd:cd12116 454 LDALPLTANGKLDRKAL 470
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
132-622 |
3.50e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 173.15 E-value: 3.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 132 GTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKCSTGYS 211
Cdd:PRK06145 46 ARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEEFDAIVALETPKIVIDAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 212 LLPSV-------ESIPPKIESQEplsseltssvssllaeidnlkkikgDDPALILYTSGTTGKPKGVVHTHKGILSQVQI 284
Cdd:PRK06145 126 AQADSrrlaqggLEIPPQAAVAP-------------------------TDLVRLMYTSGTTDRPKGVMHSYGNLHWKSID 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 285 LTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGVWQrwresypsgvSKSNDAITVFTGVPTVYT 364
Cdd:PRK06145 181 HVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLA----------AIERHRLTCAWMAPVMLS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 365 RLLQGYDtmnPDEqsacsYAAKQLRLMMCGSSALPSPLMKRWEEV-TGHRLLERYGMTEFV-----MALSNPLHgprKEG 438
Cdd:PRK06145 251 RVLTVPD---RDR-----FDLDSLAWCIGGGEKTPESRIRDFTRVfTRARYIDAYGLTETCsgdtlMEAGREIE---KIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 439 TVGKPLPRVEAKIIMDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIdGGFFKTGDTVTIDEDGYFKILGRTNaD 517
Cdd:PRK06145 320 STGRALAHVEIRIADGAGRWLPPNMkGEICMRGPKVTKGYWKDPEKTAEAFY-GDWFRSGDVGYLDEEGFLYLTDRKK-D 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 518 IMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVkeraeqasepALTLQALTSWSKDKLAPYK 597
Cdd:PRK06145 398 MIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGA----------TLTLEALDRHCRQRLASFK 467
|
490 500
....*....|....*....|....*
gi 2212542879 598 IPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:PRK06145 468 VPRQLKVRDELPRNPSGKVLKRVLR 492
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
131-580 |
4.02e-47 |
|
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: 172.24 E-value: 4.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 131 DGTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEhheimesistkcstgy 210
Cdd:cd05914 25 KINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSDE---------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 211 sllpsvesippkiesqeplsseltssvssllaeidnlkkikgDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWG 290
Cdd:cd05914 89 ------------------------------------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 291 YQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVrgvwqrwresyPSGVSKSNDAITVFTGVPTVYTrLLQGY 370
Cdd:cd05914 127 LGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPS-----------AKIIALAFAQVTPTLGVPVPLV-IEKIF 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 371 --DTMN--------------PDEQSACSYAAKQL--------RLMMCGSSALPSPLMKRWEEVtGHRLLERYGMTEFVMA 426
Cdd:cd05914 195 kmDIIPkltlkkfkfklakkINNRKIRKLAFKKVheafggniKEFVIGGAKINPDVEEFLRTI-GFPYTIGYGMTETAPI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 427 LSNPLHGPRKEGTVGKPLPRVEAKIimdDGTETKAGVGELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDG 506
Cdd:cd05914 274 ISYSPPNRIRLGSAGKVIDGVEVRI---DSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEG 350
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2212542879 507 YFKILGRTNADIMKVGGYKLSALEIEAVLLEHDTILECAVLglpDEAYGEVICAII-VAKEDVKERAEQASEPAL 580
Cdd:cd05914 351 YLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVV---VQEKKLVALAYIdPDFLDVKALKQRNIIDAI 422
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
128-624 |
4.27e-47 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 174.23 E-value: 4.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 128 KGIDGTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLS-----TKEHHEIMESI 202
Cdd:PRK08315 58 KGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAadgfkDSDYVAMLYEL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 203 STKCST---GY---SLLPSVESI----PPKIESQEPLSSELTSSVSSLLAEIDNLKK-IKGDDPALILYTSGTTGKPKGV 271
Cdd:PRK08315 138 APELATcepGQlqsARLPELRRViflgDEKHPGMLNFDELLALGRAVDDAELAARQAtLDPDDPINIQYTSGTTGFPKGA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 272 VHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGS-----VVEFMPKFSVRGVwqrwresypsgv 346
Cdd:PRK08315 218 TLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLYHCFGMVLGNLACVTHGAtmvypGEGFDPLATLAAV------------ 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 347 skSNDAITVFTGVPTVYTRLLQGYDTMNPDEQSacsyaakqLRL-MMCGSSAlPSPLMKR------WEEVTghrllERYG 419
Cdd:PRK08315 286 --EEERCTALYGVPTMFIAELDHPDFARFDLSS--------LRTgIMAGSPC-PIEVMKRvidkmhMSEVT-----IAYG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 420 MTE-----FVMALSNPLHgpRKEGTVGKPLPRVEAKII-MDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGG 492
Cdd:PRK08315 350 MTEtspvsTQTRTDDPLE--KRVTTVGRALPHLEVKIVdPETGETVPRGEqGELCTRGYSVMKGYWNDPEKTAEAIDADG 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 493 FFKTGDTVTIDEDGYFKILGRtNADIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVkera 572
Cdd:PRK08315 428 WMHTGDLAVMDEEGYVNIVGR-IKDMIIRGGENIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGA---- 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2212542879 573 eqasepALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKL 624
Cdd:PRK08315 503 ------TLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREM 548
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
134-621 |
2.82e-46 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 170.46 E-value: 2.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEhheimesistkcSTGYSLL 213
Cdd:cd12117 43 GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLTDRS------------LAGRAGG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 214 PSVESIPPKIESQEPLSSELTSsvssllaeidnlkkIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQ-----ILTEa 288
Cdd:cd12117 111 LEVAVVIDEALDAGPAGNPAVP--------------VSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKntnyvTLGP- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 289 wgyqsEDQFLHCLPLHhvhglFNA----LFAPLYSGSVVEFMPKFSVRGvwqrwresypsgvsksndaitvftgvPTVYT 364
Cdd:cd12117 176 -----DDRVLQTSPLA-----FDAstfeIWGALLNGARLVLAPKGTLLD--------------------------PDALG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 365 RLL--QGYDTM-------N--PDEQSACsyaAKQLRLMMCGSSALPSPLMKRWEEVTGH-RLLERYGMTE-FVMALSNPL 431
Cdd:cd12117 220 ALIaeEGVTVLwltaalfNqlADEDPEC---FAGLRELLTGGEVVSPPHVRRVLAACPGlRLVNGYGPTEnTTFTTSHVV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 432 HGPRKEGT---VGKPLPRVEAKIIMDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGF------FKTGDTVT 501
Cdd:cd12117 297 TELDEVAGsipIGRPIANTRVYVLDEDGRPVPPGVpGELYVGGDGLALGYLNRPALTAERFVADPFgpgerlYRTGDLAR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 502 IDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAkedvkeraeqasEPALT 581
Cdd:cd12117 377 WLPDGRLEFLGRID-DQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVA------------EGALD 443
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2212542879 582 LQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 621
Cdd:cd12117 444 AAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
254-616 |
2.65e-45 |
|
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: 163.35 E-value: 2.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 254 DPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFApLYSGSVVEFMPKFSVRG 333
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISA-LYLGGTFIGQRKFNPKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 334 VWqRWRESYpsgvsksndAITVFTGVPTVYTRLLQGYDTMNPdeqsacsyaakqLRLMMCGSSALPSPLMKRWEEVTGH- 412
Cdd:cd17633 80 WI-RKINQY---------NATVIYLVPTMLQALARTLEPESK------------IKSIFSSGQKLFESTKKKLKNIFPKa 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 413 RLLERYGMTE--FVMALSNplHGPRKEGTVGKPLPRVEAKIIMDDGTEtkagVGELCIRSPSLFREYWKRPEVTEesfid 490
Cdd:cd17633 138 NLIEFYGTSElsFITYNFN--QESRPPNSVGRPFPNVEIEIRNADGGE----IGKIFVKSEMVFSGYVRGGFSNP----- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 491 GGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEdvke 570
Cdd:cd17633 207 DGWMSVGDIGYVDEEGYLYLVGRES-DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDK---- 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2212542879 571 raeqasepaLTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKV 616
Cdd:cd17633 282 ---------LTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
253-623 |
8.11e-45 |
|
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: 166.32 E-value: 8.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKGI----LSQVQilteAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVeFMPK 328
Cdd:cd12118 133 WDPIALNYTSGTTGRPKGVVYHHRGAylnaLANIL----EWEMKQHPVYLWTLPMFHCNGWCFPWTVAAVGGTNV-CLRK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 329 FSVRGVWQRWREsypsgvsksnDAITVFTGVPTVYTRLLqgydtmNPDEQSACSYAAKQLrlMMCGSSALPSPLMKRWEE 408
Cdd:cd12118 208 VDAKAIYDLIEK----------HKVTHFCGAPTVLNMLA------NAPPSDARPLPHRVH--VMTAGAPPPAAVLAKMEE 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 409 VtGHRLLERYGMTEFV--------MALSNPLHGPR------KEG--------------TVGKPLPRveakiimdDGTEtk 460
Cdd:cd12118 270 L-GFDVTHVYGLTETYgpatvcawKPEWDELPTEErarlkaRQGvryvgleevdvldpETMKPVPR--------DGKT-- 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 461 agVGELCIRSPSLFREYWKRPEVTEESFiDGGFFKTGDTVTIDEDGYFKILGRtNADIMKVGGYKLSALEIEAVLLEHDT 540
Cdd:cd12118 339 --IGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDR-SKDIIISGGENISSVEVEGVLYKHPA 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 541 ILECAVLGLPDEAYGEVICAIIVAKEDVKERAEQasepaltlqaLTSWSKDKLAPYKIPtRLYLWDSLPRNAMGKVNKKE 620
Cdd:cd12118 415 VLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEE----------IIAFCREHLAGFMVP-KTVVFGELPKTSTGKIQKFV 483
|
...
gi 2212542879 621 LKK 623
Cdd:cd12118 484 LRD 486
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
134-622 |
4.65e-44 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 165.84 E-value: 4.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKE--HHEIMESistkcstgys 211
Cdd:PRK04319 94 GVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPAllERKPADD---------- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 212 lLPSVESIPPKIESQEPLSSELTSSVSSLLA----EIDNLKKikgDDPALILYTSGTTGKPKGVVHTHKGILSQVQilTE 287
Cdd:PRK04319 164 -LPSLKHVLLVGEDVEEGPGTLDFNALMEQAsdefDIEWTDR---EDGAILHYTSGSTGKPKGVLHVHNAMLQHYQ--TG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 288 AWGyqsedqflhcLPLHH------------VHGLFNALFAPLYSG--SVV---EFMPKFsvrgvWQRWRESYpsgvsksn 350
Cdd:PRK04319 238 KYV----------LDLHEddvywctadpgwVTGTSYGIFAPWLNGatNVIdggRFSPER-----WYRILEDY-------- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 351 dAITVFTGVPTVYTRLlqgydtMNPDEQSACSYAAKQLRLMMCGSSALpSPLMKRW-EEVTGHRLLERYGMTEF--VMaL 427
Cdd:PRK04319 295 -KVTVWYTAPTAIRML------MGAGDDLVKKYDLSSLRHILSVGEPL-NPEVVRWgMKVFGLPIHDNWWMTETggIM-I 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 428 SNPLHGPRKEGTVGKPLPRVEAKIIMDDGTETKAGV-GELCIRS--PSLFREYWKRPEVTEESFIdGGFFKTGDTVTIDE 504
Cdd:PRK04319 366 ANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRmGNLAIKKgwPSMMRGIWNNPEKYESYFA-GDWYVSGDSAYMDE 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 505 DGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVkeraeqasEPALTLQA 584
Cdd:PRK04319 445 DGYFWFQGRVD-DVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGY--------EPSEELKE 515
|
490 500 510
....*....|....*....|....*....|....*....
gi 2212542879 585 -LTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:PRK04319 516 eIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLK 554
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
138-621 |
1.21e-43 |
|
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: 162.48 E-value: 1.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 138 GARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTkehheimesistkcstgysllpsve 217
Cdd:cd17643 37 GDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLLTD------------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 218 sippkiesqeplsseltssvssllaeidnlkkikGDDPALILYTSGTTGKPKGVVHTHKGILSqvqiL---TEAW-GYQS 293
Cdd:cd17643 92 ----------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLA----LfaaTQRWfGFNE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 294 EDQFLHClplHH------VHGLFNALfapLYSGSVVefMPKFSVRgvwqRWRESYPSGVSKsnDAITVFTGVPTVYTRLL 367
Cdd:cd17643 134 DDVWTLF---HSyafdfsVWEIWGAL---LHGGRLV--VVPYEVA----RSPEDFARLLRD--EGVTVLNQTPSAFYQLV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 368 QGYDTMNPDEQSacsyaakqLRLMMCGSSALPSPLMKRWEEVTGH---RLLERYGMTE---FVM--ALSNPLHGPRKEGT 439
Cdd:cd17643 200 EAADRDGRDPLA--------LRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITEttvHVTfrPLDAADLPAAAASP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 440 VGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFIDGGF-------FKTGDTVTIDEDGYFKIL 511
Cdd:cd17643 272 IGRPLPGLRVYVLDADGRPVPPGvVGELYVSGAGVARGYLGRPELTAERFVANPFggpgsrmYRTGDLARRLPDGELEYL 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 512 GRTNADImKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKERAEqasepaltlqALTSWSKD 591
Cdd:cd17643 352 GRADEQV-KIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIA----------ELRALLKE 420
|
490 500 510
....*....|....*....|....*....|
gi 2212542879 592 KLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 621
Cdd:cd17643 421 LLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
254-624 |
2.74e-43 |
|
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: 164.27 E-value: 2.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 254 DPALILYTSGTTGKPKGVVHTHKGILSQVQiLTEAW--GYQSEDQFLHCLPLHHVHGLFNALFAPLYSG--SVV-EFMPK 328
Cdd:cd05966 232 DPLFILYTSGSTGKPKGVVHTTGGYLLYAA-TTFKYvfDYHPDDIYWCTADIGWITGHSYIVYGPLANGatTVMfEGTPT 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 329 FSVRGVW----QRWResypsgvsksndaITVFTGVPTVyTRLLQGYDTMNPDeqsacSYAAKQLRLMmcGSSALP-SPLM 403
Cdd:cd05966 311 YPDPGRYwdivEKHK-------------VTIFYTAPTA-IRALMKFGDEWVK-----KHDLSSLRVL--GSVGEPiNPEA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 404 KRW-EEVTGHR---LLERYGMTEFVMALSNPLHG--PRKEGTVGKPLPRVEAKIIMDDGTETKAGV-GELCIRS--PSLF 474
Cdd:cd05966 370 WMWyYEVIGKErcpIVDTWWQTETGGIMITPLPGatPLKPGSATRPFFGIEPAILDEEGNEVEGEVeGYLVIKRpwPGMA 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 475 REYWKRPEVTEESFI--DGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDE 552
Cdd:cd05966 450 RTIYGDHERYEDTYFskFPGYYFTGDGARRDEDGYYWITGRVD-DVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHD 528
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2212542879 553 AYGEVICAIIVAKEDVKERAEQASEpaltlqaLTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKL 624
Cdd:cd05966 529 IKGEAIYAFVTLKDGEEPSDELRKE-------LRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKI 593
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
137-621 |
3.70e-43 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 161.67 E-value: 3.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 137 RGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKCSTGYSLLPSV 216
Cdd:cd17646 47 PEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 217 ESIPPKIESQeplsseltssvssllaeidnlkkikGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQ 296
Cdd:cd17646 127 PATPPLVPPR-------------------------PDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 297 FLHCLPLHhvhglF----NALFAPLYSGSVV-----------EFMPKFSVRgvwqrwresypsgvsksnDAITVFTGVPT 361
Cdd:cd17646 182 VLQKTPLS-----FdvsvWELFWPLVAGARLvvarpgghrdpAYLAALIRE------------------HGVTTCHFVPS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 362 VYTRLLQgydtmNPDEQSACSyaakqLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSN-PLHGPRKEGTV 440
Cdd:cd17646 239 MLRVFLA-----EPAAGSCAS-----LRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHwPVRGPAETPSV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 441 --GKPLPRVEAKIIMDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGF------FKTGDTVTIDEDGYFKIL 511
Cdd:cd17646 309 piGRPVPNTRLYVLDDALRPVPVGVpGELYLGGVQLARGYLGRPALTAERFVPDPFgpgsrmYRTGDLARWRPDGALEFL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 512 GRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAkedvkeraeQASEPALTLQALTSWSKD 591
Cdd:cd17646 389 GRSD-DQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVP---------AAGAAGPDTAALRAHLAE 458
|
490 500 510
....*....|....*....|....*....|
gi 2212542879 592 KLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 621
Cdd:cd17646 459 RLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
254-618 |
1.43e-42 |
|
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: 156.65 E-value: 1.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 254 DPALILYTSGTTGKPKGVVHTHKGILSQVQIL-TEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVR 332
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILqKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 333 GVWQrwresypsgVSKSNDAiTVFTGVPTVYTRLLQGYDTMNPDeqsacsyaAKQLRLMMCGSSaLPSPLMKRWEEVTGH 412
Cdd:cd17635 82 SLFK---------ILTTNAV-TTTCLVPTLLSKLVSELKSANAT--------VPSLRLIGYGGS-RAIAADVRFIEATGL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 413 -RLLERYGMTEFVMALSNPLHGPRKE-GTVGKPLPRVEAKIIMDDGTET-KAGVGELCIRSPSLFREYWKRPEVTEESFI 489
Cdd:cd17635 143 tNTAQVYGLSETGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGpSASFGTIWIKSPANMLGYWNNPERTAEVLI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 490 DGgFFKTGDTVTIDEDGYFKILGRTnADIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAkedvk 569
Cdd:cd17635 223 DG-WVNTGDLGERREDGFLFITGRS-SESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA----- 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2212542879 570 erAEQASEPALTLQALTswSKDKLAPYKIPTRLYLWDSLPRNAMGKVNK 618
Cdd:cd17635 296 --SAELDENAIRALKHT--IRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
248-624 |
3.15e-42 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 161.65 E-value: 3.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 248 KKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQiLTEAW--GYQSEDQFLHCLPLHHVHGLFNALFAPLYSGS---V 322
Cdd:TIGR02188 232 EPMDSEDPLFILYTSGSTGKPKGVLHTTGGYLLYAA-MTMKYvfDIKDGDIFWCTADVGWITGHSYIVYGPLANGAttvM 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 323 VEFMPKFSVRGVWQRWRESYpsgvsksndAITVFTGVPTVyTRLLQGYDTMNPDeqsacSYAAKQLRLMmcGSSALP-SP 401
Cdd:TIGR02188 311 FEGVPTYPDPGRFWEIIEKH---------KVTIFYTAPTA-IRALMRLGDEWVK-----KHDLSSLRLL--GSVGEPiNP 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 402 LMKRW--EEVTGHR--LLERYGMTEFVMALSNPLHG--PRKEGTVGKPLPRVEAKIIMDDGTE-TKAGV-GELCIRS--P 471
Cdd:TIGR02188 374 EAWMWyyKVVGKERcpIVDTWWQTETGGIMITPLPGatPTKPGSATLPFFGIEPAVVDEEGNPvEGPGEgGYLVIKQpwP 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 472 SLFREYWKRPEVTEESFIDG--GFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGL 549
Cdd:TIGR02188 454 GMLRTIYGDHERFVDTYFSPfpGYYFTGDGARRDKDGYIWITGRVD-DVINVSGHRLGTAEIESALVSHPAVAEAAVVGI 532
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2212542879 550 PDEAYGEVICAIIVAKEDVKERAEQASEpaltlqaLTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKL 624
Cdd:TIGR02188 533 PDDIKGQAIYAFVTLKDGYEPDDELRKE-------LRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRKI 600
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
136-580 |
1.00e-41 |
|
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: 158.94 E-value: 1.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 136 LRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVE---LLHVMNDSDISMVLSTKEHHE-IMESISTKCSTGYS 211
Cdd:cd05931 46 KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPRVVLTTAAALAaVRAFAASRPAAGTP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 212 LLPSVESIPPKIESQEPLSseltssvssllaeidnlkKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGY 291
Cdd:cd05931 126 RLLVVDLLPDTSAADWPPP------------------SPDPDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 292 QSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFS-VR--GVWQRWRESYPSgvsksndaitVFTGVPTVytrllq 368
Cdd:cd05931 188 DPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAfLRrpLRWLRLISRYRA----------TISAAPNF------ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 369 GYD---TMNPDEQsACSYAAKQLRLMMCGSSALPSPLMKRWEE------------------------VTGHRLLERYGMT 421
Cdd:cd05931 252 AYDlcvRRVRDED-LEGLDLSSWRVALNGAEPVRPATLRRFAEafapfgfrpeafrpsyglaeatlfVSGGPPGTGPVVL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 422 EF-VMALSNPLHGPRKEGT-------VGKPLPRVEAKIImDDGTETK---AGVGELCIRSPSLFREYWKRPEVTEESFI- 489
Cdd:cd05931 331 RVdRDALAGRAVAVAADDPaarelvsCGRPLPDQEVRIV-DPETGRElpdGEVGEIWVRGPSVASGYWGRPEATAETFGa 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 490 -----DGGFFKTGDTVTIDeDGYFKILGRTnADIMKVGGYKLSALEIEAVLLEHDTILE---CAVLGLPDEAYGEVicaI 561
Cdd:cd05931 410 laatdEGGWLRTGDLGFLH-DGELYITGRL-KDLIIVRGRNHYPQDIEATAEEAHPALRpgcVAAFSVPDDGEERL---V 484
|
490
....*....|....*....
gi 2212542879 562 IVAkeDVKERAEQASEPAL 580
Cdd:cd05931 485 VVA--EVERGADPADLAAI 501
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
140-626 |
1.03e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 157.63 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 140 RIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKehheimesistkcstgYSLLPSVESI 219
Cdd:PRK07638 52 TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTER----------------YKLNDLPDEE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 220 PPKIESQEplSSELTSSVSSLLAEIDNLkkikGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLH 299
Cdd:PRK07638 116 GRVIEIDE--WKRMIEKYLPTYAPIENV----QNAPFYMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 300 CLPLHHVHGLFNALFApLYSGSVVEFMPKFSvrgvwqrwresyPSGVSKS--NDAITVFTGVPTVYTRLLQGYDTMNpDE 377
Cdd:PRK07638 190 AGTLVHSLFLYGAIST-LYVGQTVHLMRKFI------------PNQVLDKleTENISVMYTVPTMLESLYKENRVIE-NK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 378 QSACSYAAKqlrlmmcgssaLPSPLMKRWEEVTGH-RLLERYGMTE--FVMALSnPLHGPRKEGTVGKPLPRVEAKIIMD 454
Cdd:PRK07638 256 MKIISSGAK-----------WEAEAKEKIKNIFPYaKLYEFYGASElsFVTALV-DEESERRPNSVGRPFHNVQVRICNE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 455 DGTETKAG-VGELCIRSPSLFREYwKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNADIMkVGGYKLSALEIEA 533
Cdd:PRK07638 324 AGEEVQKGeIGTVYVKSPQFFMGY-IIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMIL-FGGINIFPEEIES 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 534 VLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKEraeqasepaltlqaLTSWSKDKLAPYKIPTRLYLWDSLPRNAM 613
Cdd:PRK07638 402 VLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSATKQQ--------------LKSFCLQRLSSFKIPKEWHFVDEIPYTNS 467
|
490
....*....|...
gi 2212542879 614 GKVNKKELKKLLQ 626
Cdd:PRK07638 468 GKIARMEAKSWIE 480
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
138-573 |
1.06e-41 |
|
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: 158.02 E-value: 1.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 138 GARIGIVAKPSAEFVAGIFGTWLSGGVAVPLalsYPevellhVMNDSDISMVLstkEHHEIMESISTKCSTGYSLLPSVE 217
Cdd:cd05932 31 GSKIALISKNCAEWFITDLAIWMAGHISVPL---YP------TLNPDTIRYVL---EHSESKALFVGKLDDWKAMAPGVP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 218 SIPPKIESQEPLSSELTSSVSSLLAEIDNLKKIKGDDP---ALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSE 294
Cdd:cd05932 99 EGLISISLPPPSAANCQYQWDDLIAQHPPLEERPTRFPeqlATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEEN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 295 DQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFsvrgvwqrwrESYPSGVSKSNDaiTVFTGVPTVYTRLLQG-YDTM 373
Cdd:cd05932 179 DRMLSYLPLAHVTERVFVEGGSLYGGVLVAFAESL----------DTFVEDVQRARP--TLFFSVPRLWTKFQQGvQDKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 374 NPDE----------------QSACSYAAKQLRLMMCGSSALPSPLMKrWEEVTGHRLLERYGMTE--FVMALSNPlhGPR 435
Cdd:cd05932 247 PQQKlnlllkipvvnslvkrKVLKGLGLDQCRLAGCGSAPVPPALLE-WYRSLGLNILEAYGMTEnfAYSHLNYP--GRD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 436 KEGTVGKPLPRVEAKIIMDdgtetkagvGELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTN 515
Cdd:cd05932 324 KIGTVGNAGPGVEVRISED---------GEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVK 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2212542879 516 aDIMKVGGYKLSA-LEIEAVLLEHDTILECAVLG--LPDEAYGEVICAIIVAKEDVKERAE 573
Cdd:cd05932 395 -DIFKTSKGKYVApAPIENKLAEHDRVEMVCVIGsgLPAPLALVVLSEEARLRADAFARAE 454
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
251-566 |
1.95e-41 |
|
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: 157.38 E-value: 1.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 251 KGDDPALILYTSGTTGKPKGVVHTHK----GILSQVQILTEAWGyqSEDQFLHCLPLHHV-----------HG------- 308
Cdd:cd17639 86 KPDDLACIMYTSGSTGNPKGVMLTHGnlvaGIAGLGDRVPELLG--PDDRYLAYLPLAHIfelaaenvclyRGgtigygs 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 309 ---LFNALFAPLYsGSVVEFMPKF--SVRGVWQRWREsypsGV-SKSNDAITVFTGV-PTVYTR----LLQGYDTMNPDE 377
Cdd:cd17639 164 prtLTDKSKRGCK-GDLTEFKPTLmvGVPAIWDTIRK----GVlAKLNPMGGLKRTLfWTAYQSklkaLKEGPGTPLLDE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 378 ---QSACSYAAKQLRLMMCGSSALpSPLMKRWEEVTGHRLLERYGMTEFV--MALSNPlhGPRKEGTVGKPLPRVEAKII 452
Cdd:cd17639 239 lvfKKVRAALGGRLRYMLSGGAPL-SADTQEFLNIVLCPVIQGYGLTETCagGTVQDP--GDLETGRVGPPLPCCEIKLV 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 453 -MDDG---TETKAGVGELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKV--GGYkl 526
Cdd:cd17639 316 dWEEGgysTDKPPPRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKK-DLVKLqnGEY-- 392
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2212542879 527 SALE-IEAVLLEHDTILECAVLGLPDEAYgevICAIIVAKE 566
Cdd:cd17639 393 IALEkLESIYRSNPLVNNICVYADPDKSY---PVAIVVPNE 430
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
134-621 |
5.71e-41 |
|
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: 155.58 E-value: 5.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLStkehHEimesistkcstGYSLL 213
Cdd:cd17651 41 GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLT----HP-----------ALAGE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 214 PSVESIPPKIESQEPLSSEltssvssllAEIDNLKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQS 293
Cdd:cd17651 106 LAVELVAVTLLDQPGAAAG---------ADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 294 EDQFLHCLPLHhvhglFNA----LFAPLYSGSVVEFMP---KFSVRGVWQRWRESypsgvsksndAIT-VFtgVPTVYTR 365
Cdd:cd17651 177 GARTLQFAGLG-----FDVsvqeIFSTLCAGATLVLPPeevRTDPPALAAWLDEQ----------RISrVF--LPTVALR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 366 LLqgydTMNPDEQSACSYAakqLRLMMCGSSALP-SPLMKRW-EEVTGHRLLERYGMTE--FVMA--LSNPLHGPRKEGT 439
Cdd:cd17651 240 AL----AEHGRPLGVRLAA---LRYLLTGGEQLVlTEDLREFcAGLPGLRLHNHYGPTEthVVTAlsLPGDPAAWPAPPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 440 VGKPLPRVEAKIIMDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGF------FKTGDTVTIDEDGYFKILG 512
Cdd:cd17651 313 IGRPIDNTRVYVLDAALRPVPPGVpGELYIGGAGLARGYLNRPELTAERFVPDPFvpgarmYRTGDLARWLPDGELEFLG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 513 RtNADIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKERAEqasepaltlqALTSWSKDK 592
Cdd:cd17651 393 R-ADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAA----------ELRAALATH 461
|
490 500
....*....|....*....|....*....
gi 2212542879 593 LAPYKIPTRLYLWDSLPRNAMGKVNKKEL 621
Cdd:cd17651 462 LPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
254-621 |
1.24e-40 |
|
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: 154.97 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 254 DPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQ--SEDQFLHCLPLHHVHGLFNALFAPLYSGsvvefmpkfsv 331
Cdd:cd05923 151 QPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRhgRHNVVLGLMPLYHVIGFFAVLVAALALD----------- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 332 rGVWQRWRESYPSGVSK--SNDAITVFTGVPTVYTRLLqGYDTMNPDEQSAcsyaakqLRLMMCGSSALPSPLMKRWEEV 409
Cdd:cd05923 220 -GTYVVVEEFDPADALKliEQERVTSLFATPTHLDALA-AAAEFAGLKLSS-------LRHVTFAGATMPDAVLERVNQH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 410 TGHRLLERYGMTEFVMALSNPlhgPRKEGTVGKPLPRVEAKIIMDDGTETKA---GV-GELCIR--SPSLFREYWKRPEV 483
Cdd:cd05923 291 LPGEKVNIYGTTEAMNSLYMR---DARTGTEMRPGFFSEVRIVRIGGSPDEAlanGEeGELIVAaaADAAFTGYLNQPEA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 484 TEESFIDGGFFkTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIV 563
Cdd:cd05923 368 TAKKLQDGWYR-TGDVGYVDPSGDVRILGRVD-DMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVV 445
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2212542879 564 AKEdvkeraEQASEPALTLQALTSwskdKLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 621
Cdd:cd05923 446 PRE------GTLSADELDQFCRAS----ELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
256-622 |
7.72e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 152.75 E-value: 7.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 256 ALILYTSGTTGKPKGVVH--THKGI---LSQVQILTEAWGYQSEDQ-FLHCLPLHHVhglfnalfAPL-YSGSV------ 322
Cdd:PRK08276 143 ADMLYSSGTTGRPKGIKRplPGLDPdeaPGMMLALLGFGMYGGPDSvYLSPAPLYHT--------APLrFGMSAlalggt 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 323 VEFMPKFSVRGVW---QRWResypsgvsksndaITVFTGVPTVYTRLLQgydtmNPDEQSAcSYAAKQLRLMMCGSSALP 399
Cdd:PRK08276 215 VVVMEKFDAEEALaliERYR-------------VTHSQLVPTMFVRMLK-----LPEEVRA-RYDVSSLRVAIHAAAPCP 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 400 SPLMKRWEEVTGHRLLERYGMTEFVM-ALSNPLHGPRKEGTVGKPLpRVEAKIIMDDGTETKAG-VGELCIRSPSLFREY 477
Cdd:PRK08276 276 VEVKRAMIDWWGPIIHEYYASSEGGGvTVITSEDWLAHPGSVGKAV-LGEVRILDEDGNELPPGeIGTVYFEMDGYPFEY 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 478 WKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRtNADIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEV 557
Cdd:PRK08276 355 HNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLTDR-KSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGER 433
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2212542879 558 ICAIIVAKEDVKERAEQASEpaltlqaLTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:PRK08276 434 VKAVVQPADGADAGDALAAE-------LIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLR 491
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
140-624 |
1.49e-39 |
|
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: 152.30 E-value: 1.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 140 RIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKCST--GYSLLPSVE 217
Cdd:cd17642 71 RIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIikTIIILDSKE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 218 SIPPK------IESQEPLSSELTSSVSSllaEIDnlkkiKGDDPALILYTSGTTGKPKGVVHTHKGILSQV-QILTEAWG 290
Cdd:cd17642 151 DYKGYqclytfITQNLPPGFNEYDFKPP---SFD-----RDEQVALIMNSSGSTGLPKGVQLTHKNIVARFsHARDPIFG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 291 YQ--SEDQFLHCLPLHHVHGLFNALfAPLYSGSVVEFMPKFSVRgVWQRWRESYpsgvsKSNDAITvftgVPTVY----- 363
Cdd:cd17642 223 NQiiPDTAILTVIPFHHGFGMFTTL-GYLICGFRVVLMYKFEEE-LFLRSLQDY-----KVQSALL----VPTLFaffak 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 364 TRLLQGYDTMNpdeqsacsyaakqLRLMMCGSsalpSPLMKRWEEVTGHR-----LLERYGMTEFVMALSNPLHGPRKEG 438
Cdd:cd17642 292 STLVDKYDLSN-------------LHEIASGG----APLSKEVGEAVAKRfklpgIRQGYGLTETTSAILITPEGDDKPG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 439 TVGKPLPRVEAKIImDDGTETKAGV---GELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTN 515
Cdd:cd17642 355 AVGKVVPFFYAKVV-DLDTGKTLGPnerGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLK 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 516 AdIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKeraeqasepaLTLQALTSWSKDKLAP 595
Cdd:cd17642 434 S-LIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKT----------MTEKEVMDYVASQVST 502
|
490 500 510
....*....|....*....|....*....|...
gi 2212542879 596 YKiptRL----YLWDSLPRNAMGKVNKKELKKL 624
Cdd:cd17642 503 AK---RLrggvKFVDEVPKGLTGKIDRRKIREI 532
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
246-624 |
3.09e-39 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 155.08 E-value: 3.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 246 NLKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSG-SVVE 324
Cdd:PRK08633 775 YGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGiKVVY 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 325 FMPKFSVRGVWQRwresypsgVSKSNdaITVFTGVPT---VYTRLLQgydtMNPDE-QSacsyaakqLRLMMCGSSALPS 400
Cdd:PRK08633 855 HPDPTDALGIAKL--------VAKHR--ATILLGTPTflrLYLRNKK----LHPLMfAS--------LRLVVAGAEKLKP 912
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 401 PLMKRWEEVTGHRLLERYGMTEF--VMALSNP---------LHGpRKEGTVGKPLPRVEAKII-MDDGTETKAGV-GELC 467
Cdd:PRK08633 913 EVADAFEEKFGIRILEGYGATETspVASVNLPdvlaadfkrQTG-SKEGSVGMPLPGVAVRIVdPETFEELPPGEdGLIL 991
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 468 IRSPSLFREYWKRPEVTEESF--IDG-GFFKTGDTVTIDEDGYFKILGRTnADIMKVGGYKLSALEIEAVLLE--HDTIL 542
Cdd:PRK08633 992 IGGPQVMKGYLGDPEKTAEVIkdIDGiGWYVTGDKGHLDEDGFLTITDRY-SRFAKIGGEMVPLGAVEEELAKalGGEEV 1070
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 543 ECAVLGLPDEAYGEVICAIIVAK----EDVKERAEQASEPALtlqaltsWskdklapykIPTRLYLWDSLPRNAMGKVNK 618
Cdd:PRK08633 1071 VFAVTAVPDEKKGEKLVVLHTCGaedvEELKRAIKESGLPNL-------W---------KPSRYFKVEALPLLGSGKLDL 1134
|
....*.
gi 2212542879 619 KELKKL 624
Cdd:PRK08633 1135 KGLKEL 1140
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
137-621 |
6.24e-39 |
|
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: 149.73 E-value: 6.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 137 RGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKCSTGYSLLPSv 216
Cdd:cd12114 36 PGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTDGPDAQLDVAVFDVLILDLDALAA- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 217 ESIPPKIESQEplsseltssvssllaeidnlkkikgDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQ 296
Cdd:cd12114 115 PAPPPPVDVAP-------------------------DDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 297 FLHCLPLHH---VHGLFNALFAplySGSVVefMPKFSVRGV---WQRWRESYPsgvsksndaITVFTGVPTVYTRLLQGY 370
Cdd:cd12114 170 VLALSSLSFdlsVYDIFGALSA---GATLV--LPDEARRRDpahWAELIERHG---------VTLWNSVPALLEMLLDVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 371 DTMNPDEQSacsyaakqLRLMMCGSSALPSPLMKRWEEVTGH-RLLERYGMTEfVMALSN--PLHGPRKEGTV---GKPL 444
Cdd:cd12114 236 EAAQALLPS--------LRLVLLSGDWIPLDLPARLRALAPDaRLISLGGATE-ASIWSIyhPIDEVPPDWRSipyGRPL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 445 PRVEAKIIMDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFID----GGFFKTGDTVTIDEDGYFKILGRTNADIm 519
Cdd:cd12114 307 ANQRYRVLDPRGRDCPDWVpGELWIGGRGVALGYLGDPELTAARFVThpdgERLYRTGDLGRYRPDGTLEFLGRRDGQV- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 520 KVGGYKLSALEIEAVLLEHDTILECAVLGLpDEAYGEVICAIIVAKEDVkeraEQASEPALTLQAltswsKDKLAPYKIP 599
Cdd:cd12114 386 KVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDG----TPIAPDALRAFL-----AQTLPAYMIP 455
|
490 500
....*....|....*....|..
gi 2212542879 600 TRLYLWDSLPRNAMGKVNKKEL 621
Cdd:cd12114 456 SRVIALEALPLTANGKVDRAAL 477
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
249-626 |
8.94e-39 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 150.13 E-value: 8.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 249 KIKGDDPALILYTSGTTGKPKGVVHTHKGILSQV--QILTEA--WGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVE 324
Cdd:PLN02246 175 EISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVaqQVDGENpnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAIL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 325 FMPKF---SVRGVWQRWResypsgvsksndaITVFTGVPTVYTRLLQGYDTMNPDEQSacsyaakqLRLMMCGSsalpSP 401
Cdd:PLN02246 255 IMPKFeigALLELIQRHK-------------VTIAPFVPPIVLAIAKSPVVEKYDLSS--------IRMVLSGA----AP 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 402 LMKRWEEVTGHR-----LLERYGMTEF--VMALS-----NPLhgPRKEGTVGKPLPRVEAKIImddGTETKAGV-----G 464
Cdd:PLN02246 310 LGKELEDAFRAKlpnavLGQGYGMTEAgpVLAMClafakEPF--PVKSGSCGTVVRNAELKIV---DPETGASLprnqpG 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 465 ELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILEC 544
Cdd:PLN02246 385 EICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLK-ELIKYKGFQVAPAELEALLISHPSIADA 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 545 AVLGLPDEAYGEVICAIIVAKEDVKeraeqasepaLTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKL 624
Cdd:PLN02246 464 AVVPMKDEVAGEVPVAFVVRSNGSE----------ITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
..
gi 2212542879 625 LQ 626
Cdd:PLN02246 534 LA 535
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
132-623 |
9.67e-39 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 154.16 E-value: 9.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 132 GTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEhheimesistkcstGYS 211
Cdd:PRK12467 556 AAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSH--------------LLA 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 212 LLP---SVESIPpkIESQEPLSSELTSSVSSLLAEIDNLkkikgddpALILYTSGTTGKPKGVVHTHKGILSQVQILTEA 288
Cdd:PRK12467 622 QLPvpaGLRSLC--LDEPADLLCGYSGHNPEVALDPDNL--------AYVIYTSGSTGQPKGVAISHGALANYVCVIAER 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 289 WGYQSEDQFLHCLPLhHVHGLFNALFAPLYSGSVVEFMPKFSVRGVWQRWRESYPSGVsksndaiTVFTGVPTVYTRLLq 368
Cdd:PRK12467 692 LQLAADDSMLMVSTF-AFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGV-------TVLKIVPSHLQALL- 762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 369 gydtmnpdeQSACSYAAKQLRLMMCGSSALPSPLMKRWEEVT-GHRLLERYGMTE-FVMALSNPLHG-PRKEGTV--GKP 443
Cdd:PRK12467 763 ---------QASRVALPRPQRALVCGGEALQVDLLARVRALGpGARLINHYGPTEtTVGVSTYELSDeERDFGNVpiGQP 833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 444 LPRVEAKIIMDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFI------DGG-FFKTGDTVTIDEDGYFKILGRTN 515
Cdd:PRK12467 834 LANLGLYILDHYLNPVPVGVvGELYIGGAGLARGYHRRPALTAERFVpdpfgaDGGrLYRTGDLARYRADGVIEYLGRMD 913
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 516 aDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYgevicAIIVAKEdVKERAEQASEPALTLQALTSWSKDKLAP 595
Cdd:PRK12467 914 -HQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAG-----LQLVAYL-VPAAVADGAEHQATRDELKAQLRQVLPD 986
|
490 500
....*....|....*....|....*...
gi 2212542879 596 YKIPTRLYLWDSLPRNAMGKVNKKELKK 623
Cdd:PRK12467 987 YMVPAHLLLLDSLPLTPNGKLDRKALPK 1014
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
134-621 |
1.38e-38 |
|
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: 147.85 E-value: 1.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTkehheimesistkcstgysll 213
Cdd:cd12115 45 GVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLTD--------------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 214 psvesippkiesqeplsseltssvssllaeidnlkkikGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQS 293
Cdd:cd12115 104 --------------------------------------PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 294 EDQFLHCLPLHHVHGLFNaLFAPLYSGSVVefmpkFSVRGVWQRWRESYPSGVSKSNDaitvftgVPTVYTRLLqgydtm 373
Cdd:cd12115 146 LAGVLASTSICFDLSVFE-LFGPLATGGKV-----VLADNVLALPDLPAAAEVTLINT-------VPSAAAELL------ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 374 npdEQSACSYAAKQLRLmmcGSSALPSPLMKR-WEEVTGHRLLERYGMTE---FVMALSNPLHGPRkEGTVGKPLPRVEA 449
Cdd:cd12115 207 ---RHDALPASVRVVNL---AGEPLPRDLVQRlYARLQVERVVNLYGPSEdttYSTVAPVPPGASG-EVSIGRPLANTQA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 450 KIIMDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGF------FKTGDTVTIDEDGYFKILGRTNaDIMKVG 522
Cdd:cd12115 280 YVLDRALQPVPLGVpGELYIGGAGVARGYLGRPGLTAERFLPDPFgpgarlYRTGDLVRWRPDGLLEFLGRAD-NQVKVR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 523 GYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKedvkeraeqaSEPALTLQALTSWSKDKLAPYKIPTRL 602
Cdd:cd12115 359 GFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAE----------PGAAGLVEDLRRHLGTRLPAYMVPSRF 428
|
490
....*....|....*....
gi 2212542879 603 YLWDSLPRNAMGKVNKKEL 621
Cdd:cd12115 429 VRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
141-621 |
4.34e-38 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 147.20 E-value: 4.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 141 IGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEhheimesistkcstgysllpsvesip 220
Cdd:cd17644 53 VGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVLLTQPE-------------------------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 221 pkiesqeplsseltssvssllaeidNLkkikgddpALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHC 300
Cdd:cd17644 107 -------------------------NL--------AYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 301 LPLHhvhglFNA----LFAPLYSGSVVEFMPkfsvrgvwQRWRESYPSGVSKSND-AITVFTgVPTVYTRLLqgydtMNP 375
Cdd:cd17644 154 ASIA-----FDVaaeeIYVTLLSGATLVLRP--------EEMRSSLEDFVQYIQQwQLTVLS-LPPAYWHLL-----VLE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 376 DEQSACSYAAKqLRLMMCGSSALPSPLMKRWEEVTGH--RLLERYGMTEFVMA-----LSNPLHGPRKEGTVGKPLPRVE 448
Cdd:cd17644 215 LLLSTIDLPSS-LRLVIVGGEAVQPELVRQWQKNVGNfiQLINVYGPTEATIAatvcrLTQLTERNITSVPIGRPIANTQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 449 AKIIMDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGF--------FKTGDTVTIDEDGYFKILGRTNADIm 519
Cdd:cd17644 294 VYILDENLQPVPVGVpGELHIGGVGLARGYLNRPELTAEKFISHPFnsseserlYKTGDLARYLPDGNIEYLGRIDNQV- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 520 KVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKedvkeraeqaSEPALTLQALTSWSKDKLAPYKIP 599
Cdd:cd17644 373 KIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPH----------YEESPSTVELRQFLKAKLPDYMIP 442
|
490 500
....*....|....*....|..
gi 2212542879 600 TRLYLWDSLPRNAMGKVNKKEL 621
Cdd:cd17644 443 SAFVVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
134-621 |
1.36e-37 |
|
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: 145.09 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTkehheimesistkcstgysll 213
Cdd:cd17652 33 GVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLTT--------------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 214 psvesippkiesqeplsseltssvssllaeidnlkkikGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQS 293
Cdd:cd17652 92 --------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 294 EDQFLHCLPLHhvhglFNA----LFAPLYSGS--VV----EFMPKFSVRGVWQRWResypsgvsksndaITVFTGVPTVY 363
Cdd:cd17652 134 GSRVLQFASPS-----FDAsvweLLMALLAGAtlVLapaeELLPGEPLADLLREHR-------------ITHVTLPPAAL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 364 trllqgyDTMNPDEQSAcsyaakqLRLMMCGSSALPSPLMKRWeeVTGHRLLERYGMTEF-VMALSNPLHGPRKEGTVGK 442
Cdd:cd17652 196 -------AALPPDDLPD-------LRTLVVAGEACPAELVDRW--APGRRMINAYGPTETtVCATMAGPLPGGGVPPIGR 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 443 PLPRVEAKIiMDDGTE-TKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGF-------FKTGDTVTIDEDGYFKILGR 513
Cdd:cd17652 260 PVPGTRVYV-LDARLRpVPPGVpGELYIAGAGLARGYLNRPGLTAERFVADPFgapgsrmYRTGDLARWRADGQLEFLGR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 514 TNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAkedvkeraeqASEPALTLQALTSWSKDKL 593
Cdd:cd17652 339 AD-DQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVP----------APGAAPTAAELRAHLAERL 407
|
490 500
....*....|....*....|....*...
gi 2212542879 594 APYKIPTRLYLWDSLPRNAMGKVNKKEL 621
Cdd:cd17652 408 PGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
134-603 |
3.00e-37 |
|
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: 144.81 E-value: 3.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLstkehheimesistkcstgysll 213
Cdd:cd17640 26 GVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV----------------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 214 psvesippkiesqeplsseltssvssllaeIDNlkkiKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQS 293
Cdd:cd17640 83 ------------------------------VEN----DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 294 EDQFLHCLPLHHVhglfnalfaplYSGSVVEFmpkFSVRGVWQrwreSYPSGVSKSNDAI----TVFTGVPTVYTRLLQG 369
Cdd:cd17640 129 GDRFLSILPIWHS-----------YERSAEYF---IFACGCSQ----AYTSIRTLKDDLKrvkpHYIVSVPRLWESLYSG 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 370 YDtmnpDEQSACSYAAKQL----------RLMMCGSSALPsPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHGPRKEGT 439
Cdd:cd17640 191 IQ----KQVSKSSPIKQFLflfflsggifKFGISGGGALP-PHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGS 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 440 VGKPLPRVEAKIIMDDGTE--TKAGVGELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNAD 517
Cdd:cd17640 266 VGRPLPGTEIKIVDPEGNVvlPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDT 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 518 IMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGevicAIIVAKEDVKERAEQASEPALtLQALTSWSKDklapyK 597
Cdd:cd17640 346 IVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQKRLG----ALIVPNFEELEKWAKESGVKL-ANDRSQLLAS-----K 415
|
....*.
gi 2212542879 598 IPTRLY 603
Cdd:cd17640 416 KVLKLY 421
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
251-626 |
5.21e-37 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 148.19 E-value: 5.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 251 KGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPK-F 329
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYPSpL 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 330 SVRGVwqrwresyPSGVSKSNdaITVFTGVPTvytrLLQGYdtmnpdEQSACSYAAKQLRLMMCGSSALPSPLMKRWEEV 409
Cdd:PRK06814 871 HYRII--------PELIYDTN--ATILFGTDT----FLNGY------ARYAHPYDFRSLRYVFAGAEKVKEETRQTWMEK 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 410 TGHRLLERYGMTEF--VMALSNPLHGprKEGTVGKPLPRVEAKIimddgtETKAGV---GELCIRSPSLFREYWK--RPE 482
Cdd:PRK06814 931 FGIRILEGYGVTETapVIALNTPMHN--KAGTVGRLLPGIEYRL------EPVPGIdegGRLFVRGPNVMLGYLRaeNPG 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 483 VTEEsfIDGGFFKTGDTVTIDEDGYFKILGRTNAdIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVIcaII 562
Cdd:PRK06814 1003 VLEP--PADGWYDTGDIVTIDEEGFITIKGRAKR-FAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGERI--IL 1077
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2212542879 563 VAKEDVKERAeqasepaltlqALTSWSKDKLAP-YKIPTRLYLWDSLPRNAMGKVNKKELKKLLQ 626
Cdd:PRK06814 1078 LTTASDATRA-----------AFLAHAKAAGASeLMVPAEIITIDEIPLLGTGKIDYVAVTKLAE 1131
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
250-624 |
7.13e-37 |
|
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: 145.92 E-value: 7.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 250 IKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQI-LTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSG--SVV-EF 325
Cdd:cd05967 227 VAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWsMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLLHGatTVLyEG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 326 MPkfsVR----GVWQRWRESYpsGVSksndaiTVFTgVPTVYtRLLQGYDtmnPDEQSACSYAAKQLRLMMCGSSALPSP 401
Cdd:cd05967 307 KP---VGtpdpGAFWRVIEKY--QVN------ALFT-APTAI-RAIRKED---PDGKYIKKYDLSSLRTLFLAGERLDPP 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 402 LMKRWEEVTGHRLLERYGMTEFVMALSNPLHG----PRKEGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIR---SPSL 473
Cdd:cd05967 371 TLEWAENTLGVPVIDHWWQTETGWPITANPVGleplPIKAGSPGKPVPGYQVQVLDEDGEPVGPNeLGNIVIKlplPPGC 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 474 FREYWKRPEVTEESFI--DGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPD 551
Cdd:cd05967 451 LLTLWKNDERFKKLYLskFPGYYDTGDAGYKDEDGYLFIMGRTD-DVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRD 529
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2212542879 552 EAYGEVICAIIVAKEDVKERAEQASepaltlQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKL 624
Cdd:cd05967 530 ELKGQVPLGLVVLKEGVKITAEELE------KELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKI 596
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
255-622 |
1.90e-36 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 142.92 E-value: 1.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 255 PALILYTSGTTGKPKGVVH---THKGILSQVQILTEAWGYQSEDQFLHCLPLHH----VHGLFNALFaplysGSVVEFMP 327
Cdd:PRK12406 154 PQSMIYTSGTTGHPKGVRRaapTPEQAAAAEQMRALIYGLKPGIRALLTGPLYHsapnAYGLRAGRL-----GGVLVLQP 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 328 KFSVRGVWQ---RWResypsgvsksndaITVFTGVPTVYTRLLQgydtmNPDEQSAcSYAAKQLRLMMCGSSALPSPLMK 404
Cdd:PRK12406 229 RFDPEELLQlieRHR-------------ITHMHMVPTMFIRLLK-----LPEEVRA-KYDVSSLRHVIHAAAPCPADVKR 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 405 RWEEVTGHRLLERYGMTEF-VMALSNPLHGPRKEGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIRSP--SLFrEYWKR 480
Cdd:PRK12406 290 AMIEWWGPVIYEYYGSTESgAVTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGeIGEIYSRIAgnPDF-TYHNK 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 481 PEvtEESFID-GGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVIC 559
Cdd:PRK12406 369 PE--KRAEIDrGGFITSGDVGYLDADGYLFLCDRKR-DMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALM 445
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2212542879 560 AIIvakedvkeraEQASEPALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:PRK12406 446 AVV----------EPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
257-622 |
3.03e-36 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 142.98 E-value: 3.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 257 LILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVV---EFMPKFSVRG 333
Cdd:PRK13382 200 VILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQLVLAASLACTIVtrrRFDPEATLDL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 334 VwQRWResyPSGVSKsndaitvftgVPTVYTRLLQGydtmnPDEQSAcSYAAKQLRLMMCGSSALPSPLMKRWEEVTGHR 413
Cdd:PRK13382 280 I-DRHR---ATGLAV----------VPVMFDRIMDL-----PAEVRN-RYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 414 LLERYGMTEFVM-ALSNPLHGPRKEGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYwkRPEVTEEsFIDG 491
Cdd:PRK13382 340 IYNNYNATEAGMiATATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGeVGTIFVRNDTQFDGY--TSGSTKD-FHDG 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 492 gFFKTGDTVTIDEDGYFKILGRTnaDIMKV-GGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVke 570
Cdd:PRK13382 417 -FMASGDVGYLDENGRLFVVGRD--DEMIVsGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGA-- 491
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2212542879 571 raeqasepALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:PRK13382 492 --------SATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
253-616 |
5.13e-36 |
|
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: 143.10 E-value: 5.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKG-ILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVeFMpkFSV 331
Cdd:cd17634 232 EDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATT-LL--YEG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 332 RGVW----QRWRESYPSGVSKSNDAITVFTGVPTVYTRLLQGYDTmnpdeqsacsyaaKQLR-LMMCGSSALPSPLMKRW 406
Cdd:cd17634 309 VPNWptpaRMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDR-------------SSLRiLGSVGEPINPEAYEWYW 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 407 EEVTGHR--LLERYGMTEFVMALSNPLHG--PRKEGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIRS--PSLFREYWK 479
Cdd:cd17634 376 KKIGKEKcpVVDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVVDNEGHPQPGGtEGNLVITDpwPGQTRTLFG 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 480 RPEVTEESFID--GGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEV 557
Cdd:cd17634 456 DHERFEQTYFStfKGMYFSGDGARRDEDGYYWITGRSD-DVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQA 534
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2212542879 558 ICAIIVAKEDVKERAEQASEpaltlqaLTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKV 616
Cdd:cd17634 535 PYAYVVLNHGVEPSPELYAE-------LRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
138-623 |
9.87e-36 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 144.71 E-value: 9.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 138 GARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLsTKEHheIMESIStkCSTGYSLLPsve 217
Cdd:PRK12316 2053 EVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLL-TQRH--LLERLP--LPAGVARLP--- 2124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 218 sIPPKIESQEplsseltssvsslLAEIDNLKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQF 297
Cdd:PRK12316 2125 -LDRDAEWAD-------------YPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCE 2190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 298 LHCLPLhHVHGLFNALFAPLYSGSVVeFMPKFSVRGVWQRWRESYPSGVSksndaITVFtgvPTVYTRLLQgydtmnpdE 377
Cdd:PRK12316 2191 LQFMSF-SFDGAHEQWFHPLLNGARV-LIRDDELWDPEQLYDEMERHGVT-----ILDF---PPVYLQQLA--------E 2252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 378 QSACSYAAKQLRLMMCGSSALPSPLMKR-WEEVTGHRLLERYGMTEFVMalsNPLH---GPRK-EGTVGKPLPRV---EA 449
Cdd:PRK12316 2253 HAERDGRPPAVRVYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTEAVV---TPLLwkcRPQDpCGAAYVPIGRAlgnRR 2329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 450 KIIMDDGTETKA--GVGELCIRSPSLFREYWKRPEVTEESFIDGGF-------FKTGDTVTIDEDGYFKILGRTNADImK 520
Cdd:PRK12316 2330 AYILDADLNLLApgMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRADGVVEYLGRIDHQV-K 2408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 521 VGGYKLSALEIEAVLLEHDTILECAVLGLpDEAYGEVICAIIVAkEDVKEraeqasepaLTLQALTSWSKDKLAPYKIPT 600
Cdd:PRK12316 2409 IRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVP-DDAAE---------DLLAELRAWLAARLPAYMVPA 2477
|
490 500
....*....|....*....|...
gi 2212542879 601 RLYLWDSLPRNAMGKVNKKELKK 623
Cdd:PRK12316 2478 HWVVLERLPLNPNGKLDRKALPK 2500
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
140-624 |
2.18e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 143.94 E-value: 2.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 140 RIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLStkeHHEIMESistkcstgyslLPSVESI 219
Cdd:PRK12316 4603 LVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLT---QSHLLQR-----------LPIPDGL 4668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 220 PPKIESQEplsseltsSVSSLLAEIDNLKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLH 299
Cdd:PRK12316 4669 ASLALDRD--------EDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQ 4740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 300 CLPLhHVHGLFNALFAPLYSGSVVeFMPKFSVRGVWQRWRESYPSGVSksndaITVFTgvPTVYTRLLQGydtmnPDEQS 379
Cdd:PRK12316 4741 FMSF-SFDGSHEGLYHPLINGASV-VIRDDSLWDPERLYAEIHEHRVT-----VLVFP--PVYLQQLAEH-----AERDG 4806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 380 ACSyaakQLRLMMCGSSALPSPLMKR-WEEVTGHRLLERYGMTEFVMalsNPLHGPRKEGT--------VGKPLPRVEAK 450
Cdd:PRK12316 4807 EPP----SLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTV---TVLLWKARDGDacgaaympIGTPLGNRSGY 4879
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 451 IIMDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGF-------FKTGDTVTIDEDGYFKILGRTNADImKVG 522
Cdd:PRK12316 4880 VLDGQLNPLPVGVaGELYLGGEGVARGYLERPALTAERFVPDPFgapggrlYRTGDLARYRADGVIDYLGRVDHQV-KIR 4958
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 523 GYKLSALEIEAVLLEHDTILECAVLGLPDeAYGEVICAIIVAKEdvKERAEQASEPALTLQALTSWSKDKLAPYKIPTRL 602
Cdd:PRK12316 4959 GFRIELGEIEARLREHPAVREAVVIAQEG-AVGKQLVGYVVPQD--PALADADEAQAELRDELKAALRERLPEYMVPAHL 5035
|
490 500
....*....|....*....|..
gi 2212542879 603 YLWDSLPRNAMGKVNKKELKKL 624
Cdd:PRK12316 5036 VFLARMPLTPNGKLDRKALPQP 5057
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
140-621 |
3.57e-35 |
|
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: 138.07 E-value: 3.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 140 RIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLStkehheimesistkcstgysllpsvesi 219
Cdd:cd17645 50 QVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLT---------------------------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 220 ppkiesqeplsseltssvssllaeidnlkkiKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQflh 299
Cdd:cd17645 102 -------------------------------NPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADK--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 300 clplhhvhglfNALFAPL-YSGSVVEFMPKFSVRGVWQRWRESYPSGVSKSND-----AITVfTGVPTVYTRLLqgydtM 373
Cdd:cd17645 148 -----------SLVYASFsFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDyfnqeGITI-SFLPTGAAEQF-----M 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 374 NPDEQSacsyaakqLRLMMCGSSALpsplmKRWEEvTGHRLLERYGMTE-FVMALSNPLHGPRKEGTVGKPLPRVEAKII 452
Cdd:cd17645 211 QLDNQS--------LRVLLTGGDKL-----KKIER-KGYKLVNNYGPTEnTVVATSFEIDKPYANIPIGKPIDNTRVYIL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 453 MDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGF------FKTGDTVTIDEDGYFKILGRTNaDIMKVGGYK 525
Cdd:cd17645 277 DEALQLQPIGVaGELCIAGEGLARGYLNRPELTAEKFIVHPFvpgermYRTGDLAKFLPDGNIEFLGRLD-QQVKIRGYR 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 526 LSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKeraeqasepaltLQALTSWSKDKLAPYKIPTRLYLW 605
Cdd:cd17645 356 IEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIP------------HEELREWLKNDLPDYMIPTYFVHL 423
|
490
....*....|....*.
gi 2212542879 606 DSLPRNAMGKVNKKEL 621
Cdd:cd17645 424 KALPLTANGKVDRKAL 439
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
138-621 |
4.08e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 142.79 E-value: 4.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 138 GARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLStkEHHeIMESISTKCST-------GY 210
Cdd:PRK12316 561 DVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLS--QSH-LGRKLPLAAGVqvldldrPA 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 211 SLLPSVESIPPKIEsqeplsseltssvssllaeidnlkkIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWG 290
Cdd:PRK12316 638 AWLEGYSEENPGTE-------------------------LNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYG 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 291 YQSEDQFLHCLPLHhvhglFNA----LFAPLYSGSVVEFMPKFSVRGVWQRWRESypsgvskSNDAITVFTGVPTVYTRL 366
Cdd:PRK12316 693 LGVGDTVLQKTPFS-----FDVsvweFFWPLMSGARLVVAAPGDHRDPAKLVELI-------NREGVDTLHFVPSMLQAF 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 367 LQgydtmNPDEQSACSyaakqLRLMMCGSSALPSPLM-----KRWEEvtghRLLERYGMTEFVMALSNplHGPRKEG--- 438
Cdd:PRK12316 761 LQ-----DEDVASCTS-----LRRIVCSGEALPADAQeqvfaKLPQA----GLYNLYGPTEAAIDVTH--WTCVEEGgds 824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 439 -TVGKPLPRVEAKIIMDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGF------FKTGDTVTIDEDGYFKI 510
Cdd:PRK12316 825 vPIGRPIANLACYILDANLEPVPVGVlGELYLAGRGLARGYHGRPGLTAERFVPSPFvagermYRTGDLARYRADGVIEY 904
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 511 LGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPdeayGEVICAIIVAKedvkeraeqaSEPALTLQALTSWSK 590
Cdd:PRK12316 905 AGRID-HQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLE----------SEGGDWREALKAHLA 969
|
490 500 510
....*....|....*....|....*....|.
gi 2212542879 591 DKLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 621
Cdd:PRK12316 970 ASLPEYMVPAQWLALERLPLTPNGKLDRKAL 1000
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
260-623 |
7.35e-35 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 139.12 E-value: 7.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 260 YTSGTTGKPKGVVHTHKG--ILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVefMPKFSVRG--VW 335
Cdd:PRK06018 184 YTSGTTGDPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLV--MPGAKLDGasVY 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 336 QRWresypsgvskSNDAITVFTGVPTVYTRLLQGYDTMN---PDeqsacsyaakqLRLMMCGSSALPSPLMKRWEEVtGH 412
Cdd:PRK06018 262 ELL----------DTEKVTFTAGVPTVWLMLLQYMEKEGlklPH-----------LKMVVCGGSAMPRSMIKAFEDM-GV 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 413 RLLERYGMTEF-----VMALSNPLHGPRKEG------TVGKPLPRVEAKIIMDDGTET----KAgVGELCIRSPSLFREY 477
Cdd:PRK06018 320 EVRHAWGMTEMsplgtLAALKPPFSKLPGDArldvlqKQGYPPFGVEMKITDDAGKELpwdgKT-FGRLKVRGPAVAAAY 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 478 WKrpeVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEV 557
Cdd:PRK06018 399 YR---VDGEILDDDGFFDTGDVATIDAYGYMRITDRSK-DVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDER 474
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2212542879 558 ICAIIVAKEDVkeraeqasepALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKK 623
Cdd:PRK06018 475 PLLIVQLKPGE----------TATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
131-625 |
8.07e-35 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 139.15 E-value: 8.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 131 DGTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKCstgy 210
Cdd:PRK05620 57 DELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQLGEILKEC---- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 211 sllPSVES---IPPKIESQEPLSSELTSSVSSLLAEID------NLKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQ 281
Cdd:PRK05620 133 ---PCVRAvvfIGPSDADSAAAHMPEGIKVYSYEALLDgrstvyDWPELDETTAAAICYSTGTTGAPKGVVYSHRSLYLQ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 282 VQIL--TEAWGYQSEDQFLHCLPLHHVHGlFNALFAPLYSGSVVeFMPKFSVrgvwqrwreSYPSGVSKSNDAIT-VFTG 358
Cdd:PRK05620 210 SLSLrtTDSLAVTHGESFLCCVPIYHVLS-WGVPLAAFMSGTPL-VFPGPDL---------SAPTLAKIIATAMPrVAHG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 359 VPTVYTRLLQGYDTMNPDEQSacsyaakqLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEfvmalSNPLhgprkeG 438
Cdd:PRK05620 279 VPTLWIQLMVHYLKNPPERMS--------LQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTE-----TSPV------G 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 439 TVGKPLPRV--EAKI----------------IMDDG---TETKAGVGELCIRSPSLFREYWKRPEVTE------------ 485
Cdd:PRK05620 340 TVARPPSGVsgEARWayrvsqgrfpasleyrIVNDGqvmESTDRNEGEIQVRGNWVTASYYHSPTEEGggaastfrgedv 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 486 ----ESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAI 561
Cdd:PRK05620 420 edanDRFTADGWLRTGDVGSVTRDGFLTIHDRAR-DVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAV 498
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2212542879 562 IVAKEDVKERAEQASEpaltlqaLTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLL 625
Cdd:PRK05620 499 TVLAPGIEPTRETAER-------LRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQHL 555
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
257-624 |
1.14e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 138.52 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 257 LILYTSGTTGKPKGVVHTHKGILSQV-QILTEAwGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVV---EFMPKFSVR 332
Cdd:PRK07788 211 IVILTSGTTGTPKGAPRPEPSPLAPLaGLLSRV-PFRAGETTLLPAPMFHATGWAHLTLAMALGSTVVlrrRFDPEATLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 333 GVwQRWREsypsgvsksnDAITVftgVPTVYTRLL-------QGYDTmnpdeqSAcsyaakqLRLMMCGSSALPSPLMKR 405
Cdd:PRK07788 290 DI-AKHKA----------TALVV---VPVMLSRILdlgpevlAKYDT------SS-------LKIIFVSGSALSPELATR 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 406 WEEVTGHRLLERYGMTEF-VMALSNPLHGPRKEGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYW--KRP 481
Cdd:PRK07788 343 ALEAFGPVLYNLYGSTEVaFATIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGvVGRIFVGNGFPFEGYTdgRDK 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 482 EvteesfIDGGFFKTGDTVTIDEDGYFKILGRtnADIMKV-GGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICA 560
Cdd:PRK07788 423 Q------IIDGLLSSGDVGYFDEDGLLFVDGR--DDDMIVsGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRA 494
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2212542879 561 IIVAKEDVkeraeqasepALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKL 624
Cdd:PRK07788 495 FVVKAPGA----------ALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
140-621 |
2.15e-34 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 140.69 E-value: 2.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 140 RIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPeVELLHVM-NDSDISMVLStkeHHEIMESISTkcstgyslLP---- 214
Cdd:PRK05691 2240 RVGLALERSLEMVVGLLAILKAGGAYVPLDPEYP-LERLHYMiEDSGIGLLLS---DRALFEALGE--------LPagva 2307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 215 --SVESIPPKIESQEPlsseltssvssllAEIDNLKKikGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQ 292
Cdd:PRK05691 2308 rwCLEDDAAALAAYSD-------------APLPFLSL--PQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMR 2372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 293 SEDQFLHCLPLHhvhglFNA----LFAPLYSGSVVefmpkfSVRGVWQRWRESYPSGVSKSNDAITVFTgvPTVYTRLLQ 368
Cdd:PRK05691 2373 ADDCELHFYSIN-----FDAaserLLVPLLCGARV------VLRAQGQWGAEEICQLIREQQVSILGFT--PSYGSQLAQ 2439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 369 gydtmnpdeqsacsYAAKQ-----LRLMMCGSSALPSPLMKRWEEVTGHRLL-ERYGMTE-FVMALSNPLHGPRKEGTVG 441
Cdd:PRK05691 2440 --------------WLAGQgeqlpVRMCITGGEALTGEHLQRIRQAFAPQLFfNAYGPTEtVVMPLACLAPEQLEEGAAS 2505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 442 KPLPRV----EAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFI------DGG-FFKTGDTVTIDEDGYFK 509
Cdd:PRK05691 2506 VPIGRVvgarVAYILDADLALVPQGaTGELYVGGAGLAQGYHDRPGLTAERFVadpfaaDGGrLYRTGDLVRLRADGLVE 2585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 510 ILGRTNADImKVGGYKLSALEIEAVLLEHDTILECAVLGLpDEAYGEVICAIIVAKEdvkerAEQASEPALTL-QALTSW 588
Cdd:PRK05691 2586 YVGRIDHQV-KIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLVSAV-----AGQDDEAQAALrEALKAH 2658
|
490 500 510
....*....|....*....|....*....|...
gi 2212542879 589 SKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 621
Cdd:PRK05691 2659 LKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
134-621 |
2.88e-34 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 136.45 E-value: 2.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLsTKEHHEIMESISTkcstgysll 213
Cdd:cd17656 34 GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVL-TQRHLKSKLSFNK--------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 214 pSVESIPPKIESQEplsseltssvssllaEIDNLKKI-KGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQ 292
Cdd:cd17656 104 -STILLEDPSISQE---------------DTSNIDYInNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNIN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 293 SED---QFLHClplhHVHGLFNALFAPLYSGSVVEFMPKFSVRGVWQRWresypsGVSKSNDAITVFtgVPTVYTRLLQG 369
Cdd:cd17656 168 FSDkvlQFATC----SFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLF------DLVKRHNIEVVF--LPVAFLKFIFS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 370 ydtmnpDEQSACSYAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTE---FVMALSNPLHGPRKEGTVGKPLPR 446
Cdd:cd17656 236 ------EREFINRFPTCVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSEthvVTTYTINPEAEIPELPPIGKPISN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 447 VEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFIDGGF------FKTGDTVTIDEDGYFKILGRTNaDIM 519
Cdd:cd17656 310 TWIYILDQEQQLQPQGiVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRAD-HQV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 520 KVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVakedvkeraeqaSEPALTLQALTSWSKDKLAPYKIP 599
Cdd:cd17656 389 KIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV------------MEQELNISQLREYLAKQLPEYMIP 456
|
490 500
....*....|....*....|..
gi 2212542879 600 TRLYLWDSLPRNAMGKVNKKEL 621
Cdd:cd17656 457 SFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
254-627 |
3.12e-34 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 135.51 E-value: 3.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 254 DPALILY-TSGTTGKPKGVVHTHKGILSQVQILTEawgYQSEDQfLHC---LPLHHVHGLFNALFAPLYSGsvvefmpKF 329
Cdd:PRK07445 120 ETGWIMIpTGGSSGQIRFAIHTWETLTASVQGFQR---YFQLQQ-VNSfcvLPLYHVSGLMQFMRSFLTGG-------KL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 330 SVrgvwQRWRESYPSGVSKSNDAITVFTGVPTVYTRLLQGydtmnpdeqsaCSYAAKQLRLMMCGSS-ALPSPLmkrwEE 408
Cdd:PRK07445 189 VI----LPYKRLKSGQELPPNPSDFFLSLVPTQLQRLLQL-----------RPQWLAQFRTILLGGApAWPSLL----EQ 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 409 VTGH--RLLERYGMTE---FVMALSnP---LHGPRkegTVGKPLPrvEAKIIMDDGTetkagVGELCIRSPSLFREYWkr 480
Cdd:PRK07445 250 ARQLqlRLAPTYGMTEtasQIATLK-PddfLAGNN---SSGQVLP--HAQITIPANQ-----TGNITIQAQSLALGYY-- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 481 PEVTEESfidgGFFKTGDTVTIDEDGYFKILGRTNADIMKvGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICA 560
Cdd:PRK07445 317 PQILDSQ----GIFETDDLGYLDAQGYLHILGRNSQKIIT-GGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTA 391
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2212542879 561 IIVAKEdvkeraeqasePALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLLQV 627
Cdd:PRK07445 392 IYVPKD-----------PSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQ 447
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
254-617 |
6.14e-34 |
|
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: 132.04 E-value: 6.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 254 DPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVeFMPKFSVRG 333
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHIGTLMFTLATFHAGGTNV-FVRRVDAEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 334 VwqrwresypSGVSKSNDAITVFTGVPTVyTRLLQGYDTMNPDEQSACSYAAKQLRLMMcgSSALPSPLMKRweevtghr 413
Cdd:cd17636 80 V---------LELIEAERCTHAFLLPPTI-DQIVELNADGLYDLSSLRSSPAAPEWNDM--ATVDTSPWGRK-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 414 lLERYGMTEfVMALSNPLH-GPRKEGTVGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFIDG 491
Cdd:cd17636 140 -PGGYGQTE-VMGLATFAAlGGGAIGGAGRPSPLVQVRILDEDGREVPDGeVGEIVARGPTVMAGYWNRPEVNARRTRGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 492 GFfKTGDTVTIDEDGYFKILGrTNADIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVker 571
Cdd:cd17636 218 WH-HTNDLGRREPDGSLSFVG-PKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGA--- 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2212542879 572 aeqasepALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVN 617
Cdd:cd17636 293 -------SVTEAELIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
260-623 |
6.31e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 136.23 E-value: 6.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 260 YTSGTTGKPKGVVHTHKG--ILSQVQILteAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVeFMPKFSVRGVWQR 337
Cdd:PRK08162 189 YTSGTTGNPKGVVYHHRGayLNALSNIL--AWGMPKHPVYLWTLPMFHCNGWCFPWTVAARAGTNV-CLRKVDPKLIFDL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 338 WREsypsgvsksnDAITVFTGVPTVYTRLLQGydtmnPDEQSACsyAAKQLRLMMCGsSALPSPLMKRWEEVtGHRLLER 417
Cdd:PRK08162 266 IRE----------HGVTHYCGAPIVLSALINA-----PAEWRAG--IDHPVHAMVAG-AAPPAAVIAKMEEI-GFDLTHV 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 418 YGMTEfvmalsnpLHGP-------------------RKEGTVGKPLPRVEAKIIMD---------DGtETkagVGELCIR 469
Cdd:PRK08162 327 YGLTE--------TYGPatvcawqpewdalplderaQLKARQGVRYPLQEGVTVLDpdtmqpvpaDG-ET---IGEIMFR 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 470 SPSLFREYWKRPEVTEESFiDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGL 549
Cdd:PRK08162 395 GNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSK-DIIISGGENISSIEVEDVLYRHPAVLVAAVVAK 472
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2212542879 550 PDEAYGEVICAIIVAKEDVkeraeQASEpaltlQALTSWSKDKLAPYKIPTRLYLwDSLPRNAMGKVNKKELKK 623
Cdd:PRK08162 473 PDPKWGEVPCAFVELKDGA-----SATE-----EEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLRE 535
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
255-622 |
6.62e-34 |
|
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: 135.20 E-value: 6.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 255 PALILYTSGTTGKPKGVVHTHKGILSQVQILTEA---WGYQSEDQFLHCLPLHHVHGL---FNALFAplysGSVVEFMPK 328
Cdd:cd05929 127 GWKMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAalgFGPGADSVYLSPAPLYHAAPFrwsMTALFM----GGTLVLMEK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 329 FS----VRGVwQRWResypsgvsksndaITVFTGVPTVYTRLLQgydtmNPDEQSAcSYAAKQLRLMMCGSSALPSPLMK 404
Cdd:cd05929 203 FDpeefLRLI-ERYR-------------VTFAQFVPTMFVRLLK-----LPEAVRN-AYDLSSLKRVIHAAAPCPPWVKE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 405 RWEEVTGHRLLERYGMTEFV-MALSNPLHGPRKEGTVGKPLpRVEAKIIMDDGTETKAGV-GELCIRSPSLFrEYWKRPE 482
Cdd:cd05929 263 QWIDWGGPIIWEYYGGTEGQgLTIINGEEWLTHPGSVGRAV-LGKVHILDEDGNEVPPGEiGEVYFANGPGF-EYTNDPE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 483 VTEESFIDGGFFKTGDTVTIDEDGYFKILGRtNADIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAII 562
Cdd:cd05929 341 KTAAARNEGGWSTLGDVGYLDEDGYLYLTDR-RSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVV 419
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 563 VAKEDVKERAEQASEpaltlqaLTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:cd05929 420 QPAPGADAGTALAEE-------LIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
134-622 |
1.18e-33 |
|
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: 136.08 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTK--CSTGYS 211
Cdd:cd05968 112 GVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGFTRRGREVNLKeeADKACA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 212 LLPSVESIppKIESQEPLSSELTSSVSSLLAEI-----DNLKKIKGDDPALILYTSGTTGKPKGVVHTHKGI-LSQVQIL 285
Cdd:cd05968 192 QCPTVEKV--VVVRHLGNDFTPAKGRDLSYDEEketagDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFpLKAAQDM 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 286 TEAWGYQSEDQFLHCLPLHHVHGLFnALFAPLYSGSVV---EFMPKFSVRGVWQRWRESYpsgvsksndAITVFTGVPTV 362
Cdd:cd05968 270 YFQFDLKPGDLLTWFTDLGWMMGPW-LIFGGLILGATMvlyDGAPDHPKADRLWRMVEDH---------EITHLGLSPTL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 363 yTRLLQGYDTmNPDEQSACSyaakQLRLM-MCGSSALPSPLMKRWEEVTGHRL--LERYGMTEFVMA-LSNPLHGPRKEG 438
Cdd:cd05968 340 -IRALKPRGD-APVNAHDLS----SLRVLgSTGEPWNPEPWNWLFETVGKGRNpiINYSGGTEISGGiLGNVLIKPIKPS 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 439 TVGKPLPRVEAKIIMDDGTETKAGVGELCIRSP--SLFREYWKRPEVTEESFID--GGFFKTGDTVTIDEDGYFKILGRT 514
Cdd:cd05968 414 SFNGPVPGMKADVLDESGKPARPEVGELVLLAPwpGMTRGFWRDEDRYLETYWSrfDNVWVHGDFAYYDEEGYFYILGRS 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 515 NaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKERAEQASEpaltlqaLTSWSKDKLA 594
Cdd:cd05968 494 D-DTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEE-------LMERVADELG 565
|
490 500
....*....|....*....|....*...
gi 2212542879 595 PYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:cd05968 566 KPLSPERILFVKDLPKTRNAKVMRRVIR 593
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
251-568 |
1.78e-33 |
|
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: 135.04 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 251 KGDDPALILYTSGTTGKPKGVVHTHKGILSQV----QILTEAWGYQSEDQFLHCLPLHHVHGLFNALFApLYSGSVVefm 326
Cdd:cd05927 112 KPEDLATICYTSGTTGNPKGVMLTHGNIVSNVagvfKILEILNKINPTDVYISYLPLAHIFERVVEALF-LYHGAKI--- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 327 pkfsvrGVWQrwresypsG-VSKSNDAI-----TVFTGVPTVYTRLLQGydTMNPDEQS----------ACSYAAKQL-- 388
Cdd:cd05927 188 ------GFYS--------GdIRLLLDDIkalkpTVFPGVPRVLNRIYDK--IFNKVQAKgplkrklfnfALNYKLAELrs 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 389 -------------------------RLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHGPRKEGTVGKP 443
Cdd:cd05927 252 gvvraspfwdklvfnkikqalggnvRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 444 LPRVEAKII----MDDGTETKAGVGELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIM 519
Cdd:cd05927 332 LPCAEVKLVdvpeMNYDAKDPNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKK-NIF 410
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2212542879 520 KV--GGYkLSALEIEAVLLEHDTILECAVLGLPDEAYgevICAIIVAKEDV 568
Cdd:cd05927 411 KLsqGEY-VAPEKIENIYARSPFVAQIFVYGDSLKSF---LVAIVVPDPDV 457
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
242-622 |
4.22e-33 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 135.16 E-value: 4.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 242 AEIDNLKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILT-EAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSG 320
Cdd:PRK06060 134 VAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCrKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATG 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 321 S--VVEFMPKFSVRGVWQRWRESyPSgvsksndaitVFTGVPTVYTRLLqgyDTMNPDeqsacsyAAKQLRLMMCGSSAL 398
Cdd:PRK06060 214 GsaVINSAPVTPEAAAILSARFG-PS----------VLYGVPNFFARVI---DSCSPD-------SFRSLRCVVSAGEAL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 399 PSPLMKRWEEVTGH-RLLERYGMTE----FVmalSNPLHGPRKeGTVGKPLPRVEAKIIMDDGTETKAGV-GELCIRSPS 472
Cdd:PRK06060 273 ELGLAERLMEFFGGiPILDGIGSTEvgqtFV---SNRVDEWRL-GTLGRVLPPYEIRVVAPDGTTAGPGVeGDLWVRGPA 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 473 LFREYWKRPEVTEEsfiDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDE 552
Cdd:PRK06060 349 IAKGYWNRPDSPVA---NEGWLDTRDRVCIDSDGWVTYRCRAD-DTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRES 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 553 AYGEVICAIIVAKedVKERAEQASEPALTLQALTswskdKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:PRK06060 425 TGASTLQAFLVAT--SGATIDGSVMRDLHRGLLN-----RLSAFKVPHRFAVVDRLPRTPNGKLVRGALR 487
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
253-624 |
5.40e-33 |
|
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: 131.54 E-value: 5.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHK----GILSqvqilTEAW-GYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFM- 326
Cdd:cd05974 85 DDPMLLYFTSGTTSKPKLVEHTHRsypvGHLS-----TMYWiGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFn 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 327 -PKFSVRGVWqrwresypSGVSKSNdaITVFTGVPTVYTRLLQgydtmnpdeQSACSYAAKqLRLMMCGSSALPSPLMKR 405
Cdd:cd05974 160 yARFDAKRVL--------AALVRYG--VTTLCAPPTVWRMLIQ---------QDLASFDVK-LREVVGAGEPLNPEVIEQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 406 WEEVTGHRLLERYGMTEFVMALSNPLHGPRKEGTVGKPLPRVEAKIIMDDGTETKAgvGELCI-----RSPSLFREYWKR 480
Cdd:cd05974 220 VRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPATE--GEVALdlgdtRPVGLMKGYAGD 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 481 PEVTEESfIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICA 560
Cdd:cd05974 298 PDKTAHA-MRGGYYRTGDIAMRDEDGYLTYVGRAD-DVFKSSDYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKA 375
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2212542879 561 IIVakedVKERAEQASEPALTlqaLTSWSKDKLAPYKIPTRLYLWDsLPRNAMGKVNKKELKKL 624
Cdd:cd05974 376 FIV----LRAGYEPSPETALE---IFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRRVELRRR 431
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
260-626 |
1.14e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 132.52 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 260 YTSGTTGKPKGVVHTHKGIL--SQVQILTEAWGYQSEDQFLHCLPLHHVH--GLFNAlfAPLYSGSVVEFMPKFSVRGVW 335
Cdd:PRK07008 183 YTSGTTGNPKGALYSHRSTVlhAYGAALPDAMGLSARDAVLPVVPMFHVNawGLPYS--APLTGAKLVLPGPDLDGKSLY 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 336 QRWREsypsgvsksnDAITVFTGVPTVYTRLLQgydTMNPDEQSACSyaakqLRLMMCGSSALPSPLMKRWEEVTGHRLL 415
Cdd:PRK07008 261 ELIEA----------ERVTFSAGVPTVWLGLLN---HMREAGLRFST-----LRRTVIGGSACPPAMIRTFEDEYGVEVI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 416 ERYGMTEFvmalsNPL---------HGPRKEGTV-------GKPLPRVEAKIIMDDGTET----KAgVGELCIRSPSLFR 475
Cdd:PRK07008 323 HAWGMTEM-----SPLgtlcklkwkHSQLPLDEQrkllekqGRVIYGVDMKIVGDDGRELpwdgKA-FGDLQVRGPWVID 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 476 EYWKRpevtEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYG 555
Cdd:PRK07008 397 RYFRG----DASPLVDGWFPTGDVATIDADGFMQITDRSK-DVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWD 471
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2212542879 556 EVICAIIVAKEDVKeraeqasepaLTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLLQ 626
Cdd:PRK07008 472 ERPLLVVVKRPGAE----------VTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQFR 532
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
252-623 |
2.22e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 131.34 E-value: 2.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 252 GDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSV 331
Cdd:PRK07867 151 PDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 332 RGVWQRWREsYpsGVSKSNdaitvFTGVPTVYtrLLQGYDTmnPDEqsacsyAAKQLRLMMcGSSALPSPLmKRWEEVTG 411
Cdd:PRK07867 231 SGFLPDVRR-Y--GATYAN-----YVGKPLSY--VLATPER--PDD------ADNPLRIVY-GNEGAPGDI-ARFARRFG 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 412 HRLLERYGMTEFVMALSNPLHGPrkEGTVGKPLPRVE------------AKIIMDDGTETKAGVGELC-IRSPSLFREYW 478
Cdd:PRK07867 291 CVVVDGFGSTEGGVAITRTPDTP--PGALGPLPPGVAivdpdtgtecppAEDADGRLLNADEAIGELVnTAGPGGFEGYY 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 479 KRPEVTEESfIDGGFFKTGDTVTIDEDGYFKILGRTnADIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVI 558
Cdd:PRK07867 369 NDPEADAER-MRGGVYWSGDLAYRDADGYAYFAGRL-GDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQV 446
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2212542879 559 CAIIVAKEDVKERAEQASEpALTLQaltswskDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKK 623
Cdd:PRK07867 447 MAALVLAPGAKFDPDAFAE-FLAAQ-------PDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
386-626 |
2.75e-32 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 131.27 E-value: 2.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 386 KQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEfvmALSN--PLHGP--RKEGTVGKPL-PRVEAKIIMDDGTETK 460
Cdd:PRK10946 300 ASLKLLQVGGARLSETLARRIPAELGCQLQQVFGMAE---GLVNytRLDDSdeRIFTTQGRPMsPDDEVWVADADGNPLP 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 461 AG-VGELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNADIMKvGGYKLSALEIEAVLLEHD 539
Cdd:PRK10946 377 QGeVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKDQINR-GGEKIAAEEIENLLLRHP 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 540 TILECAVLGLPDEAYGEVICAIIVAKEDVKeraeqasepALTLQaltSWSKDK-LAPYKIPTRLYLWDSLPRNAMGKVNK 618
Cdd:PRK10946 456 AVIHAALVSMEDELMGEKSCAFLVVKEPLK---------AVQLR---RFLREQgIAEFKLPDRVECVDSLPLTAVGKVDK 523
|
....*...
gi 2212542879 619 KELKKLLQ 626
Cdd:PRK10946 524 KQLRQWLA 531
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
141-623 |
3.41e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 133.93 E-value: 3.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 141 IGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLsTKEHHEimesistkcstgyslLPSVESIP 220
Cdd:PRK12316 3110 VGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLL-SQSHLR---------------LPLAQGVQ 3173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 221 PKIESQEPlsseltssvsSLLAEIDNLKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHC 300
Cdd:PRK12316 3174 VLDLDRGD----------ENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQF 3243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 301 LPLhHVHGLFNALFAPLYSGSVVefmpkfsVRGVWQRWRESYPSGVSKSNDAITVFTGVPTVYTRLLQgydtmNPDEQSA 380
Cdd:PRK12316 3244 TTF-SFDVFVEELFWPLMSGARV-------VLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLE-----EEDAHRC 3310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 381 CSyaakqLRLMMCGSSALPSPLMKRWeeVTGHRLLERYGMTEFVMALSNPLHGPRKEGT--VGKPLPRVEAKIIMDDGTE 458
Cdd:PRK12316 3311 TS-----LKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDGSLEP 3383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 459 TKAG-VGELCIRSPSLFREYWKRPEVTEESFIDGGF------FKTGDTVTIDEDGYFKILGRTNADImKVGGYKLSALEI 531
Cdd:PRK12316 3384 VPVGaLGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQV-KIRGFRIELGEI 3462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 532 EAVLLEHDTILECAVLGLPdeayGEVICAIIVAkedvkeraeQASEPALTlQALTSWSKDKLAPYKIPTRLYLWDSLPRN 611
Cdd:PRK12316 3463 EARLLEHPWVREAVVLAVD----GRQLVAYVVP---------EDEAGDLR-EALKAHLKASLPEYMVPAHLLFLERMPLT 3528
|
490
....*....|..
gi 2212542879 612 AMGKVNKKELKK 623
Cdd:PRK12316 3529 PNGKLDRKALPR 3540
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
139-624 |
4.32e-32 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 133.36 E-value: 4.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 139 ARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLStkeHHEIMESistkcstgyslLPSVES 218
Cdd:PRK12467 1625 VLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLT---QSHLQAR-----------LPLPDG 1690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 219 IPPKIESQEplsseltSSVSSLLAEIDNLKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFL 298
Cdd:PRK12467 1691 LRSLVLDQE-------DDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVL 1763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 299 HCLPLHhvhglFN----ALFAPLYSGSVVEFMPKFSVRGVWQRWRESYPSGVsksndaiTVFTGVPTVYTRLLQgydtmn 374
Cdd:PRK12467 1764 QFTSFA-----FDvsvwELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQV-------TTLHFVPSMLQQLLQ------ 1825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 375 PDEQSAcsyAAKQLRLMMCGSSALPSPLMKRWEEVTGHR-LLERYGMTEfvmALSNPLHGP--------RKEGTVGKPLP 445
Cdd:PRK12467 1826 MDEQVE---HPLSLRRVVCGGEALEVEALRPWLERLPDTgLFNLYGPTE---TAVDVTHWTcrrkdlegRDSVPIGQPIA 1899
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 446 RVeAKIIMDDGTETKA-GV-GELCIRSPSLFREYWKRPEVTEESFI-------DGGFFKTGDTVTIDEDGYFKILGRTNA 516
Cdd:PRK12467 1900 NL-STYILDASLNPVPiGVaGELYLGGVGLARGYLNRPALTAERFVadpfgtvGSRLYRTGDLARYRADGVIEYLGRIDH 1978
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 517 DImKVGGYKLSALEIEAVLLEHDTILECAVLGLpDEAYGEVICAIIVAKEdvKERAEQASEPALTLQALTSWSKDKLAPY 596
Cdd:PRK12467 1979 QV-KIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVPTD--PGLVDDDEAQVALRAILKNHLKASLPEY 2054
|
490 500
....*....|....*....|....*...
gi 2212542879 597 KIPTRLYLWDSLPRNAMGKVNKKELKKL 624
Cdd:PRK12467 2055 MVPAHLVFLARMPLTPNGKLDRKALPAP 2082
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
254-624 |
1.25e-31 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 129.75 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 254 DPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVefmpkfSVRG 333
Cdd:PLN03102 187 DPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNGWTFTWGTAARGGTSV------CMRH 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 334 VWQRwrESYPSgVSKSNdaITVFTGVPTVYTRLLQGydtmNPDEQSACSYAAKqlrlMMCGSSALPSPLMKRWEEVtGHR 413
Cdd:PLN03102 261 VTAP--EIYKN-IEMHN--VTHMCCVPTVFNILLKG----NSLDLSPRSGPVH----VLTGGSPPPAALVKKVQRL-GFQ 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 414 LLERYGMTEFV--------------MALSNPLHGPRKEGTVGKPLPRVEAKiimddGTETKAGV-------GELCIRSPS 472
Cdd:PLN03102 327 VMHAYGLTEATgpvlfcewqdewnrLPENQQMELKARQGVSILGLADVDVK-----NKETQESVprdgktmGEIVIKGSS 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 473 LFREYWKRPEVTEESFiDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDE 552
Cdd:PLN03102 402 IMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSK-DIIISGGENISSVEVENVLYKYPKVLETAVVAMPHP 479
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2212542879 553 AYGEVICAIIVAKEDVKERAEQASEPALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKL 624
Cdd:PLN03102 480 TWGETPCAFVVLEKGETTKEDRVDKLVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDI 551
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
251-513 |
1.30e-31 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 130.60 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 251 KGDDPALILYTSGTTGKPKGVVHTHKGILSQV-QILTEAwGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPK- 328
Cdd:PRK08043 363 QPEDAALILFTSGSEGHPKGVVHSHKSLLANVeQIKTIA-DFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYPSp 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 329 FSVRGVwqrwresyPSGVSKSNdaITVFTGVPTV---YTRLLQGYDtmnpdeqsacsYAakQLRLMMCGSSALPSPLMKR 405
Cdd:PRK08043 442 LHYRIV--------PELVYDRN--CTVLFGTSTFlgnYARFANPYD-----------FA--RLRYVVAGAEKLQESTKQL 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 406 WEEVTGHRLLERYGMTEF--VMALSNPLHGprKEGTVGKPLPRVEAKIIMDDGTETKagvGELCIRSPSLFREYWK--RP 481
Cdd:PRK08043 499 WQDKFGLRILEGYGVTECapVVSINVPMAA--KPGTVGRILPGMDARLLSVPGIEQG---GRLQLKGPNIMNGYLRveKP 573
|
250 260 270
....*....|....*....|....*....|....*....
gi 2212542879 482 EVTE-------ESFIDGGFFKTGDTVTIDEDGYFKILGR 513
Cdd:PRK08043 574 GVLEvptaenaRGEMERGWYDTGDIVRFDEQGFVQIQGR 612
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
254-624 |
1.54e-31 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 129.88 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 254 DPALILYTSGTTGKPKGVVHTHKGILSQVQiLTEAW--GYQSEDQFLhClplhhvhglfNA-----------LFAPLYSG 320
Cdd:PRK00174 246 DPLFILYTSGSTGKPKGVLHTTGGYLVYAA-MTMKYvfDYKDGDVYW-C----------TAdvgwvtghsyiVYGPLANG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 321 S---VVEFMPKFSVRGVWqrWR--ESYpsGVsksndaiTVFTGVPTVyTRLLQGYDTMNPDeqsacSYAAKQLRLMmcGS 395
Cdd:PRK00174 314 AttlMFEGVPNYPDPGRF--WEviDKH--KV-------TIFYTAPTA-IRALMKEGDEHPK-----KYDLSSLRLL--GS 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 396 SALP-SPLMKRW-EEVTGHrllER------YGMTEFVMALSNPLHG--PRKEGTVGKPLPRVEAKIIMDDGTETKAGV-G 464
Cdd:PRK00174 375 VGEPiNPEAWEWyYKVVGG---ERcpivdtWWQTETGGIMITPLPGatPLKPGSATRPLPGIQPAVVDEEGNPLEGGEgG 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 465 ELCIRS--PSLFREYWKRPEVTEESF---IDGGFFkTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHD 539
Cdd:PRK00174 452 NLVIKDpwPGMMRTIYGDHERFVKTYfstFKGMYF-TGDGARRDEDGYYWITGRVD-DVLNVSGHRLGTAEIESALVAHP 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 540 TILECAVLGLPDEAYGEVICAIIVAKEDVKERAEQASEpaltlqaLTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKK 619
Cdd:PRK00174 530 KVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKE-------LRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKIMRR 602
|
....*
gi 2212542879 620 ELKKL 624
Cdd:PRK00174 603 ILRKI 607
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
136-623 |
5.80e-31 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 127.40 E-value: 5.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 136 LRGARIGIVAKPS-AEFVAGIFGTWLSGGV---AVPLALsypEVELLHVMNDSDISMVLSTKEHHEIMESIStkcstgys 211
Cdd:PLN02330 77 LRKGQVVVVVLPNvAEYGIVALGIMAAGGVfsgANPTAL---ESEIKKQAEAAGAKLIVTNDTNYGKVKGLG-------- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 212 lLPSV----ESIPPKIESQEPLSSELTSSVSSLLAEIdnlkkIKGDDPALIlYTSGTTGKPKGVVHTHKGILSQvqILTE 287
Cdd:PLN02330 146 -LPVIvlgeEKIEGAVNWKELLEAADRAGDTSDNEEI-----LQTDLCALP-FSSGTTGISKGVMLTHRNLVAN--LCSS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 288 AWGYQSE--DQF--LHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGVWQrwresypsgvSKSNDAITVFTGVPTVY 363
Cdd:PLN02330 217 LFSVGPEmiGQVvtLGLIPFFHIYGITGICCATLRNKGKVVVMSRFELRTFLN----------ALITQEVSFAPIVPPII 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 364 TRLLQgydtmNP--DEqsaCSYAAKQLRLMMCGSSALPSPLMKRWE-EVTGHRLLERYGMTE---FVMALSNPL--HGPR 435
Cdd:PLN02330 287 LNLVK-----NPivEE---FDLSKLKLQAIMTAAAPLAPELLTAFEaKFPGVQVQEAYGLTEhscITLTHGDPEkgHGIA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 436 KEGTVGKPLPRVEAKIIMDDGTET--KAGVGELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGR 513
Cdd:PLN02330 359 KKNSVGFILPNLEVKFIDPDTGRSlpKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDR 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 514 TNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKERAEQasepaltlqaLTSWSKDKL 593
Cdd:PLN02330 439 IK-ELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEED----------ILNFVAANV 507
|
490 500 510
....*....|....*....|....*....|
gi 2212542879 594 APYKIPTRLYLWDSLPRNAMGKVNKKELKK 623
Cdd:PLN02330 508 AHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
253-621 |
1.94e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 125.91 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFnALFAP-LYSGSVVEFMPKFSV 331
Cdd:PRK13388 150 MDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVM-AGWAPaVASGAAVALPAKFSA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 332 RGVW---QRWRESYPSGVSKsndAITVFTGVPTvytrllqgydtmNPDEqsacsyAAKQLRLMMcGSSALPSPlMKRWEE 408
Cdd:PRK13388 229 SGFLddvRRYGATYFNYVGK---PLAYILATPE------------RPDD------ADNPLRVAF-GNEASPRD-IAEFSR 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 409 VTGHRLLERYGMTEFVMALSNPLHGPrkEGTVGKPLPRVE----------AKIIMD-DGTETKA--GVGELCIRS-PSLF 474
Cdd:PRK13388 286 RFGCQVEDGYGSSEGAVIVVREPGTP--PGSIGRGAPGVAiynpetltecAVARFDaHGALLNAdeAIGELVNTAgAGFF 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 475 REYWKRPEVTEESfIDGGFFKTGDTVTIDEDGYFKILGRTnADIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAY 554
Cdd:PRK13388 364 EGYYNNPEATAER-MRHGMYWSGDLAYRDADGWIYFAGRT-ADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERV 441
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 555 G-EVICAIIVAKEDvkeraeqasepALTLQALTSW--SKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 621
Cdd:PRK13388 442 GdQVMAALVLRDGA-----------TFDPDAFAAFlaAQPDLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
253-574 |
4.81e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 125.86 E-value: 4.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTH----KGILSQVQILTEAWGYQSEDQ-FLHCLPLHHV--HGLFNALFA---------- 315
Cdd:PTZ00216 264 DDLALIMYTSGTTGDPKGVMHTHgsltAGILALEDRLNDLIGPPEEDEtYCSYLPLAHImeFGVTNIFLArgaligfgsp 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 316 ---------PlySGSVVEFMPKFSVrGVwQRWRESY---------PSGVSKSndaiTVFTgvpTVY-TRL---LQGYDTM 373
Cdd:PTZ00216 344 rtltdtfarP--HGDLTEFRPVFLI-GV-PRIFDTIkkaveaklpPVGSLKR----RVFD---HAYqSRLralKEGKDTP 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 374 NPDEQ--SACSYA-AKQLRLMMCGSSALpSPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHGPRKEGTVGKPLPRVEAK 450
Cdd:PTZ00216 413 YWNEKvfSAPRAVlGGRVRAMLSGGGPL-SAATQEFVNVVFGMVIQGWGLTETVCCGGIQRTGDLEPNAVGQLLKGVEMK 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 451 IIMDDG---TETKAGVGELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNADIMKVGGYKLs 527
Cdd:PTZ00216 492 LLDTEEykhTDTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYI- 570
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2212542879 528 ALE-IEAVLLEHDTILE---CaVLGLPDEAYgevICAIIVAKED-VKERAEQ 574
Cdd:PTZ00216 571 ALEaLEALYGQNELVVPngvC-VLVHPARSY---ICALVLTDEAkAMAFAKE 618
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
150-626 |
6.56e-30 |
|
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: 124.32 E-value: 6.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 150 EFVAGIFGTWLSGGVAVPL--ALSYPEVE-----LLHVmndsdismvlstkehHEIMESisTKCSTGYSLLPSVESIppK 222
Cdd:cd05906 76 DFIPAFWACVLAGFVPAPLtvPPTYDEPNarlrkLRHI---------------WQLLGS--PVVLTDAELVAEFAGL--E 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 223 IESQEPLSSELTSSVSSLLAEIDNLKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLP 302
Cdd:cd05906 137 TLSGLPGIRVLSIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVP 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 303 LHHVhglfnalfaplysGSVVEFmpkfSVRGVWqrwresypSGVSKSNDAITVFTGVPTVYTRLLQGYD---TMNPdeQS 379
Cdd:cd05906 217 LDHV-------------GGLVEL----HLRAVY--------LGCQQVHVPTEEILADPLRWLDLIDRYRvtiTWAP--NF 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 380 ACSYAAKQLRLMMCGSSALPSplMKRW----EEV---TGHRLLER--------------YGMTE------FVMALSNPLH 432
Cdd:cd05906 270 AFALLNDLLEEIEDGTWDLSS--LRYLvnagEAVvakTIRRLLRLlepyglppdairpaFGMTEtcsgviYSRSFPTYDH 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 433 GPRKEGT-VGKPLPRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDeDGYFKI 510
Cdd:cd05906 348 SQALEFVsLGRPIPGVSMRIVDDEGQLLPEGeVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLD-NGNLTI 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 511 LGRTnADIMKVGGYKLSALEIEAVLLEHDtILE----CAVLGLPDEAYGEVICAIIVAkedvkeRAEQASEPALTLQALT 586
Cdd:cd05906 427 TGRT-KDTIIVNGVNYYSHEIEAAVEEVP-GVEpsftAAFAVRDPGAETEELAIFFVP------EYDLQDALSETLRAIR 498
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2212542879 587 SWSKDK--LAP-YKIPTRLylwDSLPRNAMGKVNKKELKKLLQ 626
Cdd:cd05906 499 SVVSREvgVSPaYLIPLPK---EEIPKTSLGKIQRSKLKAAFE 538
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
130-623 |
7.09e-30 |
|
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: 122.42 E-value: 7.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 130 IDGTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKehheimesistkcstg 209
Cdd:cd17653 39 LLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTD---------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 210 ysllpsvesippkiesqeplsseltssvssllaeidnlkkiKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQilteaw 289
Cdd:cd17653 103 -----------------------------------------SPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVS------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 290 gyQSEDQfLHCLPlHHVHGLF---------NALFAPL-YSGSVVEFMPkfsvrgvwqrwrESYPSGVSKSndaITVFTGV 359
Cdd:cd17653 136 --QPPAR-LDVGP-GSRVAQVlsiafdaciGEIFSTLcNGGTLVLADP------------SDPFAHVART---VDALMST 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 360 PTVytrlLQgydTMNPDEQSacsyaakQLRLMMCGSSALPSPLMKRWEEvtGHRLLERYGMTEFVMALSNPLHGPRKEGT 439
Cdd:cd17653 197 PSI----LS---TLSPQDFP-------NLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVT 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 440 VGKPLPRVEAKIIMDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGF------FKTGDTVTIDEDGYFKILG 512
Cdd:cd17653 261 IGKPIPNSTCYILDADLQPVPEGVvGEICISGVQVARGYLGNPALTASKFVPDPFwpgsrmYRTGDYGRWTEDGGLEFLG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 513 RTNADImKVGGYKLSALEIEAVLLEHDTILECAVLGLpdeaYGEVICAII----VAKEDVKERAEQasepaltlqaltsw 588
Cdd:cd17653 341 REDNQV-KVRGFRINLEEIEEVVLQSQPEVTQAAAIV----VNGRLVAFVtpetVDVDGLRSELAK-------------- 401
|
490 500 510
....*....|....*....|....*....|....*
gi 2212542879 589 skdKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKK 623
Cdd:cd17653 402 ---HLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
260-622 |
7.79e-30 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 124.19 E-value: 7.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 260 YTSGTTGKPKGVVHTHKGilSQVQILTEA--WGYQSEDQFLHCLPLHHVHG-LFNALFAPLYSGSVVefMPKFSVRGVWQ 336
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRG--AYLMALSNAliWGMNEGAVYLWTLPMFHCNGwCFTWTLAALCGTNIC--LRQVTAKAIYS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 337 rwresypsgvSKSNDAITVFTGVPTVYTRLLQGydtmnPDEQSACSYAaKQLRLMMCGSSALPSPLMKRWEEvtGHRLLE 416
Cdd:PLN02479 278 ----------AIANYGVTHFCAAPVVLNTIVNA-----PKSETILPLP-RVVHVMTAGAAPPPSVLFAMSEK--GFRVTH 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 417 RYGMTE-------------------FVMALSNPLHGPRKEGTVG---------KPLPRveakiimdDGTEtkagVGELCI 468
Cdd:PLN02479 340 TYGLSEtygpstvcawkpewdslppEEQARLNARQGVRYIGLEGldvvdtktmKPVPA--------DGKT----MGEIVM 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 469 RSPSLFREYWKRPEVTEESFiDGGFFKTGDTVTIDEDGYFKILGRtNADIMKVGGYKLSALEIEAVLLEHDTILECAVLG 548
Cdd:PLN02479 408 RGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDR-SKDIIISGGENISSLEVENVVYTHPAVLEASVVA 485
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2212542879 549 LPDEAYGEVICAIIVAKEDvkerAEQASEPALTlQALTSWSKDKLAPYKIPtRLYLWDSLPRNAMGKVNKKELK 622
Cdd:PLN02479 486 RPDERWGESPCAFVTLKPG----VDKSDEAALA-EDIMKFCRERLPAYWVP-KSVVFGPLPKTATGKIQKHVLR 553
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
139-621 |
2.16e-29 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 125.28 E-value: 2.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 139 ARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKCSTGYSLLpSVES 218
Cdd:PRK05691 1182 VCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSL-HLDS 1260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 219 IPpkieSQEPLSSeltssvssllaeidnlkkIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFL 298
Cdd:PRK05691 1261 WP----SQAPGLH------------------LHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLM 1318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 299 HCLPLHHVHGLFNAlFAPLYSGSvvefmpKFSVRGVWQRwRESYPSGVSKSNDAITVFTGVPTvytrLLQGYdTMNPDEQ 378
Cdd:PRK05691 1319 QKAPISFDVSVWEC-FWPLITGC------RLVLAGPGEH-RDPQRIAELVQQYGVTTLHFVPP----LLQLF-IDEPLAA 1385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 379 SACSyaakqLRLMMCGSSALPSPLMKR-WEEVTGHRLLERYGMTEFVMALSNpLHGPRKEGT---VGKPLPRVEAKIIMD 454
Cdd:PRK05691 1386 ACTS-----LRRLFSGGEALPAELRNRvLQRLPQVQLHNRYGPTETAINVTH-WQCQAEDGErspIGRPLGNVLCRVLDA 1459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 455 DGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFI------DGG-FFKTGDTVTIDEDGYFKILGRTNADImKVGGYKL 526
Cdd:PRK05691 1460 ELNLLPPGVaGELCIGGAGLARGYLGRPALTAERFVpdplgeDGArLYRTGDRARWNADGALEYLGRLDQQV-KLRGFRV 1538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 527 SALEIEAVLLEHDTILECAVLgLPDEAYGEVICAIIVAKedvkerAEQASEPALTLQALtswsKDKLAPYKIPTRLYLWD 606
Cdd:PRK05691 1539 EPEEIQARLLAQPGVAQAAVL-VREGAAGAQLVGYYTGE------AGQEAEAERLKAAL----AAELPEYMVPAQLIRLD 1607
|
490
....*....|....*
gi 2212542879 607 SLPRNAMGKVNKKEL 621
Cdd:PRK05691 1608 QMPLGPSGKLDRRAL 1622
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
253-625 |
2.83e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 119.38 E-value: 2.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGyqSEDQFLHCLPLHHVHGLfNALFAPLYSGS---VVEFMPKF 329
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLG--GPGQWLLALPAHHIAGL-QVLVRSVIAGSepvELDVSAGF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 330 SVrgvwqrwrESYPSGVSKsndaitvfTGVPTVYTRL--LQGYDTMNPDEQSAcsyAAKQLRLMMCGSSALPSPLMKRWE 407
Cdd:PRK07824 112 DP--------TALPRAVAE--------LGGGRRYTSLvpMQLAKALDDPAATA---ALAELDAVLVGGGPAPAPVLDAAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 408 EVtGHRLLERYGMTEfvmalsnplhgpRKEGTV--GKPLprveakiimdDGTETKAGVGELCIRSPSLFREYwkRPEVTE 485
Cdd:PRK07824 173 AA-GINVVRTYGMSE------------TSGGCVydGVPL----------DGVRVRVEDGRIALGGPTLAKGY--RNPVDP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 486 ESFIDGGFFKTGDTVTIDeDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAk 565
Cdd:PRK07824 228 DPFAEPGWFRTDDLGALD-DGVLTVLGRAD-DAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVG- 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 566 edvkeraeqASEPALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLL 625
Cdd:PRK07824 305 ---------DGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
253-626 |
3.68e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 122.16 E-value: 3.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGlFNALFAPLYSGSVVEFMPKFSVR 332
Cdd:PRK06164 181 DAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFG-FSTLLGALAGGAPLVCEPVFDAA 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 333 GVWQRWRESYPSGVSKSNDAitvftgvptvYTRLLQGYDTmNPDEQSA--CSYAAkqlrlMMCGSSALPSplmkrWEEVT 410
Cdd:PRK06164 260 RTARALRRHRVTHTFGNDEM----------LRRILDTAGE-RADFPSArlFGFAS-----FAPALGELAA-----LARAR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 411 GHRLLERYGMTE-FVMALSNPLHGP---RKE--GTVGKPLPRVEAKIIMDDGTETKAGVGELCIRSPSLFREYWKRPEVT 484
Cdd:PRK06164 319 GVPLTGLYGSSEvQALVALQPATDPvsvRIEggGRPASPEARVRARDPQDGALLPDGESGEIEIRAPSLMRGYLDNPDAT 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 485 EESFIDGGFFKTGDTVTIDEDGYFKILGRTnADIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVIcAIIVA 564
Cdd:PRK06164 399 ARALTDDGYFRTGDLGYTRGDGQFVYQTRM-GDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV-AFVIP 476
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2212542879 565 KEdvkerAEQASEPaltlqALTSWSKDKLAPYKIPTRLYLWDSLPRNAMG---KVNKKELKKLLQ 626
Cdd:PRK06164 477 TD-----GASPDEA-----GLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQ 531
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
253-626 |
6.03e-29 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 120.73 E-value: 6.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHclplhhvhglFNA---------LFAPLYSGSVV 323
Cdd:cd05918 106 SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQ----------FASytfdvsileIFTTLAAGGCL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 324 eFMPKFSVR-----GVWQRWResypsgvsksndaITVFTGVPTVyTRLLQgydtmnPDEqsacsyaAKQLRLMMCGSSAL 398
Cdd:cd05918 176 -CIPSEEDRlndlaGFINRLR-------------VTWAFLTPSV-ARLLD------PED-------VPSLRTLVLGGEAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 399 PSPLMKRWEEVTghRLLERYGMTEF-VMALSNPLHGPRKEGTVGKPLPRVeaKIIMDDGTETK----AGVGELCIRSPSL 473
Cdd:cd05918 228 TQSDVDTWADRV--RLINAYGPAECtIAATVSPVVPSTDPRNIGRPLGAT--CWVVDPDNHDRlvpiGAVGELLIEGPIL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 474 FREYWKRPEVTEESFID-------------GGFFKTGDTVTIDEDGYFKILGRTNADImKVGGYKLSALEIEAVLLEHDT 540
Cdd:cd05918 304 ARGYLNDPEKTAAAFIEdpawlkqegsgrgRRLYRTGDLVRYNPDGSLEYVGRKDTQV-KIRGQRVELGEIEHHLRQSLP 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 541 ILECAVLGL---PDEAYGEVICAIIVAKEDVKER-------AEQASEPALTLQALTSWSKDKLAPYKIPTrlyLW---DS 607
Cdd:cd05918 383 GAKEVVVEVvkpKDGSSSPQLVAFVVLDGSSSGSgdgdslfLEPSDEFRALVAELRSKLRQRLPSYMVPS---VFlplSH 459
|
410
....*....|....*....
gi 2212542879 608 LPRNAMGKVNKKELKKLLQ 626
Cdd:cd05918 460 LPLTASGKIDRRALRELAE 478
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
132-621 |
2.25e-28 |
|
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: 118.34 E-value: 2.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 132 GTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLStkehheimesistkcstgys 211
Cdd:cd17650 31 GLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLT-------------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 212 llpsvesippkiesqEPlsseltssvssllaeidnlkkikgDDPALILYTSGTTGKPKGVVHTHKGILSQVQilteAWGY 291
Cdd:cd17650 91 ---------------QP------------------------EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAH----AWRR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 292 QSEdqfLHCLPLHHVH------GLFNALFA-PLYSGSVVEFMP---KFSVRGVWQRWRESypsgvsksndAITVFTGVPT 361
Cdd:cd17650 128 EYE---LDSFPVRLLQmasfsfDVFAGDFArSLLNGGTLVICPdevKLDPAALYDLILKS----------RITLMESTPA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 362 VyTRLLQGYDTMNPDEQSacsyaakQLRLMMCGSSALPSPLMKRWEEVTGH--RLLERYGMTEFVMALSNPLHGPRKEGT 439
Cdd:cd17650 195 L-IRPVMAYVYRNGLDLS-------AMRLLIVGSDGCKAQDFKTLAARFGQgmRIINSYGVTEATIDSTYYEEGRDPLGD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 440 -----VGKPLPRVEAKIIMDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGF------FKTGDTVTIDEDGY 507
Cdd:cd17650 267 sanvpIGRPLPNTAMYVLDERLQPQPVGVaGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGN 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 508 FKILGRtNADIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEdvkeraeqasepALTLQALTS 587
Cdd:cd17650 347 VELLGR-VDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAA------------TLNTAELRA 413
|
490 500 510
....*....|....*....|....*....|....
gi 2212542879 588 WSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 621
Cdd:cd17650 414 FLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
253-623 |
1.38e-27 |
|
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: 116.38 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVR 332
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSAS 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 333 gvwQRWRESYPSGVsksndaiTVFTGVPTVYTRLLQGydTMNPDEqsacsyaaKQLRLMMCGSSALPSPLMKRWEEVTGH 412
Cdd:cd05937 167 ---QFWKDVRDSGA-------TIIQYVGELCRYLLST--PPSPYD--------RDHKVRVAWGNGLRPDIWERFRERFNV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 413 RLL-ERYGMTEFVMALSNPLHGPRKEGTVGK--PLPR-----VEAKIIMDDGTET-----KAGV---------GELCIRS 470
Cdd:cd05937 227 PEIgEFYAATEGVFALTNHNVGDFGAGAIGHhgLIRRwkfenQVVLVKMDPETDDpirdpKTGFcvrapvgepGEMLGRV 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 471 P----SLFREYWKRPEVTEESFIDGGF------FKTGDTVTIDEDGYFKILGRTnADIMKVGGYKLSALEIEAVLLEHDT 540
Cdd:cd05937 307 PfknrEAFQGYLHNEDATESKLVRDVFrkgdiyFRTGDLLRQDADGRWYFLDRL-GDTFRWKSENVSTTEVADVLGAHPD 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 541 ILECAVLGLPDEAY-GEVICAIIVAKEdvkeraEQASEPALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKK 619
Cdd:cd05937 386 IAEANVYGVKVPGHdGRAGCAAITLEE------SSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKG 459
|
....
gi 2212542879 620 ELKK 623
Cdd:cd05937 460 VLRD 463
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
256-622 |
2.09e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 116.33 E-value: 2.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 256 ALILYTSGTTGKPKGVVH--THKGILSQVQI---LTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVV---EFMP 327
Cdd:PRK13391 157 TDMLYSSGTTGRPKGIKRplPEQPPDTPLPLtafLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIvmeHFDA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 328 KFSVRGVwQRWResypsgvsksndaITVFTGVPTVYTRLLQgydtmNPDEQSAcSYAAKQLRLMMcgSSALPSPL----- 402
Cdd:PRK13391 237 EQYLALI-EEYG-------------VTHTQLVPTMFSRMLK-----LPEEVRD-KYDLSSLEVAI--HAAAPCPPqvkeq 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 403 MKRWeevTGHRLLERYGMTEFVMA--------LSNPlhgprkeGTVGKPL---PRveakIIMDDGTETKAGV-GELCIRS 470
Cdd:PRK13391 295 MIDW---WGPIIHEYYAATEGLGFtacdseewLAHP-------GTVGRAMfgdLH----ILDDDGAELPPGEpGTIWFEG 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 471 PSLFrEYWKRPEVTEES-FIDGGFFKTGDTVTIDEDGYFKILGRTnADIMKVGGYKLSALEIEAVLLEHDTILECAVLGL 549
Cdd:PRK13391 361 GRPF-EYLNDPAKTAEArHPDGTWSTVGDIGYVDEDGYLYLTDRA-AFMIISGGVNIYPQEAENLLITHPKVADAAVFGV 438
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2212542879 550 PDEAYGEVICAIIVAKEDVKERAEQASEpaltlqaLTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:PRK13391 439 PNEDLGEEVKAVVQPVDGVDPGPALAAE-------LIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLR 504
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
141-624 |
2.54e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 118.73 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 141 IGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTK---EHHEIMESISTKCSTGYSLLPSVE 217
Cdd:PRK12467 3148 VGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAhllEQLPAPAGDTALTLDRLDLNGYSE 3227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 218 SIPPKiesqeplsseltssvssllaeidnlkKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQF 297
Cdd:PRK12467 3228 NNPST--------------------------RVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRV 3281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 298 LhclplhhvhglfnaLFAPL-YSGSVVEFMP------KFSVRGVWQRWRESYPSGVSKSNdaITVFTGVPTVYTRLLQgy 370
Cdd:PRK12467 3282 L--------------LFMSFsFDGAQERFLWtlicggCLVVRDNDLWDPEELWQAIHAHR--ISIACFPPAYLQQFAE-- 3343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 371 dtmnpDEQSAcsyAAKQLRLMMCGSSALPSPLMKRWEEVTGHR-LLERYGMTEFVM----------ALSNPLHGPrkegt 439
Cdd:PRK12467 3344 -----DAGGA---DCASLDIYVFGGEAVPPAAFEQVKRKLKPRgLTNGYGPTEAVVtvtlwkcggdAVCEAPYAP----- 3410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 440 VGKPLPRVEAKIIMDDGTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGF-------FKTGDTVTIDEDGYFKIL 511
Cdd:PRK12467 3411 IGRPVAGRSIYVLDGQLNPVPVGVaGELYIGGVGLARGYHQRPSLTAERFVADPFsgsggrlYRTGDLARYRADGVIEYL 3490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 512 GRTNADImKVGGYKLSALEIEAVLLEHDTILECAVLGLpDEAYGEVICAIIVAkedvkeraeqASEPALTLQALTSWSKD 591
Cdd:PRK12467 3491 GRIDHQV-KIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVP----------ADPQGDWRETLRDHLAA 3558
|
490 500 510
....*....|....*....|....*....|...
gi 2212542879 592 KLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKL 624
Cdd:PRK12467 3559 SLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDP 3591
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
250-624 |
6.51e-27 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 116.15 E-value: 6.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 250 IKGDDPALILYTSGTTGKPKGVVHTHKG-ILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVV---EF 325
Cdd:PLN02654 272 VDAEDPLFLLYTSGSTGKPKGVLHTTGGyMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVlvfEG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 326 MPKFSVRG-VWQRwresypsgVSKSNdaITVFTGVPTVYTRLlqgydtMNPDEQSACSYAAKQLRLMmcGSSALP-SPLM 403
Cdd:PLN02654 352 APNYPDSGrCWDI--------VDKYK--VTIFYTAPTLVRSL------MRDGDEYVTRHSRKSLRVL--GSVGEPiNPSA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 404 KRW-EEVTGHR---LLERYGMTEFVMALSNPLHG--PRKEGTVGKPLPRVEAKIIMDDGTETKAGV-GELCIRS--PSLF 474
Cdd:PLN02654 414 WRWfFNVVGDSrcpISDTWWQTETGGFMITPLPGawPQKPGSATFPFFGVQPVIVDEKGKEIEGECsGYLCVKKswPGAF 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 475 REYWKRPEVTEESFID--GGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDE 552
Cdd:PLN02654 494 RTLYGDHERYETTYFKpfAGYYFSGDGCSRDKDGYYWLTGRVD-DVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHE 572
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2212542879 553 AYGEVICAIIVAKEDVKERAEQASEPALTLqaltswsKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKL 624
Cdd:PLN02654 573 VKGQGIYAFVTLVEGVPYSEELRKSLILTV-------RNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKI 637
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
129-587 |
8.23e-27 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 115.21 E-value: 8.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 129 GIDGTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPL-ALSYPEvELLHVMNDSDISMVLSTKEhheimESIStKCS 207
Cdd:cd17641 27 GLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIyQDSMAE-EVAYLLNYTGARVVIAEDE-----EQVD-KLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 208 TGYSLLPSVESI------------PPKIESQEPLSSELTSSVSSLLAEIDN-LKKIKGDDPALILYTSGTTGKPKGVVHT 274
Cdd:cd17641 100 EIADRIPSVRYViycdprgmrkydDPRLISFEDVVALGRALDRRDPGLYEReVAAGKGEDVAVLCTTSGTTGKPKLAMLS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 275 HKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEF-------MPK---------FSVRGVWqrw 338
Cdd:cd17641 180 HGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIVNFpeepetmMEDlreigptfvLLPPRVW--- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 339 rESYPSGV-SKSNDAiTVFT------GVPTVYTRLLQGYDTMNPDEQSACSYA------AKQLRLMMcGSSALPS----- 400
Cdd:cd17641 257 -EGIAADVrARMMDA-TPFKrfmfelGMKLGLRALDRGKRGRPVSLWLRLASWladallFRPLRDRL-GFSRLRSaatgg 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 401 ----PLMKRWEEVTGHRLLERYGMTEFVMALSNPLHGPRKEGTVGKPLPRVEAKIimddgtetkAGVGELCIRSPSLFRE 476
Cdd:cd17641 334 aalgPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI---------DEVGEILVRSPGVFVG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 477 YWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVG-GYKLSALEIEAVLLEHDTILECAVLGLPDEAYG 555
Cdd:cd17641 405 YYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAK-DVGTTSdGTRFSPQFIENKLKFSPYIAEAVVLGAGRPYLT 483
|
490 500 510
....*....|....*....|....*....|..
gi 2212542879 556 EVICaiiVAKEDVKERAEQASEPALTLQALTS 587
Cdd:cd17641 484 AFIC---IDYAIVGKWAEQRGIAFTTYTDLAS 512
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
140-621 |
9.83e-27 |
|
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: 113.65 E-value: 9.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 140 RIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLstkehheimesistkcstgysllpsvesi 219
Cdd:cd17648 40 LVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVI----------------------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 220 ppkiesqeplsseltssvssllAEIDNLkkikgddpALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQflh 299
Cdd:cd17648 91 ----------------------TNSTDL--------AYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGD--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 300 clplHHVHGLFNALFAP--------LYSGSVVeFMPKFSVRGVWQRWresYPSGvskSNDAITVFTGVPTVytrlLQGYD 371
Cdd:cd17648 138 ----EAVLFFSNYVFDFfveqmtlaLLNGQKL-VVPPDEMRFDPDRF---YAYI---NREKVTYLSGTPSV----LQQYD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 372 TmnpdeqSACSYaakqLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEF-VMALSNPLHGP-RKEGTVGKPLPRVEA 449
Cdd:cd17648 203 L------ARLPH----LKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETtVTNHKRFFPGDqRFDKSLGRPVRNTKC 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 450 KIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFIDGGF--------------FKTGDTVTIDEDGYFKILGRT 514
Cdd:cd17648 273 YVLNDAMKRVPVGaVGELYLGGDGVARGYLNRPELTAERFLPNPFqteqerargrnarlYKTGDLVRWLPSGELEYLGRN 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 515 NADImKVGGYKLSALEIEAVLLEHDTILECAVlglpdeaygevicaiiVAKEDVKERAEQ----------ASEPALTLQA 584
Cdd:cd17648 353 DFQV-KIRGQRIEPGEVEAALASYPGVRECAV----------------VAKEDASQAQSRiqkylvgyylPEPGHVPESD 415
|
490 500 510
....*....|....*....|....*....|....*..
gi 2212542879 585 LTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 621
Cdd:cd17648 416 LLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
251-568 |
6.72e-26 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 112.89 E-value: 6.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 251 KGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALfAPLYSGSVVEFmpkfs 330
Cdd:PLN02736 219 KPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQI-VMLHYGVAVGF----- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 331 vrgvwqrwresYPSGVSKSNDAI-----TVFTGVPTVYTRLlqgYD-TMNPDEQS--------ACSYAAKQ--------- 387
Cdd:PLN02736 293 -----------YQGDNLKLMDDLaalrpTIFCSVPRLYNRI---YDgITNAVKESgglkerlfNAAYNAKKqalengknp 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 388 -------------------LRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSNPLHGPRKEGTVGKPLPRVE 448
Cdd:PLN02736 359 spmwdrlvfnkikaklggrVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 449 AKII----MDDGTETKA-GVGELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGG 523
Cdd:PLN02736 439 VKLVdvpeMNYTSEDQPyPRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKK-NIFKLAQ 517
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2212542879 524 YKLSALE-IEAVLLEHDTILECAVLGlpdEAYGEVICAIIVAKEDV 568
Cdd:PLN02736 518 GEYIAPEkIENVYAKCKFVAQCFVYG---DSLNSSLVAVVVVDPEV 560
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
137-621 |
2.14e-25 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 110.48 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 137 RGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLstkehheimesISTKCSTGYSLLPSV 216
Cdd:PRK05857 65 RGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAAL-----------VAPGSKMASSAVPEA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 217 ESIPPKIEsqepLSSELTSSVSSLLAEIDNLKKIKG---DDPALILYTSGTTGKPKGVVHTHKGILSQVQILTE---AW- 289
Cdd:PRK05857 134 LHSIPVIA----VDIAAVTRESEHSLDAASLAGNADqgsEDPLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKeglNWv 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 290 GYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPK-FSVRGVWqrwresypsgvskSNDAITVFTGVPTVYTRL-- 366
Cdd:PRK05857 210 TWVVGETTYSPLPATHIGGLWWILTCLMHGGLCVTGGENtTSLLEIL-------------TTNAVATTCLVPTLLSKLvs 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 367 -LQGYDTMNPdeqsacsyaakQLRLMMCGSS-ALPSPLmkRWEEVTGHRLLERYGMTEF-VMALSNPLHGPR----KEGT 439
Cdd:PRK05857 277 eLKSANATVP-----------SLRLVGYGGSrAIAADV--RFIEATGVRTAQVYGLSETgCTALCLPTDDGSivkiEAGA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 440 VGKPLPRVEAKIIMDDG-------TETKAGVGELCIRSPSLFREYWKRPEVTEESFIDgGFFKTGDTVTIDEDGYFKILG 512
Cdd:PRK05857 344 VGRPYPGVDVYLAATDGigptapgAGPSASFGTLWIKSPANMLGYWNNPERTAEVLID-GWVNTGDLLERREDGFFYIKG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 513 RTNADIMKvGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKERAeqASEPALTLQALTSWSKDK 592
Cdd:PRK05857 423 RSSEMIIC-GGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESA--ARALKHTIAARFRRESEP 499
|
490 500
....*....|....*....|....*....
gi 2212542879 593 LAPykiPTRLYLWDSLPRNAMGKVNKKEL 621
Cdd:PRK05857 500 MAR---PSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
249-505 |
3.52e-25 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 110.35 E-value: 3.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 249 KIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQ--FLHCLPLHHVHG---LFNALfapLYSGS-- 321
Cdd:PRK08180 205 AVGPDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPpvLVDWLPWNHTFGgnhNLGIV---LYNGGtl 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 322 -------VVEFMPKfSVRGVwqrwRESYPsgvsksndaiTVFTGVPTVYTRLLqgyDTMNPDEQSACSYAAKqLRLMMCG 394
Cdd:PRK08180 282 yiddgkpTPGGFDE-TLRNL----REISP----------TVYFNVPKGWEMLV---PALERDAALRRRFFSR-LKLLFYA 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 395 SSALPSPLMKRWEEV----TGHR--LLERYGMTE---FVMALSNPLHGPrkeGTVGKPLPRVEAKIIMDDGtetKAgvgE 465
Cdd:PRK08180 343 GAALSQDVWDRLDRVaeatCGERirMMTGLGMTEtapSATFTTGPLSRA---GNIGLPAPGCEVKLVPVGG---KL---E 413
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2212542879 466 LCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVT-IDED 505
Cdd:PRK08180 414 VRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRfVDPA 454
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
253-563 |
1.31e-24 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 108.06 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPlhhvhgLFnALFAP-LYSGSVVEFM----- 326
Cdd:PRK09274 174 DDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFP------LF-ALFGPaLGMTSVIPDMdptrp 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 327 ----PKFSVRGVwQRWresypsgvsksndAITVFTGVPTVYTRLLQgydtmnpdeqsACSYAAKQL----RLMMCGSSAl 398
Cdd:PRK09274 247 atvdPAKLFAAI-ERY-------------GVTNLFGSPALLERLGR-----------YGEANGIKLpslrRVISAGAPV- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 399 PSPLMKRWEEVTGH--RLLERYGMTE----FVMALSNPLHGPRK-----EGT-VGKPLPRVEAKII---------MDDGT 457
Cdd:PRK09274 301 PIAVIERFRAMLPPdaEILTPYGATEalpiSSIESREILFATRAatdngAGIcVGRPVDGVEVRIIaisdapipeWDDAL 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 458 ETKAG-VGELCIRSPSLFREYWKRPEVTEESFI---DGGFF-KTGDTVTIDEDGYFKILGRTnADIMKVGGYKLSALEIE 532
Cdd:PRK09274 381 RLATGeIGEIVVAGPMVTRSYYNRPEATRLAKIpdgQGDVWhRMGDLGYLDAQGRLWFCGRK-AHRVETAGGTLYTIPCE 459
|
330 340 350
....*....|....*....|....*....|.
gi 2212542879 533 AVLLEHDTILECAVLGLPDEayGEVICAIIV 563
Cdd:PRK09274 460 RIFNTHPGVKRSALVGVGVP--GAQRPVLCV 488
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
138-615 |
1.40e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 108.05 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 138 GARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLstkeHHEimesistkcstgySLLPSVE 217
Cdd:PRK07798 53 GDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALV----YER-------------EFAPRVA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 218 SIPPKI--------------ESQEPLSSELTSSVSSLLAEIDNLKKiKGDDpALILYTSGTTGKPKGVVHTHKGI----L 279
Cdd:PRK07798 116 EVLPRLpklrtlvvvedgsgNDLLPGAVDYEDALAAGSPERDFGER-SPDD-LYLLYTGGTTGMPKGVMWRQEDIfrvlL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 280 SQVQILTeawGYQSEDQFLH--------------CLPLHHVHGLFNAlFAPLYSGSVVEFMP--KFSVRGVWQ---RWRe 340
Cdd:PRK07798 194 GGRDFAT---GEPIEDEEELakraaagpgmrrfpAPPLMHGAGQWAA-FAALFSGQTVVLLPdvRFDADEVWRtieREK- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 341 sypsgvsksndaITVFTGVPTVYTR-LLQGYDTMNPdeqsacsYAAKQLRLMmcGSSALP-SPLMK-RWEEVTGHR-LLE 416
Cdd:PRK07798 269 ------------VNVITIVGDAMARpLLDALEARGP-------YDLSSLFAI--ASGGALfSPSVKeALLELLPNVvLTD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 417 RYGMTEF-VMALSNPLHGPRKEGTvgkplPRVEA----KIIMDDGTETKAGVGELCI--RSPSLFREYWKRPEVTEESF- 488
Cdd:PRK07798 328 SIGSSETgFGGSGTVAKGAVHTGG-----PRFTIgprtVVLDEDGNPVEPGSGEIGWiaRRGHIPLGYYKDPEKTAETFp 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 489 -IDGGFFK-TGDTVTIDEDGYFKILGRTNADImKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKE 566
Cdd:PRK07798 403 tIDGVRYAiPGDRARVEADGTITLLGRGSVCI-NTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLRE 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2212542879 567 DVkeraeqasepALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGK 615
Cdd:PRK07798 482 GA----------RPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
137-599 |
3.00e-24 |
|
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: 107.16 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 137 RGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKCSTGYSLL--- 213
Cdd:cd17632 92 PGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAEHLDLAVEAVLEGGTPPRLVvfd 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 214 --PSVESIPPKIESQEPLSSELTSSVSSLLAEIDNLKKIK---------GDDP-ALILYTSGTTGKPKGVVHTHkgilsq 281
Cdd:cd17632 172 hrPEVDAHRAALESARERLAAVGIPVTTLTLIAVRGRDLPpaplfrpepDDDPlALLIYTSGSTGTPKGAMYTE------ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 282 vQILTEAW--------GYQSEDQFLHCLPLHHVHGLfNALFAPLYSGSVVEFMPKFSVRGVWQRWRESYPsgvsksndai 353
Cdd:cd17632 246 -RLVATFWlkvssiqdIRPPASITLNFMPMSHIAGR-ISLYGTLARGGTAYFAAASDMSTLFDDLALVRP---------- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 354 TVFTGVPTVYTRLLQGY-------DTMNPDEQSACSYAAKQLR---------LMMCGSSALpSPLMKRW-EEVTGHRLLE 416
Cdd:cd17632 314 TELFLVPRVCDMLFQRYqaeldrrSVAGADAETLAERVKAELRervlggrllAAVCGSAPL-SAEMKAFmESLLDLDLHD 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 417 RYGMTEFVMALSNplhgprkeGTVGKPlPRVEAKII--MDDG---TETKAGVGELCIRSPSLFREYWKRPEVTEESFIDG 491
Cdd:cd17632 393 GYGSTEAGAVILD--------GVIVRP-PVLDYKLVdvPELGyfrTDRPHPRGELLVKTDTLFPGYYKRPEVTAEVFDED 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 492 GFFKTGDTVTIDEDGYFKILGRTNADImkvggyKLSALE------IEAVLLEHDTILECAVLGLPDEAYgevICAIIVAK 565
Cdd:cd17632 464 GFYRTGDVMAELGPDRLVYVDRRNNVL------KLSQGEfvtvarLEAVFAASPLVRQIFVYGNSERAY---LLAVVVPT 534
|
490 500 510
....*....|....*....|....*....|....*
gi 2212542879 566 EDVKERAEQASEPALTLQALTSWSKDK-LAPYKIP 599
Cdd:cd17632 535 QDALAGEDTARLRAALAESLQRIAREAgLQSYEIP 569
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
141-621 |
3.91e-24 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 105.63 E-value: 3.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 141 IGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEhheimesistKCSTGYSLLPSVESIp 220
Cdd:cd17654 44 IGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNKE----------LDNAPLSFTPEHRHF- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 221 pKIESQEPLsseltssvssllaeidnlkkikgddpALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHC 300
Cdd:cd17654 113 -NIRTDECL--------------------------AYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 301 LPLHhvhglfnalFAPlysgSVVEFMPKFSVRGVWQRWRESYPSGVSKSNDA------ITVFTGVPTVYTRLLqgydtmN 374
Cdd:cd17654 166 SPLT---------FDP----SVVEIFLSLSSGATLLIVPTSVKVLPSKLADIlfkrhrITVLQATPTLFRRFG------S 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 375 PDEQSACSYAAKQLRLMMCGSSALPS-PLMKRW-EEVTGHRLLERYGMTEfVMALSNPLHGPRKEGTVGKPLPRVEAKII 452
Cdd:cd17654 227 QSIKSTVLSATSSLRVLALGGEPFPSlVILSSWrGKGNRTRIFNIYGITE-VSCWALAYKVPEEDSPVQLGSPLLGTVIE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 453 MDDgTETKAGVGELCIRspSLFREYWKRPEVTEesfIDGGFFKTGDTVTIdEDGYFKILGRTNADImKVGGYKLSALEIE 532
Cdd:cd17654 306 VRD-QNGSEGTGQVFLG--GLNRVCILDDEVTV---PKGTMRATGDFVTV-KDGELFFLGRKDSQI-KRRGKRINLDLIQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 533 AVLLEHDTILECAVLGLPDEAygevICAIIVAKEdVKERAEQasepalTLQaltswsKDKLAPYKIPTRLYLWDSLPRNA 612
Cdd:cd17654 378 QVIESCLGVESCAVTLSDQQR----LIAFIVGES-SSSRIHK------ELQ------LTLLSSHAIPDTFVQIDKLPLTS 440
|
....*....
gi 2212542879 613 MGKVNKKEL 621
Cdd:cd17654 441 HGKVDKSEL 449
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
134-621 |
7.93e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 105.46 E-value: 7.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTkehHEIMESIStkcSTGysll 213
Cdd:PRK13383 81 GVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVAD---NEFAERIA---GAD---- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 214 PSVESIPPKIESQEplsseltssvssllaeiDNLKKIKGDDPA-LILYTSGTTGKPKGVVHTHK---GILSQVQILtEAW 289
Cdd:PRK13383 151 DAVAVIDPATAGAE-----------------ESGGRPAVAAPGrIVLLTSGTTGKPKGVPRAPQlrsAVGVWVTIL-DRT 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 290 GYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEfmpkfsvrgvwQRWRESYPSGVSKSNDAITVFTGVPTVYTRLLQg 369
Cdd:PRK13383 213 RLRTGSRISVAMPMFHGLGLGMLMLTIALGGTVLT-----------HRHFDAEAALAQASLHRADAFTAVPVVLARILE- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 370 ydtmNPDEQSACSyAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEF-VMALSNPLHGPRKEGTVGKPLPRVE 448
Cdd:PRK13383 281 ----LPPRVRARN-PLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVgIGALATPADLRDAPETVGKPVAGCP 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 449 AKIIMDDGTEtkagVGelcirsPSLFREYWKRPEVTEESFIDGG-------FFKTGDTVTIDEDGYFKILGRTNaDIMKV 521
Cdd:PRK13383 356 VRILDRNNRP----VG------PRVTGRIFVGGELAGTRYTDGGgkavvdgMTSTGDMGYLDNAGRLFIVGRED-DMIIS 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 522 GGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKERAEQasepaltlqaLTSWSKDKLAPYKIPTR 601
Cdd:PRK13383 425 GGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQ----------LRDYLKDRVSRFEQPRD 494
|
490 500
....*....|....*....|
gi 2212542879 602 LYLWDSLPRNAMGKVNKKEL 621
Cdd:PRK13383 495 INIVSSIPRNPTGKVLRKEL 514
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
138-544 |
1.45e-23 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 105.31 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 138 GARIGIVAKPSAEFVAGIFGTWLSGGVAVPL--ALSYPEVELlhVMNDSDISMVLSTKEHHEIMESISTKCSTGYSLLPS 215
Cdd:PLN02861 102 GDRCGIYGSNCPEWIIAMEACNSQGITYVPLydTLGANAVEF--IINHAEVSIAFVQESKISSILSCLPKCSSNLKTIVS 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 216 VESIPP--KIESQEPLSSELTSSVSSLLAEID-NLKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQV----QILTEA 288
Cdd:PLN02861 180 FGDVSSeqKEEAEELGVSCFSWEEFSLMGSLDcELPPKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVlstdHLLKVT 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 289 -WGYQSEDQFLHCLPLHHVHGLFNALFApLYSGSVVEFMpKFSVRGVWQRWRESYPsgvsksndaiTVFTGVPTVYTRLL 367
Cdd:PLN02861 260 dRVATEEDSYFSYLPLAHVYDQVIETYC-ISKGASIGFW-QGDIRYLMEDVQALKP----------TIFCGVPRVYDRIY 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 368 QG---------------------YDTMN-----PDEQSACSY------AAKQ-----LRLMMCGSSALPSPLMKRWEEVT 410
Cdd:PLN02861 328 TGimqkissggmlrkklfdfaynYKLGNlrkglKQEEASPRLdrlvfdKIKEglggrVRLLLSGAAPLPRHVEEFLRVTS 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 411 GHRLLERYGMTE------------FVMAlsnplhgprkeGTVGKPLPRVEAKI--IMDDGTETKAGV--GELCIRSPSLF 474
Cdd:PLN02861 408 CSVLSQGYGLTEscggcftsianvFSMV-----------GTVGVPMTTIEARLesVPEMGYDALSDVprGEICLRGNTLF 476
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 475 REYWKRPEVTEESFIDgGFFKTGDTVTIDEDGYFKILGRtnadimKVGGYKLSALEIEAVLLEHDTILEC 544
Cdd:PLN02861 477 SGYHKRQDLTEEVLID-GWFHTGDIGEWQPNGAMKIIDR------KKNIFKLSQGEYVAVENLENTYSRC 539
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
252-617 |
1.92e-23 |
|
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: 102.46 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 252 GDDpALILYTSGTTGKPKGVVHTHKGI---------------LSQVQILTEAWGYQSEDQFLHClPLHHVHGLFNALFAP 316
Cdd:cd05924 3 ADD-LYILYTGGTTGMPKGVMWRQEDIfrmlmggadfgtgefTPSEDAHKAAAAAAGTVMFPAP-PLMHGTGSWTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 317 LYSGSVVEFMPKFSVRGVWqrwRESYPSGVsksndaiTVFTGVPTVYTR-LLQGYDTMNPdeqsacsYAAKQLRLMMCGS 395
Cdd:cd05924 81 LGGQTVVLPDDRFDPEEVW---RTIEKHKV-------TSMTIVGDAMARpLIDALRDAGP-------YDLSSLFAISSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 396 SALPSPLMKRWEEVTGHR-LLERYGMTEF-VMALSNPLHGPRKEGTVGKPLPRVeaKIIMDDGTETKAGVGEL--CIRSP 471
Cdd:cd05924 144 ALLSPEVKQGLLELVPNItLVDAFGSSETgFTGSGHSAGSGPETGPFTRANPDT--VVLDDDGRVVPPGSGGVgwIARRG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 472 SLFREYWKRPEVTEESF--IDGGFFK-TGDTVTIDEDGYFKILGRTNADImKVGGYKLSALEIEAVLLEHDTILECAVLG 548
Cdd:cd05924 222 HIPLGYYGDEAKTAETFpeVDGVRYAvPGDRATVEADGTVTLLGRGSVCI-NTGGEKVFPEEVEEALKSHPAVYDVLVVG 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 549 LPDEAYGEVICAIIvakedvkeraeQASEPA-LTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVN 617
Cdd:cd05924 301 RPDERWGQEVVAVV-----------QLREGAgVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
256-622 |
2.10e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 103.94 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 256 ALILYTSGTTGKPKGVVHTHKG-ILSQ-----VQILTEAWGYQSEDQFLHCLPLHHVH-----GLFNALfaplysGSVVE 324
Cdd:PRK13390 151 AVMLYSSGTTGFPKGIQPDLPGrDVDApgdpiVAIARAFYDISESDIYYSSAPIYHAAplrwcSMVHAL------GGTVV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 325 FMPKFSVRGVWqRWRESYpsgvsksndAITVFTGVPTVYTRLLQgydtMNPDEQSacSYAAKQLRLMMCGSSALPSPLMK 404
Cdd:PRK13390 225 LAKRFDAQATL-GHVERY---------RITVTQMVPTMFVRLLK----LDADVRT--RYDVSSLRAVIHAAAPCPVDVKH 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 405 RWEEVTGHRLLERYGMTE-FVMALSNPLHGPRKEGTVGKPLPRvEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPE 482
Cdd:PRK13390 289 AMIDWLGPIVYEYYSSTEaHGMTFIDSPDWLAHPGSVGRSVLG-DLHICDDDGNELPAGrIGTVYFERDRLPFRYLNDPE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 483 VTEESFIDGGFFKT--GDTVTIDEDGYFKILGRTNADIMKvGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICA 560
Cdd:PRK13390 368 KTAAAQHPAHPFWTtvGDLGSVDEDGYLYLADRKSFMIIS-GGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKA 446
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2212542879 561 IIVAKEDVKERAEQASEpaltlqaLTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:PRK13390 447 VIQLVEGIRGSDELARE-------LIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
253-619 |
2.02e-22 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 101.35 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSED--QFLHCLPLHHVHGLFNALFAPLYSGSVVEF----- 325
Cdd:cd05921 165 DTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIddgkp 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 326 MP-KF--SVRGVwqrwRESYPsgvsksndaiTVFTGVPTVYTRLLQgydTMNPDEQSACSYAAKqLRLMMCGSSALPSPL 402
Cdd:cd05921 245 MPgGFeeTLRNL----REISP----------TVYFNVPAGWEMLVA---ALEKDEALRRRFFKR-LKLMFYAGAGLSQDV 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 403 MKRWEEV----TGHR--LLERYGMTEfVMALSNPLHGPR-KEGTVGKPLPRVEAKIIMDDGTEtkagvgELCIRSPSLFR 475
Cdd:cd05921 307 WDRLQALavatVGERipMMAGLGATE-TAPTATFTHWPTeRSGLIGLPAPGTELKLVPSGGKY------EVRVKGPNVTP 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 476 EYWKRPEVTEESFIDGGFFKTGDTVTI-DEDGYFKIL---GRTNADimkvggYKLSALEIEAV-LLEHDTILEC------ 544
Cdd:cd05921 380 GYWRQPELTAQAFDEEGFYCLGDAAKLaDPDDPAKGLvfdGRVAED------FKLASGTWVSVgPLRARAVAACaplvhd 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 545 AVLGLPDEAY-GEVICAIIVAKEDVKERAEQASEPALTLQALTSWSKDKLAPYK--------IPTRLYLWDSLPRNAMGK 615
Cdd:cd05921 454 AVVAGEDRAEvGALVFPDLLACRRLVGLQEASDAEVLRHAKVRAAFRDRLAALNgeatgsssRIARALLLDEPPSIDKGE 533
|
....
gi 2212542879 616 VNKK 619
Cdd:cd05921 534 ITDK 537
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
253-624 |
2.16e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 102.94 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKGIL----SQVQIL--TEA-----WGYQSED----QFLHclplhhvhglfnalfAPL 317
Cdd:PRK05691 3869 DNLAYVIYTSGSTGLPKGVMVEQRGMLnnqlSKVPYLalSEAdviaqTASQSFDisvwQFLA---------------APL 3933
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 318 YsGSVVEFMPKFSVRGvwqrwresyPSGVSKSNDA--ITVFTGVPTVYTRLLQgydtmnPDEQsacsyAAKQLRLMMCGS 395
Cdd:PRK05691 3934 F-GARVEIVPNAIAHD---------PQGLLAHVQAqgITVLESVPSLIQGMLA------EDRQ-----ALDGLRWMLPTG 3992
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 396 SALPSPLMKRWeevtghrlLERYGMTEFVMAlsnplHGPRK------------EGTVGKPLP--------RVeakIIMDD 455
Cdd:PRK05691 3993 EAMPPELARQW--------LQRYPQIGLVNA-----YGPAEcsddvaffrvdlASTRGSYLPigsptdnnRL---YLLDE 4056
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 456 GTE-TKAG-VGELCIRSPSLFREYWKRPEVTEESFIDGGF-------FKTGDTVTIDEDGYFKILGRTNADImKVGGYKL 526
Cdd:PRK05691 4057 ALElVPLGaVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQV-KIRGYRI 4135
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 527 SALEIEAVLLEHDTILECAVlGLPDEAYGEVICAIIVAkedvkerAEQASEPALTLQALTSWSKDKLAPYKIPTRLYLWD 606
Cdd:PRK05691 4136 ELGEIEARLHEQAEVREAAV-AVQEGVNGKHLVGYLVP-------HQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLD 4207
|
410
....*....|....*...
gi 2212542879 607 SLPRNAMGKVNKKELKKL 624
Cdd:PRK05691 4208 RLPLNANGKLDRKALPAL 4225
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
243-623 |
8.82e-22 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 99.20 E-value: 8.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 243 EIDNLKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHhvhglFN----ALFAPLY 318
Cdd:PRK04813 133 PYDFDHAVKGDDNYYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYS-----FDlsvmDLYPTLA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 319 SGSVVEFMPKfsvrGVWQRWRESYPSgVSKSNdaITVFTGVPTVYTRLLqgydtMNPdeqsacSYAAKQL----RLMMCG 394
Cdd:PRK04813 208 SGGTLVALPK----DMTANFKQLFET-LPQLP--INVWVSTPSFADMCL-----LDP------SFNEEHLpnltHFLFCG 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 395 ssalpsplmkrwEEVTgHR----LLER---------YGMTEFVMALS------------NPLhgPrkegtVGKPLPRVEA 449
Cdd:PRK04813 270 ------------EELP-HKtakkLLERfpsatiyntYGPTEATVAVTsieitdemldqyKRL--P-----IGYAKPDSPL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 450 KIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESF--IDG-GFFKTGDTVTIDeDGYFKILGRTNADImKVGGYK 525
Cdd:PRK04813 330 LIIDEEGTKLPDGeQGEIVISGPSVSKGYLNNPEKTAEAFftFDGqPAYHTGDAGYLE-DGLLFYQGRIDFQI-KLNGYR 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 526 LSALEIEAVLLEHDTILECAVLGL-PDEAYGEVICAIIVAKEDVKEraeqasEPALTlQALTSWSKDKLAPYKIPTRlYL 604
Cdd:PRK04813 408 IELEEIEQNLRQSSYVESAVVVPYnKDHKVQYLIAYVVPKEEDFER------EFELT-KAIKKELKERLMEYMIPRK-FI 479
|
410 420
....*....|....*....|
gi 2212542879 605 W-DSLPRNAMGKVNKKELKK 623
Cdd:PRK04813 480 YrDSLPLTPNGKIDRKALIE 499
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
141-532 |
9.45e-22 |
|
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: 99.74 E-value: 9.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 141 IGIVAKPSAEFVAGIFGTWLSGGVAVP-LALSYPEVeLLHVMNDS--DISMVLSTKEHHEIMEsISTKcstgyslLPSVE 217
Cdd:cd05933 36 VGILGFNSPEWFIAAVGAIFAGGIAVGiYTTNSPEA-CQYVAETSeaNILVVENQKQLQKILQ-IQDK-------LPHLK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 218 SIppkIESQEPLSSELT----------SSVSSLLAEIDN-LKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILT 286
Cdd:cd05933 107 AI---IQYKEPLKEKEPnlyswdefmeLGRSIPDEQLDAiISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAAS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 287 EAWGYQSEDQ----FLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRG-VWQRWRESYPsgvsksndaiTVFTGVPT 361
Cdd:cd05933 184 QHMDLRPATVgqesVVSYLPLSHIAAQILDIWLPIKVGGQVYFAQPDALKGtLVKTLREVRP----------TAFMGVPR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 362 VYTRLLqgyDTMNPDEQSACSYAAK------------QLRLMMcGSSalPSPLMKRWEE-------------------VT 410
Cdd:cd05933 254 VWEKIQ---EKMKAVGAKSGTLKRKiaswakgvgletNLKLMG-GES--PSPLFYRLAKklvfkkvrkalgldrcqkfFT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 411 GH----------------RLLERYGMTEFVMA--LSNPlhGPRKEGTVGKPLPRVEAKIIMDDgtetKAGVGELCIRSPS 472
Cdd:cd05933 328 GAapisretlefflslniPIMELYGMSETSGPhtISNP--QAYRLLSCGKALPGCKTKIHNPD----ADGIGEICFWGRH 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 473 LFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNADIMKVGGYKLSALEIE 532
Cdd:cd05933 402 VFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPVPIE 461
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
137-623 |
1.26e-21 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 100.12 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 137 RGARIG---IVAKP-SAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKCSTGYSL 212
Cdd:PRK10252 503 RGVKPGdsvAVALPrSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNA 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 213 LPSVESIPPKIESQePlsseltssvssllaeidnlkkikgDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQ 292
Cdd:PRK10252 583 PLAPQGAAPLQLSQ-P------------------------HHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLT 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 293 SEDQFLHCLPLHhvhglFNA----LFAPLYSGSVVEFMPKFSVRGvwqrwresyPSGVSK--SNDAITVFTGVPTVYTRL 366
Cdd:PRK10252 638 ADDVVLQKTPCS-----FDVsvweFFWPFIAGAKLVMAEPEAHRD---------PLAMQQffAEYGVTTTHFVPSMLAAF 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 367 LQgydtmNPDEQSACSyAAKQLRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTEFVMALSN-PLHGPRKEGTVGKPLP 445
Cdd:PRK10252 704 VA-----SLTPEGARQ-SCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWyPAFGEELAAVRGSSVP 777
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 446 --------RVEakiIMDD-GTETKAGV-GELCIRSPSLFREYWKRPEVTEESFIDGGF------FKTGDTVTIDEDGYFK 509
Cdd:PRK10252 778 igypvwntGLR---ILDArMRPVPPGVaGDLYLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLDDGAVE 854
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 510 ILGRTNaDIMKVGGYKLSALEIEAVLLEhdtilecavlgLPDEAYGEVICAIIVAKEDVKERAEQ-------ASEPALTL 582
Cdd:PRK10252 855 YLGRSD-DQLKIRGQRIELGEIDRAMQA-----------LPDVEQAVTHACVINQAAATGGDARQlvgylvsQSGLPLDT 922
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2212542879 583 QALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKK 623
Cdd:PRK10252 923 SALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPL 963
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
254-623 |
3.02e-21 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 97.50 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 254 DPALILYTSGTTGKPKGVVHTHKGIL---SQVQILTEAWGyQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVefmpkfS 330
Cdd:cd05915 154 AACGMAYTTGTTGLPKGVVYSHRALVlhsLAASLVDGTAL-SEKDVVLPVVPMFHVNAWCLPYAATLVGAKQV------L 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 331 VRGVWQRwrESYPSGVSKSNdaITVFTGVPTVYTRLLQGYDTMNPDeqsacsyAAKQLRLMMCGSSalPSPLMKRWEEVT 410
Cdd:cd05915 227 PGPRLDP--ASLVELFDGEG--VTFTAGVPTVWLALADYLESTGHR-------LKTLRRLVVGGSA--APRSLIARFERM 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 411 GHRLLERYGMTEFVMALSNPLHGPRKEGTVGKPLPRVEAKI----------IMDDGTETKAGVGE----LCIRSPSLFRE 476
Cdd:cd05915 294 GVEVRQGYGLTETSPVVVQNFVKSHLESLSEEEKLTLKAKTglpiplvrlrVADEEGRPVPKDGKalgeVQLKGPWITGG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 477 YWKRPEVTEESFIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGE 556
Cdd:cd05915 374 YYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLK-DLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQE 452
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2212542879 557 VICAIIVAKEdVKERAEQASEpaltlqaltsWSKDKLAPYK-IPTRLYLWDSLPRNAMGKVNKKELKK 623
Cdd:cd05915 453 RPLAVVVPRG-EKPTPEELNE----------HLLKAGFAKWqLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
256-505 |
4.19e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 97.81 E-value: 4.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 256 ALILYTSGTTGKPKGVVHTHKGILSQVQILTeawGYQSED------QFLHCLPLHHVHGlFNALFAP-LYSGSVVEFMPK 328
Cdd:PRK12582 223 AKYLFTSGSTGMPKAVINTQRMMCANIAMQE---QLRPREpdppppVSLDWMPWNHTMG-GNANFNGlLWGGGTLYIDDG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 329 FSVRGVW----QRWRESYPsgvsksndaiTVFTGVPTVYTRLLqgyDTMNPDEQSACSYaAKQLRLMMCGSSALPSPLMK 404
Cdd:PRK12582 299 KPLPGMFeetiRNLREISP----------TVYGNVPAGYAMLA---EAMEKDDALRRSF-FKNLRLMAYGGATLSDDLYE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 405 RWEEV----TGHR--LLERYGMTEFVMALSNPLHGPRKEGTVGKPLPRVEAKIimddgtetkAGVG---ELCIRSPSLFR 475
Cdd:PRK12582 365 RMQALavrtTGHRipFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKL---------APVGdkyEVRVKGPNVTP 435
|
250 260 270
....*....|....*....|....*....|.
gi 2212542879 476 EYWKRPEVTEESFIDGGFFKTGDTVT-IDED 505
Cdd:PRK12582 436 GYHKDPELTAAAFDEEGFYRLGDAARfVDPD 466
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
132-625 |
5.36e-21 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 97.00 E-value: 5.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 132 GTGFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLAL--------SYpeVELLHVM-NDSDISMVLSTKEHHEIMESI 202
Cdd:PRK09192 68 ALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLpmgfggreSY--IAQLRGMlASAQPAAIITPDELLPWVNEA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 203 STKCSTGYSLLPSVESIPPkiesqeplsseltssvssllAEIDNLKKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQV 282
Cdd:PRK09192 146 THGNPLLHVLSHAWFKALP--------------------EADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 283 QILTEAwGYQSE--DQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMP--KFSVRG-VWQRWresypsgVSKSNDAITVft 357
Cdd:PRK09192 206 RAISHD-GLKVRpgDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPtrDFARRPlQWLDL-------ISRNRGTISY-- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 358 gVPTVytrllqGYD--TMNPDEQSACSYAAKQLRLMMCGSSALPSPLMKRWEEVTGHR------LLERYGMTEFVMALS- 428
Cdd:PRK09192 276 -SPPF------GYElcARRVNSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFAPAgfddkaFMPSYGLAEATLAVSf 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 429 ------------------------NPLHGPRKEGTV---GKPLPRVEAKIIMDDGTE-TKAGVGELCIRSPSLFREYWKR 480
Cdd:PRK09192 349 splgsgivveevdrdrleyqgkavAPGAETRRVRTFvncGKALPGHEIEIRNEAGMPlPERVVGHICVRGPSLMSGYFRD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 481 PEVTEESFIDgGFFKTGDtVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTIL--ECAVLGLPDEAyGEVI 558
Cdd:PRK09192 429 EESQDVLAAD-GWLDTGD-LGYLLDGYLYITGRAK-DLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQEN-GEKI 504
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2212542879 559 CAIIVAK-EDVKERAEQASEPALTLQALTSWSKD-KLAPYKiptrlylwdSLPRNAMGKVNKKELKKLL 625
Cdd:PRK09192 505 VLLVQCRiSDEERRGQLIHALAALVRSEFGVEAAvELVPPH---------SLPRTSSGKLSRAKAKKRY 564
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
254-624 |
6.04e-21 |
|
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: 95.88 E-value: 6.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 254 DPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRG 333
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASN 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 334 VWQRWREsypsgvsksNDAiTVFtgvptVYTRLLQGYdTMNpdeQSACSYAAK-QLRlMMCGSSALPSPlmkrWEEVTGH 412
Cdd:cd05940 162 FWDDIRK---------YQA-TIF-----QYIGELCRY-LLN---QPPKPTERKhKVR-MIFGNGLRPDI----WEEFKER 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 413 ----RLLERYGMTEFVMALSNPlhgPRKEGTVGK--PLPRVEAKI------------IMD-DGTETKAGVGE--LCI--- 468
Cdd:cd05940 218 fgvpRIAEFYAATEGNSGFINF---FGKPGAIGRnpSLLRKVAPLalvkydlesgepIRDaEGRCIKVPRGEpgLLIsri 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 469 --RSPslFREYWKrPEVTEES-----FIDG-GFFKTGDTVTIDEDGYFKILGRTnADIMKVGGYKLSALEIEAVLLEHDT 540
Cdd:cd05940 295 npLEP--FDGYTD-PAATEKKilrdvFKKGdAWFNTGDLMRLDGEGFWYFVDRL-GDTFRWKGENVSTTEVAAVLGAFPG 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 541 ILECAVLGLPDE-AYGEVICAIIVAKEdvkeraeqasEPALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKK 619
Cdd:cd05940 371 VEEANVYGVQVPgTDGRAGMAAIVLQP----------NEEFDLSALAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKV 440
|
....*
gi 2212542879 620 ELKKL 624
Cdd:cd05940 441 DLRNE 445
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
255-622 |
4.19e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 93.18 E-value: 4.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 255 PALILYTSGTTGKPKGVVHT----HKGILSQVQILTEAwgyQSEDQFLHClPLHHVHGLFNALFAPLYSGSVVEFM---- 326
Cdd:PRK08308 103 PSLLQYSSGTTGEPKLIRRSwteiDREIEAYNEALNCE---QDETPIVAC-PVTHSYGLICGVLAALTRGSKPVIItnkn 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 327 PKFSVrgvwQRWREsYPSgvsksndaiTVFTGVPTVY---TRLLQGYDTMNpdeqsacsyaakqlRLMMCGSsALPSPLM 403
Cdd:PRK08308 179 PKFAL----NILRN-TPQ---------HILYAVPLMLhilGRLLPGTFQFH--------------AVMTSGT-PLPEAWF 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 404 KRWEEVTGHrLLERYGMTEF-VMALSNPLHGPrkeGTVGKPLPRVEAKIIMDDG--TETKAGVGELCIRspslfreywkr 480
Cdd:PRK08308 230 YKLRERTTY-MMQQYGCSEAgCVSICPDMKSH---LDLGNPLPHVSVSAGSDENapEEIVVKMGDKEIF----------- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 481 pevteesfidggffkTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICA 560
Cdd:PRK08308 295 ---------------TKDLGYKSERGTLHFMGRMD-DVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA 358
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2212542879 561 IIVAkedvkeraeqasEPALTLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELK 622
Cdd:PRK08308 359 KVIS------------HEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
251-549 |
2.29e-18 |
|
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: 88.29 E-value: 2.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 251 KGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHhvhglfnALFAPLYS-GSVVEFM--- 326
Cdd:cd05910 83 KADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLF-------ALFGPALGlTSVIPDMdpt 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 327 ------PKFSVRGVwQRWRESypsgvsksndaiTVFtGVPTVYTRLLQgydtmnpdeqsACSYAAKQL----RLMMCGsS 396
Cdd:cd05910 156 rparadPQKLVGAI-RQYGVS------------IVF-GSPALLERVAR-----------YCAQHGITLpslrRVLSAG-A 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 397 ALPSPLMKRWEEVT--GHRLLERYGMTEF----------VMALSNPLHGPRKEGTVGKPLPRVEAKII---------MDD 455
Cdd:cd05910 210 PVPIALAARLRKMLsdEAEILTPYGATEAlpvssigsreLLATTTAATSGGAGTCVGRPIPGVRVRIIeiddepiaeWDD 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 456 GTETKAG-VGELCIRSPSLFREYWKRPEVTEESFI---DGGFF-KTGDTVTIDEDGYFKILGRTNADIMKVGGyKLSALE 530
Cdd:cd05910 290 TLELPRGeIGEITVTGPTVTPTYVNRPVATALAKIddnSEGFWhRMGDLGYLDDEGRLWFCGRKAHRVITTGG-TLYTEP 368
|
330
....*....|....*....
gi 2212542879 531 IEAVLLEHDTILECAVLGL 549
Cdd:cd05910 369 VERVFNTHPGVRRSALVGV 387
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
252-626 |
3.47e-18 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 87.62 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 252 GDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLfnalfaplysgsvvefmpkfsv 331
Cdd:PRK09029 134 PQRLATMTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVSGQ---------------------- 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 332 rG-VWqRW---------RESYP-----SGVSKSndaitvfTGVPTVYTRLLQgydtmnpdeQSACSYAAKQLRLmmcGSS 396
Cdd:PRK09029 192 -GiVW-RWlyagatlvvRDKQPleqalAGCTHA-------SLVPTQLWRLLD---------NRSEPLSLKAVLL---GGA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 397 ALPSPLMKRWEEvTGHRLLERYGMTEF---VMAlsnplhgprKE----GTVGKPLPRVEAKIIMDdgtetkagvgELCIR 469
Cdd:PRK09029 251 AIPVELTEQAEQ-QGIRCWCGYGLTEMastVCA---------KRadglAGVGSPLPGREVKLVDG----------EIWLR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 470 SPSLFREYWKRPEVTeeSFIDG-GFFKTGDTVTIDeDGYFKILGRtnADIMKV-GGYKLSALEIEAVLLEHDTILECAVL 547
Cdd:PRK09029 311 GASLALGYWRQGQLV--PLVNDeGWFATRDRGEWQ-NGELTILGR--LDNLFFsGGEGIQPEEIERVINQHPLVQQVFVV 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 548 GLPDEAYGEVICAIIVakedvkeraeqaSEPALTLQALTSWSKDKLAPYKIPTRLY-LWDSLPRNAMgKVNKKELKKLLQ 626
Cdd:PRK09029 386 PVADAEFGQRPVAVVE------------SDSEAAVVNLAEWLQDKLARFQQPVAYYlLPPELKNGGI-KISRQALKEWVA 452
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
254-616 |
5.34e-18 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 87.70 E-value: 5.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 254 DPALILYTSGTTGKPKGVV---------------HTHKGILSQVQILTEAWGYqsedqflhclplhhVHGLFNALFAPLY 318
Cdd:PRK10524 234 EPSYILYTSGTTGKPKGVQrdtggyavalatsmdTIFGGKAGETFFCASDIGW--------------VVGHSYIVYAPLL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 319 SG--SVV-EFMPKFSVRGVWQRWRESYpsGVSksndaiTVFTGvPTVyTRLLQGYDTmnpdeqsAC--SYAAKQLRLMMC 393
Cdd:PRK10524 300 AGmaTIMyEGLPTRPDAGIWWRIVEKY--KVN------RMFSA-PTA-IRVLKKQDP-------ALlrKHDLSSLRALFL 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 394 GSSALPSPlMKRW-EEVTGHRLLERYGMTEF---VMALSNPLHG-PRKEGTVGKPLPRVEAKIIMD-DGTETKAGV-GEL 466
Cdd:PRK10524 363 AGEPLDEP-TASWiSEALGVPVIDNYWQTETgwpILAIARGVEDrPTRLGSPGVPMYGYNVKLLNEvTGEPCGPNEkGVL 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 467 CIRSP-------SLFRE-------YWKRpevteesfIDGGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIE 532
Cdd:PRK10524 442 VIEGPlppgcmqTVWGDddrfvktYWSL--------FGRQVYSTFDWGIRDADGYYFILGRTD-DVINVAGHRLGTREIE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 533 AVLLEHDTILECAVLGLPDEAYGEVICAIIVAKeDVKERAEQASEPALTlQALTSWSKDKLAPYKIPTRLYLWDSLPRNA 612
Cdd:PRK10524 513 ESISSHPAVAEVAVVGVKDALKGQVAVAFVVPK-DSDSLADREARLALE-KEIMALVDSQLGAVARPARVWFVSALPKTR 590
|
....
gi 2212542879 613 MGKV 616
Cdd:PRK10524 591 SGKL 594
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
242-626 |
1.97e-17 |
|
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: 85.62 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 242 AEIDNLKKIKgDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGS 321
Cdd:cd05908 96 TEEEVLCELA-DELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 322 VVEFMPK--FSVRGV-W-QRWRESYPSGVSKSNDAitvftgvptvYTRLLqgyDTMNPdeQSACSYAAKQLRLMMCGSSA 397
Cdd:cd05908 175 NQYLMPTrlFIRRPIlWlKKASEHKATIVSSPNFG----------YKYFL---KTLKP--EKANDWDLSSIRMILNGAEP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 398 LPSPLMkrwEEVTGH---------RLLERYGMTEFVMALSNP----------------LHGPRKEGT------------V 440
Cdd:cd05908 240 IDYELC---HEFLDHmskyglkrnAILPVYGLAEASVGASLPkaqspfktitlgrrhvTHGEPEPEVdkkdsecltfveV 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 441 GKPLPRVEAKIIMDDGTETKAG-VGELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIdEDGYFKILGRTNaDIM 519
Cdd:cd05908 317 GKPIDETDIRICDEDNKILPDGyIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFI-RNGRLVITGREK-DII 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 520 KVGGYKLSALEIEAVLLEHDTIL--ECAVLGLPD-EAYGEVICAIIVAKEDVKERAEQASEPALTLQALTSWSKDKLAPY 596
Cdd:cd05908 395 FVNGQNVYPHDIERIAEELEGVElgRVVACGVNNsNTRNEEIFCFIEHRKSEDDFYPLGKKIKKHLNKRGGWQINEVLPI 474
|
410 420 430
....*....|....*....|....*....|
gi 2212542879 597 KIptrlylwdsLPRNAMGKVNKKELKKLLQ 626
Cdd:cd05908 475 RR---------IPKTTSGKVKRYELAQRYQ 495
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
248-599 |
2.15e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 85.70 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 248 KKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMP 327
Cdd:PRK08279 194 SGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 328 KFSVRGVW---QRWResypsgvsksndaITVFtgvptVYT----RLLqgydtMNPDEQSacSYAAKQLRLmMCGSSALPS 400
Cdd:PRK08279 274 KFSASRFWddvRRYR-------------ATAF-----QYIgelcRYL-----LNQPPKP--TDRDHRLRL-MIGNGLRPD 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 401 PlmkrWEEVTG----HRLLERYGMTEFVMALSNPLHgprKEGTVGK-PLPRV------------EAKIIMDDGTETKAGV 463
Cdd:PRK08279 328 I----WDEFQQrfgiPRILEFYAASEGNVGFINVFN---FDGTVGRvPLWLAhpyaivkydvdtGEPVRDADGRCIKVKP 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 464 GE--LCI-----RSPslFREYwKRPEVTEESFIDGGF------FKTGDTVTIDEDGYFKILGRtnadimkVG------GY 524
Cdd:PRK08279 401 GEvgLLIgritdRGP--FDGY-TDPEASEKKILRDVFkkgdawFNTGDLMRDDGFGHAQFVDR-------LGdtfrwkGE 470
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2212542879 525 KLSALEIEAVLLEHDTILECAVLGLP-DEAYGEVICAIIVAKEDvkeraeqasePALTLQALTSWSKDKLAPYKIP 599
Cdd:PRK08279 471 NVATTEVENALSGFPGVEEAVVYGVEvPGTDGRAGMAAIVLADG----------AEFDLAALAAHLYERLPAYAVP 536
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
255-625 |
1.11e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 83.64 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 255 PALILYTSGTTGKPKGVVHTHKGILSQvqiLTEAWGYQSEDQFLHCLPLHH------VHGLFNALFA-----PLYSGSVV 323
Cdd:PTZ00237 256 PLYILYTSGTTGNSKAVVRSNGPHLVG---LKYYWRSIIEKDIPTVVFSHSsigwvsFHGFLYGSLSlgntfVMFEGGII 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 324 EfmPKFSVRGVWqrwresypSGVSKSNdaITVFTGVPTVYTRLLQgydtMNPD-EQSACSYAAKQLRLMMCGSSALPSPL 402
Cdd:PTZ00237 333 K--NKHIEDDLW--------NTIEKHK--VTHTLTLPKTIRYLIK----TDPEaTIIRSKYDLSNLKEIWCGGEVIEESI 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 403 MKRWEEVTGHRLLERYGMTEFVMALSNPLHGPRKE-GTVGKPLPRVEAKIIMDDGTETKAG-VGELCIR---SPSLFREY 477
Cdd:PTZ00237 397 PEYIENKLKIKSSRGYGQTEIGITYLYCYGHINIPyNATGVPSIFIKPSILSEDGKELNVNeIGEVAFKlpmPPSFATTF 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 478 WKRPEVTEESFID-GGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGE 556
Cdd:PTZ00237 477 YKNDEKFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRSD-DQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYN 555
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2212542879 557 VICAIIVAKEDvkeraeqASEPALTLQALTS----WSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKKELKKLL 625
Cdd:PTZ00237 556 VPIGLLVLKQD-------QSNQSIDLNKLKNeinnIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFL 621
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
530-615 |
1.89e-16 |
|
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: 74.12 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 530 EIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKERAEqasepaltlqALTSWSKDKLAPYKIPTRLYLWDSLP 609
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEE----------ELVAHVREELGPYAVPKEVVFVDELP 70
|
....*.
gi 2212542879 610 RNAMGK 615
Cdd:pfam13193 71 KTRSGK 76
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
140-561 |
1.48e-15 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 79.86 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 140 RIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTK---EH-HEI-------------MESI 202
Cdd:PRK06334 69 HIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKqlmQHlAQThgedaeypfsliyMEEV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 203 ST------KCSTGYSLLPSVESIppkiesqeplsseltssvssllAEIDNLKKIKGDDPALILYTSGTTGKPKGVVHTHK 276
Cdd:PRK06334 149 RKelsfweKCRIGIYMSIPFEWL----------------------MRWFGVSDKDPEDVAVILFTSGTEKLPKGVPLTHA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 277 GILSQVQILTEAWGYQSEDQFLHCLPLHHVHGlFN--ALFaPLYSGSVVEFmpkfsvrgvwqRWRESYPSGVSKSNDA-- 352
Cdd:PRK06334 207 NLLANQRACLKFFSPKEDDVMMSFLPPFHAYG-FNscTLF-PLLSGVPVVF-----------AYNPLYPKKIVEMIDEak 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 353 ITVFTGVPTVYTRLLQgydTMNPDEQSACSyaakqLRLMMCGSSALPSPLMKRWEEVTGH-RLLERYGMTEFVMALS-NP 430
Cdd:PRK06334 274 VTFLGSTPVFFDYILK---TAKKQESCLPS-----LRFVVIGGDAFKDSLYQEALKTFPHiQLRQGYGTTECSPVITiNT 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 431 LHGPRKEGTVGKPLPRVEAKIIMDdgtETKAGV-----GELCIRSPSLFREYWKRPEvtEESFID-GG--FFKTGDTVTI 502
Cdd:PRK06334 346 VNSPKHESCVGMPIRGMDVLIVSE---ETKVPVssgetGLVLTRGTSLFSGYLGEDF--GQGFVElGGetWYVTGDLGYV 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2212542879 503 DEDGYFKILGRTnADIMKVGGYKLSALEIEAVLLEHdtilecavLGLPDEAYGE--VICAI 561
Cdd:PRK06334 421 DRHGELFLKGRL-SRFVKIGAEMVSLEALESILMEG--------FGQNAADHAGplVVCGL 472
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
251-571 |
1.83e-15 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 80.06 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 251 KGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSE-----DQFLHCLPLHHVhglFNALFAPLY--SGSVV 323
Cdd:PLN02614 221 KKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAaltvkDVYLSYLPLAHI---FDRVIEECFiqHGAAI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 324 EFMpKFSVRGVWQRWRESYPsgvsksndaiTVFTGVPTVYTRLLQGYDTMNPDE--------QSACSYA----------- 384
Cdd:PLN02614 298 GFW-RGDVKLLIEDLGELKP----------TIFCAVPRVLDRVYSGLQKKLSDGgflkkfvfDSAFSYKfgnmkkgqshv 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 385 -------------AKQ-----LRLMMCGSSALPSPLMKRWEEVTGHRLLERYGMTE-----FVmALSNPLHgprKEGTVG 441
Cdd:PLN02614 367 easplcdklvfnkVKQglggnVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEscagtFV-SLPDELD---MLGTVG 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 442 KPLP----RVEAKIIMDDGTETKAGVGELCIRSPSLFREYWKRPEVTEESFIDgGFFKTGDTVTIDEDGYFKILGRTNaD 517
Cdd:PLN02614 443 PPVPnvdiRLESVPEMEYDALASTPRGEICIRGKTLFSGYYKREDLTKEVLID-GWLHTGDVGEWQPNGSMKIIDRKK-N 520
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2212542879 518 IMKVGGYKLSALE-IEAVLLEHDTILECAVLGLPDEAYgevICAIIVAKEDVKER 571
Cdd:PLN02614 521 IFKLSQGEYVAVEnIENIYGEVQAVDSVWVYGNSFESF---LVAIANPNQQILER 572
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
253-532 |
2.13e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 79.27 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSE-DQFLHCLPLHHVHGLFNALFAPLYSGsvvefmpkfsv 331
Cdd:PRK07768 152 DDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLTVPMYFG----------- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 332 rgvwqrwresypsgvsksNDAITV----FTGVPTVYTRLLQGYD-TMNPDEQSACSYAAKQL--------------RLMM 392
Cdd:PRK07768 221 ------------------AELVKVtpmdFLRDPLLWAELISKYRgTMTAAPNFAYALLARRLrrqakpgafdlsslRFAL 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 393 CGSSALPSPLMKRWEEVtGHR-------LLERYGMTEFVMALSNPLHG--------------------PRKEG------T 439
Cdd:PRK07768 283 NGAEPIDPADVEDLLDA-GARfglrpeaILPAYGMAEATLAVSFSPCGaglvvdevdadllaalrravPATKGntrrlaT 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 440 VGKPLPRVEAKIIMDDGTETKA-GVGELCIRSPSLFREYwkrpeVTEESFI----DGGFFKTGDTVTIDEDGYFKILGRT 514
Cdd:PRK07768 362 LGPPLPGLEVRVVDEDGQVLPPrGVGVIELRGESVTPGY-----LTMDGFIpaqdADGWLDTGDLGYLTEEGEVVVCGRV 436
|
330
....*....|....*...
gi 2212542879 515 NaDIMKVGGYKLSALEIE 532
Cdd:PRK07768 437 K-DVIIMAGRNIYPTDIE 453
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
258-567 |
3.52e-15 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 79.09 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 258 ILYTSGTTGKPKGVVHTHKGILS---QVQILTEAW--GYQSEDQFLHCLPLHHV-------------------HGLFNAL 313
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAVATfvrGVDLFMEQFedKMTHDDVYLSFLPLAHIldrmieeyffrkgasvgyyHGDLNAL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 314 faplySGSVVEFMPKF--SVRGVWQRWRESYPSGVSKSNDAITVFTGVptVYTRLL----QGYdtmnpdEQSACSYAAK- 386
Cdd:PLN02430 305 -----RDDLMELKPTLlaGVPRVFERIHEGIQKALQELNPRRRLIFNA--LYKYKLawmnRGY------SHKKASPMADf 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 387 ------------QLRLMMCGSSALpSPLMKRWEEVTG-HRLLERYGMTEfvmALSNPLHGPRKE----GTVGkpLPRVEA 449
Cdd:PLN02430 372 lafrkvkaklggRLRLLISGGAPL-STEIEEFLRVTScAFVVQGYGLTE---TLGPTTLGFPDEmcmlGTVG--APAVYN 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 450 KIIMDDGTET------KAGVGELCIRSPSLFREYWKRPEVTEESFIDgGFFKTGDTVTIDEDGYFKILGRTNaDIMKVGG 523
Cdd:PLN02430 446 ELRLEEVPEMgydplgEPPRGEICVRGKCLFSGYYKNPELTEEVMKD-GWFHTGDIGEILPNGVLKIIDRKK-NLIKLSQ 523
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2212542879 524 YKLSALE-IEAVLLEHDTILECAVLGlpdEAYGEVICAIIVAKED 567
Cdd:PLN02430 524 GEYVALEyLENVYGQNPIVEDIWVYG---DSFKSMLVAVVVPNEE 565
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
243-548 |
7.51e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 78.22 E-value: 7.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 243 EIDNLKK-------IKGDDP---ALILYTSGTTGKPKGVVHTHKGILSQV------QILTEawgyQSEDQFLHCLPLHHV 306
Cdd:PTZ00342 284 LFDDMTKnkttnykIQNEDPdfiTSIVYTSGTSGKPKGVMLSNKNLYNTVvplckhSIFKK----YNPKTHLSYLPISHI 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 307 HGLFNALFAPLYSGSVvefmpkfsvrGVWQRWRESYPSGVSKSNDAITVftGVPTVYTRLlqgYDT-MNpdEQSACSYAA 385
Cdd:PTZ00342 360 YERVIAYLSFMLGGTI----------NIWSKDINYFSKDIYNSKGNILA--GVPKVFNRI---YTNiMT--EINNLPPLK 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 386 KQL--RLMMCGSSALPSPLMKRWEEVTGHR-------------------------------LL-----ERYGMTEfvmaL 427
Cdd:PTZ00342 423 RFLvkKILSLRKSNNNGGFSKFLEGITHISskikdkvnpnlevilngggklspkiaeelsvLLnvnyyQGYGLTE----T 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 428 SNPLHGPRKEGT----VGKPL-PRVEAKIIMDDGTETKAGV--GELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTV 500
Cdd:PTZ00342 499 TGPIFVQHADDNntesIGGPIsPNTKYKVRTWETYKATDTLpkGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIV 578
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2212542879 501 TIDEDGYFKILGRTNadimkvGGYKLSALE-IEAVLL-----EHDTILECAVLG 548
Cdd:PTZ00342 579 QINKNGSLTFLDRSK------GLVKLSQGEyIETDMLnnlysQISFINFCVVYG 626
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
137-585 |
1.13e-13 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 74.01 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 137 RGARIGIVAKPSAEFVAGIFGTWLSGGVAVPL-ALSYP-EVELLH-VMNDSDISMVLSTKEHHEIMESISTKCST-GYSL 212
Cdd:PRK12476 91 PGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPgHAERLDtALRDAEPTVVLTTTAAAEAVEGFLRNLPRlRRPR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 213 LPSVESIPPKI-ESQEPlsseltssvssllAEIDNlkkikgDDPALILYTSGTTGKPKGVVHTHKGILSQ-VQILTEAWG 290
Cdd:PRK12476 171 VIAIDAIPDSAgESFVP-------------VELDT------DDVSHLQYTSGSTRPPVGVEITHRAVGTNlVQMILSIDL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 291 YQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGVwQRWRESYPSGVSKSNdaitVFTGVPTVYTRLLQGY 370
Cdd:PRK12476 232 LDRNTHGVSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTAFVRRP-QRWIKALSEGSRTGR----VVTAAPNFAYEWAAQR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 371 DTMNPDEQSACSYAAkqlrlMMCGSSALPSPLMKRWEEVTGHRLLER------YGMTE---FVM-----ALSNPLHGPRK 436
Cdd:PRK12476 307 GLPAEGDDIDLSNVV-----LIIGSEPVSIDAVTTFNKAFAPYGLPRtafkpsYGIAEatlFVAtiapdAEPSVVYLDRE 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 437 EGTVGKPLP------------------RVEAKIIMDDGTETKA---GVGELCIRSPSLFREYWKRPEVTEESF------- 488
Cdd:PRK12476 382 QLGAGRAVRvaadapnavahvscgqvaRSQWAVIVDPDTGAELpdgEVGEIWLHGDNIGRGYWGRPEETERTFgaklqsr 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 489 -----------IDGGFFKTGDtVTIDEDGYFKILGRTnADIMKVGGYKLSALEIEAVLLEHDTILE---CAVLGLPDEAY 554
Cdd:PRK12476 462 laegshadgaaDDGTWLRTGD-LGVYLDGELYITGRI-ADLIVIDGRNHYPQDIEATVAEASPMVRrgyVTAFTVPAEDN 539
|
490 500 510
....*....|....*....|....*....|...
gi 2212542879 555 GEVicaIIVAkedvkERAEQAS--EPALTLQAL 585
Cdd:PRK12476 540 ERL---VIVA-----ERAAGTSraDPAPAIDAI 564
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
253-626 |
5.29e-13 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 71.92 E-value: 5.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKGILsqVQILTEawgyqsedQFLHClPLHHVHGLF----------NALFAPLYSG-S 321
Cdd:cd05943 249 DHPLYILYSSGTTGLPKCIVHGAGGTL--LQHLKE--------HILHC-DLRPGDRLFyyttcgwmmwNWLVSGLAVGaT 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 322 VV-----EFMPKFSVrgvwqRWRESYPSGvsksndaITVFTGVPTVYTRLLQGYdtMNPDEqsacSYAAKQLRLMMCGSS 396
Cdd:cd05943 318 IVlydgsPFYPDTNA-----LWDLADEEG-------ITVFGTSAKYLDALEKAG--LKPAE----THDLSSLRTILSTGS 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 397 ALPsPLMKRW--EEVTGHRLLERY-GMTEFV--MALSNPLHgPRKEGTVGKPLPRVEAKIIMDDGTETKAGVGELCIRS- 470
Cdd:cd05943 380 PLK-PESFDYvyDHIKPDVLLASIsGGTDIIscFVGGNPLL-PVYRGEIQCRGLGMAVEAFDEEGKPVWGEKGELVCTKp 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 471 -PSLFREYWKRPEVT--EESFID--GGFFKTGDTVTIDEDGYFKILGRTNADImKVGGYKLSALEIEAVLLEHDTILECA 545
Cdd:cd05943 458 fPSMPVGFWNDPDGSryRAAYFAkyPGVWAHGDWIEITPRGGVVILGRSDGTL-NPGGVRIGTAEIYRVVEKIPEVEDSL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 546 VLGLPDEAYGE-VICAiivakedVKERAEQASEPALtLQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKvnKKEL--K 622
Cdd:cd05943 537 VVGQEWKDGDErVILF-------VKLREGVELDDEL-RKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK--KVEVavK 606
|
....
gi 2212542879 623 KLLQ 626
Cdd:cd05943 607 KIIA 610
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
147-535 |
1.01e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 71.74 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 147 PSA-EFVAGIFGTWLSGGVAVPlalSYP--------EVELLHVMNDSDISMVLSTKEHHEIMESISTKCSTGYSLLPSVE 217
Cdd:PRK05691 72 PSGpDYVAAFFGCLYAGVIAVP---AYPpesarrhhQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAANAPELLCVD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 218 SIPPKI--ESQEPlsseltssvssllaeidnlkKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWG--YQS 293
Cdd:PRK05691 149 TLDPALaeAWQEP--------------------ALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 294 EDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPK--FSVRGVwqRWRESypsgVSKSNDAItvfTGVPTVYTRL----- 366
Cdd:PRK05691 209 DDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLMSPayFLERPL--RWLEA----ISEYGGTI---SGGPDFAYRLcserv 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 367 ----LQGYDTmnpdeqsacsyaaKQLRLMMCGSSALPSPLMKRWEE------VTGHRLLERYGMTEFVMALSNplhGPRK 436
Cdd:PRK05691 280 sesaLERLDL-------------SRWRVAYSGSEPIRQDSLERFAEkfaacgFDPDSFFASYGLAEATLFVSG---GRRG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 437 EGTvgkPLPRVEAKIIMDDGTETKAG------------------------------VGELCIRSPSLFREYWKRPEVTEE 486
Cdd:PRK05691 344 QGI---PALELDAEALARNRAEPGTGsvlmscgrsqpghavlivdpqslevlgdnrVGEIWASGPSIAHGYWRNPEASAK 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2212542879 487 SFI--DG-GFFKTGDtVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVL 535
Cdd:PRK05691 421 TFVehDGrTWLRTGD-LGFLRDGELFVTGRLK-DMLIVRGHNLYPQDIEKTV 470
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
253-624 |
1.69e-12 |
|
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: 69.76 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVR 332
Cdd:cd05939 104 RDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHSAGGIMGVGQALLHGSTVVIRKKFSAS 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 333 GVWQrwresypsGVSKSNDAITVFTGVPTVYTrLLQGYdtmNPDEQSACsyaakqLRLMMcGSSALPSPlmkrWEEVTGH 412
Cdd:cd05939 184 NFWD--------DCVKYNCTIVQYIGEICRYL-LAQPP---SEEEQKHN------VRLAV-GNGLRPQI----WEQFVRR 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 413 ----RLLERYGMTEFVMALSNplhgprKEGTVGKP--LPRVEAKI-------IMDDGTETKAGVGELCIR----SPSLF- 474
Cdd:cd05939 241 fgipQIGEFYGATEGNSSLVN------IDNHVGACgfNSRILPSVypirlikVDEDTGELIRDSDGLCIPcqpgEPGLLv 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 475 -REYWKRPEVTEESFIDGG----------------FFKTGDTVTIDEDGYFKILGRTnADIMKVGGYKLSALEIEAVLLE 537
Cdd:cd05939 315 gKIIQNDPLRRFDGYVNEGatnkkiardvfkkgdsAFLSGDVLVMDELGYLYFKDRT-GDTFRWKGENVSTTEVEGILSN 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 538 HDTILECAVLG--LPdEAYGEVICAIIVAKEDvkeraeqASEPALTLQALTSwskdKLAPYKIPTRLYLWDSLPRNAMGK 615
Cdd:cd05939 394 VLGLEDVVVYGveVP-GVEGRAGMAAIVDPER-------KVDLDRFSAVLAK----SLPPYARPQFIRLLPEVDKTGTFK 461
|
....*....
gi 2212542879 616 VNKKELKKL 624
Cdd:cd05939 462 LQKTDLQKE 470
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
250-608 |
1.97e-12 |
|
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: 70.01 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 250 IKGDDPALILYTSGTTGKPKGVVHTHKGILsQVQILTEAWGYQSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKF 329
Cdd:cd05938 141 VTIKSPALYIYTSGTTGLPKAARISHLRVL-QCSGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKF 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 330 SVRGVWQRWResypsgvsKSNdaITVFTgvptvYTRLLQGYDTMNPDEQSACSYAakqLRLMMcGSSALPSPlmkrWEEV 409
Cdd:cd05938 220 SASQFWDDCR--------KHN--VTVIQ-----YIGELLRYLCNQPQSPNDRDHK---VRLAI-GNGLRADV----WREF 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 410 T---GH-RLLERYGMTEFVMALSNPlhgPRKEGTVGK---------PL------PRVEAKIIMDDGTETKAGVGE----L 466
Cdd:cd05938 277 LrrfGPiRIREFYGSTEGNIGFFNY---TGKIGAVGRvsylykllfPFelikfdVEKEEPVRDAQGFCIPVAKGEpgllV 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 467 C-IRSPSLFREYWKRPEVTEES-----FIDGG-FFKTGDTVTIDEDGYFKILGRTnADIMKVGGYKLSALEIEAVLLEHD 539
Cdd:cd05938 354 AkITQQSPFLGYAGDKEQTEKKllrdvFKKGDvYFNTGDLLVQDQQNFLYFHDRV-GDTFRWKGENVATTEVADVLGLLD 432
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 540 TILECAVLGLPDEAY-GEVICAIIVAKEDVkeraeqasepALTLQALTSWSKDKLAPYKIPTRLYLWDSL 608
Cdd:cd05938 433 FLQEVNVYGVTVPGHeGRIGMAAVKLKPGH----------EFDGKKLYQHVREYLPAYARPRFLRIQDSL 492
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
137-513 |
2.76e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 66.29 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 137 RGARIGIVAKPSAEFVAGIFGTWLSGGVAVPL-ALSYP-EVELLH-VMNDSDISMVLSTKEHHE-IMESISTKCSTGYSL 212
Cdd:PRK07769 78 PGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPgHVGRLHaVLDDCTPSAILTTTDSAEgVRKFFRARPAKERPR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 213 LPSVESIPPKI-ESQEPlsseltssvssllAEIDNlkkikgDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGY 291
Cdd:PRK07769 158 VIAVDAVPDEVgATWVP-------------PEANE------DTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 292 QSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMPKFSVRGVWqRW-RESypsgVSKSNDAITVFTGVPTVYTRLLQGY 370
Cdd:PRK07769 219 QEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVRRPG-RWiREL----ARKPGGTGGTFSAAPNFAFEHAAAR 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 371 DTMNPDEQSacsyaakqLRL-----MMCGSSALPSPLMKRWEEVTGHRLLER------YGMTEFVMALSNP--------L 431
Cdd:PRK07769 294 GLPKDGEPP--------LDLsnvkgLLNGSEPVSPASMRKFNEAFAPYGLPPtaikpsYGMAEATLFVSTTpmdeeptvI 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 432 HGPRKEGTVG----------KPLPRVEA--------KIIMD--DGTETKAG-VGELCIRSPSLFREYWKRPEVTEESF-- 488
Cdd:PRK07769 366 YVDRDELNAGrfvevpadapNAVAQVSAgkvgvsewAVIVDpeTASELPDGqIGEIWLHGNNIGTGYWGKPEETAATFqn 445
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2212542879 489 ---------------IDGGFFKTGDT-VTIDEDGYfkILGR 513
Cdd:PRK07769 446 ilksrlseshaegapDDALWVRTGDYgVYFDGELY--ITGR 484
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
134-626 |
5.87e-11 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 65.52 E-value: 5.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 134 GFLRGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLSTKEHHEIMESISTKCSTgyslL 213
Cdd:PLN02387 127 GHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQLKKLIDISSQLET----V 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 214 PSVESIPPKIESQEPLSSELTSSVSSLLAEIDNLKKIKGDDP--------ALILYTSGTTGKPKGVVHTHKGILSQVQ-I 284
Cdd:PLN02387 203 KRVIYMDDEGVDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPdlpspndiAVIMYTSGSTGLPKGVMMTHGNIVATVAgV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 285 LTEAWGYQSEDQFLHCLPLHHVHGLF--NALFA---------PL------------YSGSVVEFMPKF--SVRGVWQRWR 339
Cdd:PLN02387 283 MTVVPKLGKNDVYLAYLPLAHILELAaeSVMAAvgaaigygsPLtltdtsnkikkgTKGDASALKPTLmtAVPAILDRVR 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 340 EsypsGVSKSND-----AITVFTgvpTVYTRLLQ----------GYDTMNPDE---QSACSYAAKQLRLMMCGSSALpSP 401
Cdd:PLN02387 363 D----GVRKKVDakgglAKKLFD---IAYKRRLAaiegswfgawGLEKLLWDAlvfKKIRAVLGGRIRFMLSGGAPL-SG 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 402 LMKRWEEVT-GHRLLERYGMTEFVMALSNPLHGPRKEGTVGKPLPRVEAKII-MDDG----TETKAGVGELCIRSPSLFR 475
Cdd:PLN02387 435 DTQRFINIClGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVsWEEGgyliSDKPMPRGEIVIGGPSVTL 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 476 EYWKRPEVTEESF-IDGG---FFKTGDTVTIDEDGYFKILGRTNaDIMKV--GGYkLSALEIEAVLLEHDTILECAVLGL 549
Cdd:PLN02387 515 GYFKNQEKTDEVYkVDERgmrWFYTGDIGQFHPDGCLEIIDRKK-DIVKLqhGEY-VSLGKVEAALSVSPYVDNIMVHAD 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 550 PDEAYgeviC-AIIVAKEDVKER------------AEQASEPALTLQALTSWSKD----KLAPYKIPTRLYL----WD-- 606
Cdd:PLN02387 593 PFHSY----CvALVVPSQQALEKwakkagidysnfAELCEKEEAVKEVQQSLSKAakaaRLEKFEIPAKIKLlpepWTpe 668
|
570 580
....*....|....*....|....*...
gi 2212542879 607 --------SLPRNAMGKVNKKELKKLLQ 626
Cdd:PLN02387 669 sglvtaalKLKREQIRKKFKDDLKKLYE 696
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
138-587 |
9.22e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 64.58 E-value: 9.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 138 GARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVellH------VMNDSDISMVLSTKEhheIMESIstkcsTGYS 211
Cdd:PRK05850 59 GDRAVILAPQGLEYIVAFLGALQAGLIAVPLSVPQGGA---HdervsaVLRDTSPSVVLTTSA---VVDDV-----TEYV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 212 LLPSVESIPPKIEsqeplsseltssvssllaeIDNL----------KKIKGDDPALILYTSGTTGKPKGVVHTHKGILSQ 281
Cdd:PRK05850 128 APQPGQSAPPVIE-------------------VDLLdldsprgsdaRPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIAN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 282 V-QILTEAWGYQ-----SEDQFLHCLPLHHVHGLFNALFAPLYSG------SVVEFMPKFSvrgvwqRWRESYpsgvsKS 349
Cdd:PRK05850 189 FeQLMSDYFGDTggvppPDTTVVSWLPFYHDMGLVLGVCAPILGGcpavltSPVAFLQRPA------RWMQLL-----AS 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 350 NDAitVFTGVPTVYTRL---------LQGYDTMNpdeqsacsyaakqLRLMMCGSsalpsplmKRWEEVTGHRLLER--- 417
Cdd:PRK05850 258 NPH--AFSAAPNFAFELavrktsdddMAGLDLGG-------------VLGIISGS--------ERVHPATLKRFADRfap 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 418 -----------YGMTE---FVmALSNPLHGP----------------RKEGTVGKPL-----PRVEAKIIMD--DGTETK 460
Cdd:PRK05850 315 fnlretairpsYGLAEatvYV-ATREPGQPPesvrfdyeklsaghakRCETGGGTPLvsygsPRSPTVRIVDpdTCIECP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 461 AG-VGELCIRSPSLFREYWKRPEVTEESF-----------IDGGFFKTGDTVTIDEDGYFkILGRTNaDIMKVGGYKLSA 528
Cdd:PRK05850 394 AGtVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgtPEGPWLRTGDLGFISEGELF-IVGRIK-DLLIVDGRNHYP 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2212542879 529 LEIEAvllehdTILE-----CAVLGLPDEAyGEVICAIIvakeDVKERAEQASEPALTLQALTS 587
Cdd:PRK05850 472 DDIEA------TIQEitggrVAAISVPDDG-TEKLVAII----ELKKRGDSDEEAMDRLRTVKR 524
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
497-627 |
2.74e-08 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 56.75 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 497 GDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVLLEHD-TILECAVLGLPDEAYGEVICAIIVAKEDVKERAEQA 575
Cdd:PLN03051 362 GDIMKRTPGGYFCVQGRAD-DTMNLGGIKTSSVEIERACDRAVaGIAETAAVGVAPPDGGPELLVIFLVLGEEKKGFDQA 440
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2212542879 576 SEPALTlQALTSWSKDKLAPYKIPTRLYLWDSLPRNAMGKVNKK----ELKKLLQV 627
Cdd:PLN03051 441 RPEALQ-KKFQEAIQTNLNPLFKVSRVKIVPELPRNASNKLLRRvlrdQLKKELSG 495
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
137-327 |
5.28e-08 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 55.82 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 137 RGARIGIVAKPSAEFVAGIFGTWLSGGVAVPLALSYPEVELLHVMNDSDISMVLST----KEHHEIMESISTKCSTGYSL 212
Cdd:cd05905 39 PGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALTVeaclKGLPKKLLKSKTAAEIAKKK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 213 LpsvesIPPKIE-SQEPLSSELTSSVSSLLAEIDNlkkikgDDPALILYTSGTTGKPKGVVHTHKGILSQVQILTEAWGY 291
Cdd:cd05905 119 G-----WPKILDfVKIPKSKRSKLKKWGPHPPTRD------GDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACEL 187
|
170 180 190
....*....|....*....|....*....|....*.
gi 2212542879 292 QSEDQFLHCLPLHHVHGLFNALFAPLYSGSVVEFMP 327
Cdd:cd05905 188 YESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIP 223
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
253-279 |
1.98e-07 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 54.03 E-value: 1.98e-07
10 20
....*....|....*....|....*..
gi 2212542879 253 DDPALILYTSGTTGKPKGVVHTHKGIL 279
Cdd:PRK03584 263 DHPLWILYSSGTTGLPKCIVHGHGGIL 289
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
497-626 |
6.34e-06 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 49.31 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 497 GDTVTIDEDGYFKILGRTNaDIMKVGGYKLSALEIEAVL-LEHDTILECAVLGLPDEAYG-EVICAIIVAKEDvkerAEQ 574
Cdd:PLN03052 594 GDIFERTSGGYYRAHGRAD-DTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGpEQLVIAAVLKDP----PGS 668
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2212542879 575 ASEPALTLQALTSWSKDKLAP-YKIpTRLYLWDSLPRNA----MGKVNKKELKKLLQ 626
Cdd:PLN03052 669 NPDLNELKKIFNSAIQKKLNPlFKV-SAVVIVPSFPRTAsnkvMRRVLRQQLAQELS 724
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
463-621 |
1.78e-04 |
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Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 44.43 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 463 VGELCIRSPSLFREYWKRPEVTEESFIDGGFFKTGDTVTIDEDG-------YFKI---------LGR--TNADI------ 518
Cdd:cd17647 315 VGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDHWNYLDKDNnepwrqfWLGPrdrlyrtgdLGRylPNGDCeccgra 394
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2212542879 519 ---MKVGGYKLSALEIEAVLLEHDTILECAVLGLPDEAYGEVICAIIVAKEDVKER---------AEQASEPAL-TLQAL 585
Cdd:cd17647 395 ddqVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDesfaqedvpKEVSTDPIVkGLIGY 474
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170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2212542879 586 TSWSKD-------KLAPYKIPTRLYLWDSLPRNAMGKVNKKEL 621
Cdd:cd17647 475 RKLIKDireflkkRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
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