|
Name |
Accession |
Description |
Interval |
E-value |
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1-373 |
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: 585.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEVWe 80
Cdd:cd05941 93 LILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCPLFAGASVEFLPKFDPKEVA- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 hfLSTDSRSINVFMAVPTIYSKLIDYYESHLAKPgikDFVKAMCQQKIRLMVSGSSALPVPTLERWREITGHTLLERYGM 160
Cdd:cd05941 172 --ISRLMPSITVFMGVPTIYTRLLQYYEAHFTDP---QFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGM 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TEIGMALTNPLNGPRVPGSVGNPFPGVGVRIATEIPQKegssytvhaegdaagtevfPGFEDREGELQVRGPAVFNEYWN 240
Cdd:cd05941 247 TEIGMALSNPLDGERRPGTVGMPLPGVQARIVDEETGE-------------------PLPRGEVGEIQVRGPSVFKEYWN 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 241 KPQETREAFTPDGWFRTGDTAVYK-DNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQRVS 319
Cdd:cd05941 308 KPEATKEEFTDDGWFKTGDLGVVDeDGYYWILGRSSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVV 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2113536441 320 AIVKLRDG-HTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLLA 373
Cdd:cd05941 388 AVVVLRAGaAALSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1-375 |
1.57e-124 |
|
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: 366.44 E-value: 1.57e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEVWE 80
Cdd:COG0318 104 LILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDPERVLE 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 HFlstDSRSINVFMAVPTIYSKLIDYYESHLAkpgikDFvkamcqQKIRLMVSGSSALPVPTLERWREITGHTLLERYGM 160
Cdd:COG0318 184 LI---ERERVTVLFGVPTMLARLLRHPEFARY-----DL------SSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TEIGMALT-NPLN-GPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPAVFNEY 238
Cdd:COG0318 250 TETSPVVTvNPEDpGERRPGSVGRPLPGVEVRIV-----------------DEDGRELPPG---EVGEIVVRGPNVMKGY 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 239 WNKPQETREAFtPDGWFRTGDTAVY-KDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQR 317
Cdd:COG0318 310 WNDPEATAEAF-RDGWLRTGDLGRLdEDGYLYIVGRKK-DMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGER 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2113536441 318 VSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLLALF 375
Cdd:COG0318 388 VVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERY 445
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1-373 |
3.23e-105 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 317.70 E-value: 3.23e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPkevwE 80
Cdd:PRK07787 132 LIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLFHVHGLVLGVLGPLRIGNRFVHTGRPTP----E 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 HFLSTDSRSINVFMAVPTIYSKLIDYYESHLAkpgikdFVKAmcqqkiRLMVSGSSALPVPTLERWREITGHTLLERYGM 160
Cdd:PRK07787 208 AYAQALSEGGTLYFGVPTVWSRIAADPEAARA------LRGA------RLLVSGSAALPVPVFDRLAALTGHRPVERYGM 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TEIGMALTNPLNGPRVPGSVGNPFPGVGVRIATEipqkegssytvhaegdaAGTEVfPGFEDREGELQVRGPAVFNEYWN 240
Cdd:PRK07787 276 TETLITLSTRADGERRPGWVGLPLAGVETRLVDE-----------------DGGPV-PHDGETVGELQVRGPTLFDGYLN 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 241 KPQETREAFTPDGWFRTGDTAVYKDNSYW-ILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQRVS 319
Cdd:PRK07787 338 RPDATAAAFTADGWFRTGDVAVVDPDGMHrIVGRESTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIV 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2113536441 320 AIVKLRDGhtLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLLA 373
Cdd:PRK07787 418 AYVVGADD--VAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1-366 |
1.94e-99 |
|
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: 298.43 E-value: 1.94e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVhGVVNKLLCPLWVGATCVMLPEFSPKEVWE 80
Cdd:cd04433 4 LILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLLPKFDPEAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 HFlstDSRSINVFMAVPTIYSKLIDYYESHLAkpgikDFVKamcqqkIRLMVSGSSALPVPTLERWREITGHTLLERYGM 160
Cdd:cd04433 83 LI---EREKVTILLGVPTLLARLLKAPESAGY-----DLSS------LRALVSGGAPLPPELLERFEEAPGIKLVNGYGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TEIG--MALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGFEdreGELQVRGPAVFNEY 238
Cdd:cd04433 149 TETGgtVATGPPDDDARKPGSVGRPVPGVEVRIV-----------------DPDGGELPPGEI---GELVVRGPSVMKGY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 239 WNKPqETREAFTPDGWFRTGDTAVY-KDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQR 317
Cdd:cd04433 209 WNNP-EATAAVDEDGWYRTGDLGRLdEDGYLYIVGRLK-DMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGER 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2113536441 318 VSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKI 366
Cdd:cd04433 287 VVAVVVLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKI 335
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
2-371 |
2.48e-99 |
|
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: 302.56 E-value: 2.48e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTAlIDEW---SWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEV 78
Cdd:cd05936 130 LQYTSGTTGVPKGAMLTHRNLVANALQ-IKAWledLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIPRFRPIGV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 79 WEHflsTDSRSINVFMAVPTIYSKLIdyyesHLAKPGIKDFvkamcqQKIRLMVSGSSALPVPTLERWREITGHTLLERY 158
Cdd:cd05936 209 LKE---IRKHRVTIFPGVPTMYIALL-----NAPEFKKRDF------SSLRLCISGGAPLPVEVAERFEELTGVPIVEGY 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 159 GMTEIGMALT-NPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPAVFNE 237
Cdd:cd05936 275 GLTETSPVVAvNPLDGPRKPGSIGIPLPGTEVKIV-----------------DDDGEELPPG---EVGELWVRGPQVMKG 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 238 YWNKPQETREAFTpDGWFRTGDTAVY-KDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQ 316
Cdd:cd05936 335 YWNRPEETAEAFV-DGWLRTGDIGYMdEDGYFFIVDRKK-DMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGE 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2113536441 317 RVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd05936 413 AVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
2-371 |
2.43e-97 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 298.71 E-value: 2.43e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEVWEH 81
Cdd:PRK07514 161 ILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIFHTHGLFVATNVALLAGASMIFLPKFDPDAVLAL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 FlstdSRSiNVFMAVPTIYSKLidyyeshLAKPGikdFVKAMCQqKIRLMVSGSSALPVPTLERWREITGHTLLERYGMT 161
Cdd:PRK07514 241 M----PRA-TVMMGVPTFYTRL-------LQEPR---LTREAAA-HMRLFISGSAPLLAETHREFQERTGHAILERYGMT 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 162 EIGMALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaeGDAAGTEVFPGfedrE-GELQVRGPAVFNEYWN 240
Cdd:PRK07514 305 ETNMNTSNPYDGERRAGTVGFPLPGVSLRVT----------------DPETGAELPPG----EiGMIEVKGPNVFKGYWR 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 241 KPQETREAFTPDGWFRTGDTAVYKDNSY-WILGRtSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQRVS 319
Cdd:PRK07514 365 MPEKTAEEFRADGFFITGDLGKIDERGYvHIVGR-GKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVT 443
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2113536441 320 AIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK07514 444 AVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1-368 |
5.79e-88 |
|
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: 272.18 E-value: 5.79e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPkevwE 80
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDP----E 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 HFLSTDSRS-INVFMAVPTIYSKLIDyyeshlaKPGIK--DFvkamcqQKIRLMVSGSSALPVPTLERWREItGHTLLER 157
Cdd:cd17631 178 TVLDLIERHrVTSFFLVPTMIQALLQ-------HPRFAttDL------SSLRAVIYGGAPMPERLLRALQAR-GVKFVQG 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTEIGMALTnpLNGP----RVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPA 233
Cdd:cd17631 244 YGMTETSPGVT--FLSPedhrRKLGSAGRPVFFVEVRIV-----------------DPDGREVPPG---EVGEIVVRGPH 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 234 VFNEYWNKPQETREAFTpDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDS 312
Cdd:cd17631 302 VMAGYWNRPEATAAAFR-DGWFHTGDLGRLDEDGYlYIVDRKK-DMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDE 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2113536441 313 TWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINK 368
Cdd:cd17631 380 KWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
2-371 |
1.29e-85 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 268.98 E-value: 1.29e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHG----VVnkllcPLWVGATCVMLPEFSPKE 77
Cdd:PRK06187 172 MLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAwglpYL-----ALMAGAKQVIPRRFDPEN 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 VWEHFLstDSRsINVFMAVPTIYSKLIDYyeshlAKPGIKDFvkamcqQKIRLMVSGSSALPVPTLERWREITGHTLLER 157
Cdd:PRK06187 247 LLDLIE--TER-VTFFFAVPTIWQMLLKA-----PRAYFVDF------SSLRLVIYGGAALPPALLREFKEKFGIDLVQG 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTEIGMALT-NPLN-----GPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGFEDReGELQVRG 231
Cdd:PRK06187 313 YGMTETSPVVSvLPPEdqlpgQWTKRRSAGRPLPGVEARIV-----------------DDDGDELPPDGGEV-GEIIVRG 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 232 PAVFNEYWNKPQETREAFTpDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAP 310
Cdd:PRK06187 375 PWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYlYITDRIK-DVIISGGENIYPRELEDALYGHPAVAEVAVIGVP 452
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2113536441 311 DSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK06187 453 DEKWGERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1-371 |
4.62e-85 |
|
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: 266.49 E-value: 4.62e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEVWE 80
Cdd:cd05926 153 LILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVVLPPRFSASTFWP 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 HFLSTdsrSINVFMAVPTIYSKLIDYYESHLAKPGIkdfvkamcqqKIRLMVSGSSALPVPTLERWREITGHTLLERYGM 160
Cdd:cd05926 233 DVRDY---NATWYTAVPTIHQILLNRPEPNPESPPP----------KLRFIRSCSASLPPAVLEALEATFGAPVLEAYGM 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TEIGMALT-NPLN-GPRVPGSVGNPFpGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPAVFNEY 238
Cdd:cd05926 300 TEAAHQMTsNPLPpGPRKPGSVGKPV-GVEVRIL-----------------DEDGEILPPG---VVGEICLRGPNVTRGY 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 239 WNKPQETREAFTPDGWFRTGDTAVYKDNSYWIL-GRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQR 317
Cdd:cd05926 359 LNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLtGRIK-ELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEE 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2113536441 318 VSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd05926 438 VAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
2-371 |
2.50e-78 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 249.82 E-value: 2.50e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEVweh 81
Cdd:PRK07656 171 ILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLPVFDPDEV--- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 FLSTDSRSINVFMAVPTIYSKLIDYyeshlakPGIKDFVKAmcqqKIRLMVSGSSALPVPTLERWREITG-HTLLERYGM 160
Cdd:PRK07656 248 FRLIETERITVLPGPPTMYNSLLQH-------PDRSAEDLS----SLRLAVTGAASMPVALLERFESELGvDIVLTGYGL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TE-IGMALTNPLNGPR--VPGSVGNPFPGVGVRIATEIpqkegssytvhaegdaaGTEVFPGfEDreGELQVRGPAVFNE 237
Cdd:PRK07656 317 SEaSGVTTFNRLDDDRktVAGTIGTAIAGVENKIVNEL-----------------GEEVPVG-EV--GELLVRGPNVMKG 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 238 YWNKPQETREAFTPDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQ 316
Cdd:PRK07656 377 YYDDPEATAAAIDADGWLHTGDLGRLDEEGYlYIVDRKK-DMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGE 455
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2113536441 317 RVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK07656 456 VGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1-366 |
3.08e-76 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 245.79 E-value: 3.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHqnlSAMVTALidewSWTksdcILHVLPLHH------------VHGVVNKLLCPLWVGATCV 68
Cdd:COG0365 188 FILYTSGTTGKPKGVVHTH---GGYLVHA----ATT----AKYVLDLKPgdvfwctadigwATGHSYIVYGPLLNGATVV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 69 ML---PEF-SPKEVWE----HflstdsrSINVFMAVPTIYSKLIDYYESHLAKPGIKdfvkamcqqKIRLMVSGSSALPV 140
Cdd:COG0365 257 LYegrPDFpDPGRLWEliekY-------GVTVFFTAPTAIRALMKAGDEPLKKYDLS---------SLRLLGSAGEPLNP 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 141 PTLERWREITGHTLLERYGMTEIGMALTNPLNG-PRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPG 219
Cdd:COG0365 321 EVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGlPVKPGSMGKPVPGYDVAVV-----------------DEDGNPVPPG 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 220 fedREGELQVRG--PAVFNEYWNKPQETREAF--TPDGWFRTGDTAVY-KDNSYWILGRTSvDIIKSGGYKISALEVERH 294
Cdd:COG0365 384 ---EEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRdEDGYFWILGRSD-DVINVSGHRIGTAEIESA 459
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2113536441 295 LLAHPSIADVAVIGAPDSTWGQRVSAIVKLRDGHTLS--LKK-LKEWGRAVMAPYCIPAELIRVEEIPRNQMGKI 366
Cdd:COG0365 460 LVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSdeLAKeLQAHVREELGPYAYPREIEFVDELPKTRSGKI 534
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1-370 |
3.83e-76 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 245.68 E-value: 3.83e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSA---MVTALIDEWSwTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKE 77
Cdd:PRK05605 223 LILYTSGTTGKPKGAQLTHRNLFAnaaQGKAWVPGLG-DGPERVLAALPMFHAYGLTLCLTLAVSIGGELVLLPAPDIDL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 VwehfLSTDSRSINVFM-AVPTIYSKLIDYYESHlakpGIKdfvkamcQQKIRLMVSGSSALPVPTLERWREITGHTLLE 156
Cdd:PRK05605 302 I----LDAMKKHPPTWLpGVPPLYEKIAEAAEER----GVD-------LSGVRNAFSGAMALPVSTVELWEKLTGGLLVE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 157 RYGMTEIG-MALTNPLNGPRVPGSVGNPFPGVGVRIAteipQKEGSSYTVhaegdAAGTEvfpgfedreGELQVRGPAVF 235
Cdd:PRK05605 367 GYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVRIV----DPEDPDETM-----PDGEE---------GELLVRGPQVF 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 236 NEYWNKPQETREAFTpDGWFRTGDTAVYKDNSYW-ILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTW 314
Cdd:PRK05605 429 KGYWNRPEETAKSFL-DGWFRTGDVVVMEEDGFIrIVDRIK-ELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDG 506
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2113536441 315 GQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQ 370
Cdd:PRK05605 507 SEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRRE 562
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1-371 |
4.70e-70 |
|
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: 226.11 E-value: 4.70e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEVWE 80
Cdd:cd05903 97 LLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 hFLSTDSRSInvFMAVPTIYSKLIDyyesHLAKPGikdfvKAMCQqkIRLMVSGSSALPVPTLERWREITGHTLLERYGM 160
Cdd:cd05903 177 -LMREHGVTF--MMGATPFLTDLLN----AVEEAG-----EPLSR--LRTFVCGGATVPRSLARRAAELLGAKVCSAYGS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TEIGMALTNPLNGP--RVPGSVGNPFPGVGVRIateipqkegssytvhaeGDAAGTEVFPGfedREGELQVRGPAVFNEY 238
Cdd:cd05903 243 TECPGAVTSITPAPedRRLYTDGRPLPGVEIKV-----------------VDDTGATLAPG---VEGELLSRGPSVFLGY 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 239 WNKPQETREAFtPDGWFRTGDTAVYKDNSYW-ILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQR 317
Cdd:cd05903 303 LDRPDLTADAA-PEGWFRTGDLARLDEDGYLrITGRSK-DIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGER 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2113536441 318 VSAIVKLRDGHTLSLKKLKEW-GRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd05903 381 ACAVVVTKSGALLTFDELVAYlDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
2-367 |
9.20e-68 |
|
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: 221.70 E-value: 9.20e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMV--TALIDEWSWTKSDCILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSPkevw 79
Cdd:cd05911 151 ILYSSGTTGLPKGVCLSHRNLIANLsqVQTFLYGNDGSNDVILGFLPLYHIYGL-FTTLASLLNGATVIIMPKFDS---- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 80 EHFLSTDSR-SINVFMAVPTIYSKLidyyeshlAKPGIKDFVKAmcqQKIRLMVSGSSALPVPTLERWREITGHT-LLER 157
Cdd:cd05911 226 ELFLDLIEKyKITFLYLVPPIAAAL--------AKSPLLDKYDL---SSLRVILSGGAPLSKELQELLAKRFPNAtIKQG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTEIGMALTNPLNGPRVPGSVGNPFPGVGVRIATEipqkegssytvhAEGDAAGtevfpgfEDREGELQVRGPAVFNE 237
Cdd:cd05911 295 YGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDD------------DGKDSLG-------PNEPGEICVRGPQVMKG 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 238 YWNKPQETREAFTPDGWFRTGDTAVYKDNSYW-ILGRtSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQ 316
Cdd:cd05911 356 YYNNPEATKETFDEDGWLHTGDIGYFDEDGYLyIVDR-KKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGE 434
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2113536441 317 RVSAIVKLRDGHTLSLKKLKEWGRAVMAPY-CIPAELIRVEEIPRNQMGKIN 367
Cdd:cd05911 435 LPRAYVVRKPGEKLTEKEVKDYVAKKVASYkQLRGGVVFVDEIPKSASGKIL 486
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1-371 |
1.30e-67 |
|
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: 219.47 E-value: 1.30e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEVWE 80
Cdd:cd05934 85 SILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLPRFSASRFWS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 HFLSTDSrsiNVFMAVPTIYSKLidyyeshLAKPgikdfvKAMCQQKIRLMVSGSSALPVPTLERWREITGHTLLERYGM 160
Cdd:cd05934 165 DVRRYGA---TVTNYLGAMLSYL-------LAQP------PSPDDRAHRLRAAYGAPNPPELHEEFEERFGVRLLEGYGM 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TEIGMALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVfpgfEDRE-GELQVR---GPAVFN 236
Cdd:cd05934 229 TETIVGVIGPRDEPRRPGSIGRPAPGYEVRIV-----------------DDDGQEL----PAGEpGELVIRglrGWGFFK 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 237 EYWNKPQETREAFtPDGWFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQ 316
Cdd:cd05934 288 GYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGED 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2113536441 317 RVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd05934 367 EVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1-282 |
1.93e-65 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 213.71 E-value: 1.93e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTAL----IDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPK 76
Cdd:pfam00501 159 YIIYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFPAL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 77 EVWEHFLSTDSRSINVFMAVPTIYSKLidyyeshLAKPGIKDFVKAmcqqKIRLMVSGSSALPVPTLERWREITGHTLLE 156
Cdd:pfam00501 239 DPAALLELIERYKVTVLYGVPTLLNML-------LEAGAPKRALLS----SLRLVLSGGAPLPPELARRFRELFGGALVN 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 157 RYGMTEIGMALTNPLNGP---RVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPgfEDREGELQVRGPA 233
Cdd:pfam00501 308 GYGLTETTGVVTTPLPLDedlRSLGSVGRPLPGTEVKIV-----------------DDETGEPVP--PGEPGELCVRGPG 368
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2113536441 234 VFNEYWNKPQETREAFTPDGWFRTGDTAVY-KDNSYWILGRTSvDIIKSG 282
Cdd:pfam00501 369 VMKGYLNDPELTAEAFDEDGWYRTGDLGRRdEDGYLEIVGRKK-DQIKLG 417
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
2-376 |
2.22e-65 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 216.39 E-value: 2.22e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVvnKLLCPLWVGATCVMLPEFSPkevwEH 81
Cdd:PRK06188 173 LAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPTLLRGGTVIVLAKFDP----AE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 FLSTDSRS-INVFMAVPTIYSKLIDYYESHLAkpgikDFvkamcqQKIRLMVSGSSAL-PVptleRWRE---ITGHTLLE 156
Cdd:PRK06188 247 VLRAIEEQrITATFLVPTMIYALLDHPDLRTR-----DL------SSLETVYYGASPMsPV----RLAEaieRFGPIFAQ 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 157 RYGMTEIGMALT------NPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVR 230
Cdd:PRK06188 312 YYGQTEAPMVITylrkrdHDPDDPKRLTSCGRPTPGLRVALL-----------------DEDGREVAQG---EVGEICVR 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 231 GPAVFNEYWNKPQETREAFTpDGWFRTGDTAVYKDNSYW-ILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGA 309
Cdd:PRK06188 372 GPLVMDGYWNRPEETAEAFR-DGWLHTGDVAREDEDGFYyIVDRKK-DMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGV 449
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2113536441 310 PDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLLALFY 376
Cdd:PRK06188 450 PDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYW 516
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
3-372 |
2.64e-65 |
|
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: 215.70 E-value: 2.64e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 3 IYTSGTTGRPKGVLSTHQNLSAM-VTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEF-SPKEV-- 78
Cdd:cd05959 169 LYSSGSTGRPKGVVHLHADIYWTaELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVGATTVLMPERpTPAAVfk 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 79 -WEHFLSTdsrsinVFMAVPTIYSKLidyyeshLAKPGIKDFVkamcQQKIRLMVSGSSALPVPTLERWREITGHTLLER 157
Cdd:cd05959 249 rIRRYRPT------VFFGVPTLYAAM-------LAAPNLPSRD----LSSLRLCVSAGEALPAEVGERWKARFGLDILDG 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTEIG-MALTNpLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPAVFN 236
Cdd:cd05959 312 IGSTEMLhIFLSN-RPGRVRYGTTGKPVPGYEVELR-----------------DEDGGDVADG---EPGELYVRGPSSAT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 237 EYWNKPQETREAFTpDGWFRTGDTAVYKDN-SYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWG 315
Cdd:cd05959 371 MYWNNRDKTRDTFQ-GEWTRTGDKYVRDDDgFYTYAGRAD-DMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGL 448
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 316 QRVSAIVKLRDGHTLSLK---KLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLL 372
Cdd:cd05959 449 TKPKAFVVLRPGYEDSEAleeELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
2-371 |
1.32e-62 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 209.02 E-value: 1.32e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEVWEh 81
Cdd:PRK08316 176 ILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLYHCAQLDVFLGPYLYVGATNVILDAPDPELILR- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 flSTDSRSINVFMAVPTIYSKLidyyeshLAKPgikDFVKA--MCQQKIRLmvsGSSALPVPTLERWRE-ITGHTLLERY 158
Cdd:PRK08316 255 --TIEAERITSFFAPPTVWISL-------LRHP---DFDTRdlSSLRKGYY---GASIMPVEVLKELRErLPGLRFYNCY 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 159 GMTEIG---MALtNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPAVF 235
Cdd:PRK08316 320 GQTEIAplaTVL-GPEEHLRRPGSAGRPVLNVETRVV-----------------DDDGNDVAPG---EVGEIVHRSPQLM 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 236 NEYWNKPQETREAFTpDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTW 314
Cdd:PRK08316 379 LGYWDDPEKTAEAFR-GGWFHSGDLGVMDEEGYiTVVDRKK-DMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKW 456
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2113536441 315 GQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK08316 457 IEAVTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
1-371 |
2.96e-62 |
|
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: 205.65 E-value: 2.96e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHqnlSAMVTALIDEWSWT---KSDCILHVLPLHHVHGVVNKLLCPLWVGATCVM--LPEFSP 75
Cdd:cd05972 85 LIYFTSGTTGLPKGVLHTH---SYPLGHIPTAAYWLglrPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVyeGPRFDA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 76 kEVWEHFLStdSRSINVFMAVPTIYSKLIdyyeshlaKPGIKDFVKAmcqqKIRLMVSGSSALPVPTLERWREITGHTLL 155
Cdd:cd05972 162 -ERILELLE--RYGVTSFCGPPTAYRMLI--------KQDLSSYKFS----HLRLVVSAGEPLNPEVIEWWRAATGLPIR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 156 ERYGMTEIGMALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVR--GPA 233
Cdd:cd05972 227 DGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAII-----------------DDDGRELPPG---EEGDIAIKlpPPG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 234 VFNEYWNKPQETREAFTpDGWFRTGDTAVY-KDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDS 312
Cdd:cd05972 287 LFLGYVGDPEKTEASIR-GDYYLTGDRAYRdEDGYFWFVGRAD-DIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSPDP 364
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2113536441 313 TWGQRVSAIVKLRDGHTLS---LKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd05972 365 VRGEVVKAFVVLTSGYEPSeelAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1-371 |
3.93e-60 |
|
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: 200.01 E-value: 3.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEVWE 80
Cdd:cd05935 88 LIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 HFlstDSRSINVFMAVPTIyskLIDYyeshLAKPGIKDFvkamCQQKIRLMVSGSSALPVPTLERWREITGHTLLERYGM 160
Cdd:cd05935 168 LI---EKYKVTFWTNIPTM---LVDL----LATPEFKTR----DLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TE-IGMALTNPLNGPRVPgSVGNPFPGVGVRIateipqkegssytVHAEgdaAGTEVFPGfedREGELQVRGPAVFNEYW 239
Cdd:cd05935 234 TEtMSQTHTNPPLRPKLQ-CLGIP*FGVDARV-------------IDIE---TGRELPPN---EVGEIVVRGPQIFKGYW 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 240 NKPQETREAFTPDG---WFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQ 316
Cdd:cd05935 294 NRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGE 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2113536441 317 RVSAIVKLRDGH--TLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd05935 374 EVKAFIVLRPEYrgKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
1-371 |
5.20e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 202.50 E-value: 5.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQnlSAMVTALIDE-WS-WTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEfspkev 78
Cdd:PRK08314 194 VLPYTSGTTGVPKGCMHTHR--TVMANAVGSVlWSnSTPESVVLAVLPLFHVTGMVHSMNAPIYAGATVVLMPR------ 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 79 WEHFLSTD--SR-SINVFMAVPTIyskLIDYyeshLAKPGIKDFvkamCQQKIRLMVSGSSALPVPTLERWREITGHTLL 155
Cdd:PRK08314 266 WDREAAARliERyRVTHWTNIPTM---VVDF----LASPGLAER----DLSSLRYIGGGGAAMPEAVAERLKELTGLDYV 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 156 ERYGMTE-IGMALTNPLNGPRvPGSVGNPFPGVGVRIATeiPQkegssytvhaegdaAGTEVFPGfedREGELQVRGPAV 234
Cdd:PRK08314 335 EGYGLTEtMAQTHSNPPDRPK-LQCLGIPTFGVDARVID--PE--------------TLEELPPG---EVGEIVVHGPQV 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 235 FNEYWNKPQETREAF-TPDG--WFRTGDTAVYKDNSYWILgrtsVDIIK----SGGYKISALEVERHLLAHPSIADVAVI 307
Cdd:PRK08314 395 FKGYWNRPEATAEAFiEIDGkrFFRTGDLGRMDEEGYFFI----TDRLKrminASGFKVWPAEVENLLYKHPAIQEACVI 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113536441 308 GAPDSTWGQRVSAIVKLRDGH--TLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK08314 471 ATPDPRRGETVKAVVVLRPEArgKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQL 536
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
2-358 |
3.93e-59 |
|
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: 198.20 E-value: 3.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSpkevweh 81
Cdd:cd05907 92 IIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIYFASSAE------- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 FLSTDSRSI--NVFMAVPTIYSKLIDYYESHLAkPGIKD--FVKAMcQQKIRLMVSGSSALPVPTLERWREItGHTLLER 157
Cdd:cd05907 165 TLLDDLSEVrpTVFLAVPRVWEKVYAAIKVKAV-PGLKRklFDLAV-GGRLRFAASGGAPLPAELLHFFRAL-GIPVYEG 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTEIGMALT-NPLNGPRvPGSVGNPFPGVGVRIAteipqkegssytvhaegdaagtevfpgfEDreGELQVRGPAVFN 236
Cdd:cd05907 242 YGLTETSAVVTlNPPGDNR-IGTVGKPLPGVEVRIA----------------------------DD--GEILVRGPNVML 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 237 EYWNKPQETREAFTPDGWFRTGDTAVYKDNSY-WILGRtSVDIIK-SGGYKISALEVERHLLAHPSIADVAVIGAPDStw 314
Cdd:cd05907 291 GYYKNPEATAEALDADGWLHTGDLGEIDEDGFlHITGR-KKDLIItSGGKNISPEPIENALKASPLISQAVVIGDGRP-- 367
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2113536441 315 gqRVSAIVklrdghTLSLKKLKEWGRAVMAPYCIPAELIRVEEI 358
Cdd:cd05907 368 --FLVALI------VPDPEALEAWAEEHGIAYTDVAELAANPAV 403
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
2-371 |
9.48e-59 |
|
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: 196.03 E-value: 9.48e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSPKEVWEh 81
Cdd:cd05912 82 IMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLCALPLFHISGL-SILMRSVIYGMTVYLVDKFDAEQVLH- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 flSTDSRSINVFMAVPTIYSKLIDYYESHlakpgikdfvkamCQQKIRLMVSGSSALPVPTLERWREiTGHTLLERYGMT 161
Cdd:cd05912 160 --LINSGKVTIISVVPTMLQRLLEILGEG-------------YPNNLRCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMT 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 162 EI-GMALT-NPLNGPRVPGSVGNPFPGVGVRIATEIPQKEGssytvhaegdaagtevfpgfedrEGELQVRGPAVFNEYW 239
Cdd:cd05912 224 ETcSQIVTlSPEDALNKIGSAGKPLFPVELKIEDDGQPPYE-----------------------VGEILLKGPNVTKGYL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 240 NKPQETREAFTpDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQR- 317
Cdd:cd05912 281 NRPDATEESFE-NGWFKTGDIGYLDEEGFlYVLDRRS-DLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVp 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2113536441 318 VSAIVKLRDghtLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd05912 359 VAFVVSERP---ISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
1-368 |
3.72e-58 |
|
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: 192.10 E-value: 3.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSPKEVWE 80
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGL-NLALATFHAGGANVVMEKFDPAEALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 HflsTDSRSINVFMAVPTIYSKLIDyyesHLAKPGIK-DFVKAmcqqkirlmVSGssaLPVP-TLERWREITGHTLLERY 158
Cdd:cd17637 83 L---IEEEKVTLMGSFPPILSNLLD----AAEKSGVDlSSLRH---------VLG---LDAPeTIQRFEETTGATFWSLY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 159 GMTEIGMALTNPLNGPRvPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPAVFNEY 238
Cdd:cd17637 144 GQTETSGLVTLSPYRER-PGSAGRPGPLVRVRIV-----------------DDNDRPVPAG---ETGEIVVRGPLVFQGY 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 239 WNKPQETREAFTpDGWFRTGDTAVYKDNSY-WILGRTSV-DIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQ 316
Cdd:cd17637 203 WNLPELTAYTFR-NGWHHTGDLGRFDEDGYlWYAGRKPEkELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGE 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2113536441 317 RVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINK 368
Cdd:cd17637 282 GIKAVCVLKPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1-371 |
1.00e-57 |
|
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: 195.93 E-value: 1.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQN--LSAMVTALIDEWSWTKSDCILHVLPLHHVH--GVvnkllcP---LWVGATCVML-PE 72
Cdd:cd12119 167 AICYTSGTTGNPKGVVYSHRSlvLHAMAALLTDGLGLSESDVVLPVVPMFHVNawGL------PyaaAMVGAKLVLPgPY 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 73 FSPK---EVWEHFLSTDSrsinvfMAVPTIYSKLIDYYESHLAKpgikdfvkamcQQKIRLMVSGSSALPVPTLERWREI 149
Cdd:cd12119 241 LDPAslaELIEREGVTFA------AGVPTVWQGLLDHLEANGRD-----------LSSLRRVVIGGSAVPRSLIEAFEER 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 150 tGHTLLERYGMTEigmalTNPLNGPRVPGSV----------------GNPFPGVGVRIATEipqkegssytvhaegdaaG 213
Cdd:cd12119 304 -GVRVIHAWGMTE-----TSPLGTVARPPSEhsnlsedeqlalrakqGRPVPGVELRIVDD------------------D 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 214 TEVFP--GFEdrEGELQVRGPAVFNEYWNKPQETrEAFTPDGWFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEV 291
Cdd:cd12119 360 GRELPwdGKA--VGELQVRGPWVTKSYYKNDEES-EALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVEL 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 292 ERHLLAHPSIADVAVIGAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd12119 437 ENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1-371 |
1.08e-56 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 193.73 E-value: 1.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLpefspkEVWE 80
Cdd:PRK13295 201 QLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGFMYGLMMPVMLGATAVLQ------DIWD 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 HFLSTD---SRSINVFMAVPTIYSKLIDYYEsHLAKPgikdfvkamcQQKIRLMVSGSSALPVPTLERWREITGHTLLER 157
Cdd:PRK13295 275 PARAAElirTEGVTFTMASTPFLTDLTRAVK-ESGRP----------VSSLRTFLCAGAPIPGALVERARAALGAKIVSA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTEIGMALTNPLNGP--RVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPAVF 235
Cdd:PRK13295 344 WGMTENGAVTLTKLDDPdeRASTTDGCPLPGVEVRVV-----------------DADGAPLPAG---QIGRLQVRGCSNF 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 236 NEYWNKPQETREAFtpDGWFRTGDTAVYKDNSYW-ILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTW 314
Cdd:PRK13295 404 GGYLKRPQLNGTDA--DGWFDTGDLARIDADGYIrISGRSK-DVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERL 480
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2113536441 315 GQRVSAIVKLRDGHTLSLKKLKEWGRA--VMAPYcIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK13295 481 GERACAFVVPRPGQSLDFEEMVEFLKAqkVAKQY-IPERLVVRDALPRTPSGKIQKFRL 538
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
2-358 |
3.20e-56 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 193.78 E-value: 3.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCpLWVGATCVMLPefSPKEVWEH 81
Cdd:COG1022 188 IIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAHVFERTVSYYA-LAAGATVAFAE--SPDTLAED 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 FlstdsRSI--NVFMAVPTIYSKLidyYESHLAK----PGIK------------DFVKAMCQQK---------------- 127
Cdd:COG1022 265 L-----REVkpTFMLAVPRVWEKV---YAGIQAKaeeaGGLKrklfrwalavgrRYARARLAGKspslllrlkhaladkl 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 128 ------------IRLMVSGSSALPvPTLERWREITGHTLLERYGMTEI-GMALTNPLNGPRvPGSVGNPFPGVGVRIAte 194
Cdd:COG1022 337 vfsklrealggrLRFAVSGGAALG-PELARFFRALGIPVLEGYGLTETsPVITVNRPGDNR-IGTVGPPLPGVEVKIA-- 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 195 ipqkegssytvhaegdaagtevfpgfEDreGELQVRGPAVFNEYWNKPQETREAFTPDGWFRTGDtAVY--KDNSYWILG 272
Cdd:COG1022 413 --------------------------ED--GEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGD-IGEldEDGFLRITG 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 273 RTSvDIIK-SGGYKISALEVERHLLAHPSIADVAVIGApdstwgQR--VSAIVklrdghTLSLKKLKEWGRAVMAPYCIP 349
Cdd:COG1022 464 RKK-DLIVtSGGKNVAPQPIENALKASPLIEQAVVVGD------GRpfLAALI------VPDFEALGEWAEENGLPYTSY 530
|
....*....
gi 2113536441 350 AELIRVEEI 358
Cdd:COG1022 531 AELAQDPEV 539
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
2-371 |
4.72e-55 |
|
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: 186.96 E-value: 4.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNkLLCPLWVGATCVMLPE---FSPKEV 78
Cdd:cd05930 98 VIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWE-IFGALLAGATLVVLPEevrKDPEAL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 79 WEHFLStdsRSINVFMAVPTIYSKLIDYYESHLAKPgikdfvkamcqqkIRLMVSGSSALPVPTLERWREI-TGHTLLER 157
Cdd:cd05930 177 ADLLAE---EGITVLHLTPSLLRLLLQELELAALPS-------------LRLVLVGGEALPPDLVRRWRELlPGARLVNL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTEI-GMALTNPLNGPRVPGS---VGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGFEdreGELQVRGPA 233
Cdd:cd05930 241 YGPTEAtVDATYYRVPPDDEEDGrvpIGRPIPNTRVYVL-----------------DENLRPVPPGVP---GELYIGGAG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 234 VFNEYWNKPQETREAFTPDGWF------RTGDTAVYKDNS---YwiLGRTSvDIIKSGGYKISALEVERHLLAHPSIADV 304
Cdd:cd05930 301 LARGYLNRPELTAERFVPNPFGpgermyRTGDLVRWLPDGnleF--LGRID-DQVKIRGYRIELGEIEAALLAHPGVREA 377
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2113536441 305 AVIGAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd05930 378 AVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
2-371 |
1.06e-54 |
|
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: 187.83 E-value: 1.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEW--SWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEvw 79
Cdd:cd05904 163 LLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEgsNSDSEDVFLCVLPMFHIYGLSSFALGLLRLGATVVVMPRFDLEE-- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 80 ehFLST-DSRSINVFMAVPTIYSKLIDyyeshlaKPGIKDFVKamcqQKIRLMVSGSSALPVPTLERWREITGHT-LLER 157
Cdd:cd05904 241 --LLAAiERYKVTHLPVVPPIVLALVK-------SPIVDKYDL----SSLRQIMSGAAPLGKELIEAFRAKFPNVdLGQG 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTEIGMALT---NPLNGPRVPGSVGNPFPGVGVRIateipqkegssytVHAEgdaAGTEVFPGfedREGELQVRGPAV 234
Cdd:cd05904 308 YGMTESTGVVAmcfAPEKDRAKYGSVGRLVPNVEAKI-------------VDPE---TGESLPPN---QTGELWIRGPSI 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 235 FNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDST 313
Cdd:cd05904 369 MKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYlFIVDRLK-ELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEE 447
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2113536441 314 WGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYcipaELIR----VEEIPRNQMGKINKKQL 371
Cdd:cd05904 448 AGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPY----KKVRkvafVDAIPKSPSGKILRKEL 505
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
4-371 |
2.22e-54 |
|
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: 185.36 E-value: 2.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNLSAMVTALIDEW-SWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEF-SPKEVweh 81
Cdd:cd05919 98 YSSGTTGPPKGVMHAHRDPLLFADAMAREAlGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWpTAERV--- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 fLSTDSR-SINVFMAVPTIYSKLIDyyeshLAKPGIKDFVKamcqqkIRLMVSGSSALPVPTLERWREITGHTLLERYGM 160
Cdd:cd05919 175 -LATLARfRPTVLYGVPTFYANLLD-----SCAGSPDALRS------LRLCVSAGEALPRGLGERWMEHFGGPILDGIGA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TEIGMALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPAVFNEYWN 240
Cdd:cd05919 243 TEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLV-----------------DEEGHTIPPG---EEGDLLVRGPSAAVGYWN 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 241 KPQETREAFTpDGWFRTGDT-AVYKDNSYWILGRtSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQRVS 319
Cdd:cd05919 303 NPEKSRATFN-GGWYRTGDKfCRDADGWYTHAGR-ADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLT 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2113536441 320 AIVKLRDGHTLSLKKLKEWGRAV---MAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd05919 381 AFVVLKSPAAPQESLARDIHRHLlerLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
4-371 |
4.65e-54 |
|
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: 184.60 E-value: 4.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNLSAMVtaliDEWS-----WTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEV 78
Cdd:cd05958 104 FTSGTTGAPKATMHFHRDPLASA----DRYAvnvlrLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPDLL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 79 wehfLSTDSR-SINVFMAVPTIYSKLIdyyeshlakpGIKDFVKAMCQQkIRLMVSGSSALPVPTLERWREITGHTLLER 157
Cdd:cd05958 180 ----LSAIARyKPTVLFTAPTAYRAML----------AHPDAAGPDLSS-LRKCVSAGEALPAALHRAWKEATGIPIIDG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTEIGMALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPAVfne 237
Cdd:cd05958 245 IGSTEMFHIFISARPGDARPGATGKPVPGYEAKVV-----------------DDEGNPVPDG---TIGRLAVRGPTG--- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 238 YWNKPQETREAFTPDGWFRTGDTAVYKDNSY-WILGRtSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQ 316
Cdd:cd05958 302 CRYLADKRQRTYVQGGWNITGDTYSRDPDGYfRHQGR-SDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGV 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2113536441 317 RVSAIVKLRDGHTLS---LKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd05958 381 VVKAFVVLRPGVIPGpvlARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
5-371 |
4.78e-54 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 188.24 E-value: 4.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 5 TSGTTGRPKGVLSTHQNLSA---MVTALIDEwswTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLpefSP------ 75
Cdd:PRK07529 221 TGGTTGMPKLAQHTHGNEVAnawLGALLLGL---GPGDTVFCGLPLFHVNALLVTGLAPLARGAHVVLA---TPqgyrgp 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 76 ---KEVW---EHFlstdsrSINVFMAVPTIYSKLidyyeshLAKPgikdfVKAMCQQKIRLMVSGSSALPVPTLERWREI 149
Cdd:PRK07529 295 gviANFWkivERY------RINFLSGVPTVYAAL-------LQVP-----VDGHDISSLRYALCGAAPLPVEVFRRFEAA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 150 TGHTLLERYGMTEiGMALT--NPLNGPRVPGSVGNPFPGVGVRIATeipqkegssytvhaeGDAAGTEVFPGFEDREGEL 227
Cdd:PRK07529 357 TGVRIVEGYGLTE-ATCVSsvNPPDGERRIGSVGLRLPYQRVRVVI---------------LDDAGRYLRDCAVDEVGVL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 228 QVRGPAVFNEYWNKPQEtREAFTPDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAV 306
Cdd:PRK07529 421 CIAGPNVFSGYLEAAHN-KGLWLEDGWLNTGDLGRIDADGYfWLTGRAK-DLIIRGGHNIDPAAIEEALLRHPAVALAAA 498
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113536441 307 IGAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMA-PYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK07529 499 VGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPAL 564
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1-372 |
1.79e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 185.62 E-value: 1.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMvTALIDEWSWT---KSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKE 77
Cdd:PRK06710 210 LLQYTGGTTGFPKGVMLTHKNLVSN-TLMGVQWLYNckeGEEVVLGVLPFFHVYGMTAVMNLSIMQGYKMVLIPKFDMKM 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 VWEhflSTDSRSINVFMAVPTIYSKLIDyyeshlaKPGIKDFVKAmcqqKIRLMVSGSSALPVPTLERWREITGHTLLER 157
Cdd:PRK06710 289 VFE---AIKKHKVTLFPGAPTIYIALLN-------SPLLKEYDIS----SIRACISGSAPLPVEVQEKFETVTGGKLVEG 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTEIG-MALTNPLNGPRVPGSVGNPFPGVGVRIATEipqkegssytvhaegdAAGTEVFPGfedREGELQVRGPAVFN 236
Cdd:PRK06710 355 YGLTESSpVTHSNFLWEKRVPGSIGVPWPDTEAMIMSL----------------ETGEALPPG---EIGEIVVKGPQIMK 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 237 EYWNKPQETrEAFTPDGWFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQ 316
Cdd:PRK06710 416 GYWNKPEET-AAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGE 494
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2113536441 317 RVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLL 372
Cdd:PRK06710 495 TVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLI 550
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2-371 |
2.02e-53 |
|
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: 180.17 E-value: 2.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNL---SAMVTALIDewsWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVML-PEFSPKE 77
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIvnnGYFIGERLG---LTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPsPSFDPLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 VwehfLSTDSRSINVFM-AVPTIYsklIDyyESHLAKPGIKDFvkamcqQKIRLMVSGSSALPVPTLERWREITGHT-LL 155
Cdd:cd05917 84 V----LEAIEKEKCTALhGVPTMF---IA--ELEHPDFDKFDL------SSLRTGIMAGAPCPPELMKRVIEVMNMKdVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 156 ERYGMTEI--GMALTNPLNGP-RVPGSVGNPFPGVGVRIateipqkegssytVHAEGdaaGTEVFPGfedREGELQVRGP 232
Cdd:cd05917 149 IAYGMTETspVSTQTRTDDSIeKRVNTVGRIMPHTEAKI-------------VDPEG---GIVPPVG---VPGELCIRGY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 233 AVFNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSYW-ILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPD 311
Cdd:cd05917 210 SVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCrIVGRIK-DMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPD 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 312 STWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd05917 289 ERYGEEVCAWIRLKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
2-368 |
3.02e-53 |
|
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: 179.23 E-value: 3.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEVWEh 81
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDAILE- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 flSTDSRSINVFMAVPTIYsklidyyESHLAKPGIKDFVKAmcqqKIRLMVSGSSALPVPTLERWREITG-HTLLERYGM 160
Cdd:cd17638 84 --AIERERITVLPGPPTLF-------QSLLDHPGRKKFDLS----SLRAAVTGAATVPVELVRRMRSELGfETVLTAYGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TEIGMA-LTNPLNGPR-VPGSVGNPFPGVGVRIATEipqkegssytvhaegdaagtevfpgfedreGELQVRGPAVFNEY 238
Cdd:cd17638 151 TEAGVAtMCRPGDDAEtVATTCGRACPGFEVRIADD------------------------------GEVLVRGYNVMQGY 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 239 WNKPQETREAFTPDGWFRTGDTAVYKDNSYW-ILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQR 317
Cdd:cd17638 201 LDDPEATAEAIDADGWLHTGDVGELDERGYLrITDRLK-DMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEV 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2113536441 318 VSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINK 368
Cdd:cd17638 280 GKAFVVARPGVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
5-371 |
5.50e-53 |
|
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: 182.53 E-value: 5.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 5 TSGTTGRPKGVLSTHQNLSAMVTALIdEWSWTKSDCI-LHVLPLHHvhgvvN-KLLCP-----LWVGATCVMLPEFSPKE 77
Cdd:cd05920 147 SGGTTGTPKLIPRTHNDYAYNVRASA-EVCGLDQDTVyLAVLPAAH-----NfPLACPgvlgtLLAGGRVVLAPDPSPDA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 VwehFLSTDSRSINVFMAVPTIYSKLIDYYESHLAKPGikdfvkamcqqKIRLMVSGSSALPVPTLERWREITGHTLLER 157
Cdd:cd05920 221 A---FPLIEREGVTVTALVPALVSLWLDAAASRRADLS-----------SLRLLQVGGARLSPALARRVPPVLGCTLQQV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTEiGMALTNPLNGP--RVPGSVGNPF-PGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPAV 234
Cdd:cd05920 287 FGMAE-GLLNYTRLDDPdeVIIHTQGRPMsPDDEIRVV-----------------DEEGNPVPPG---EEGELLTRGPYT 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 235 FNEYWNKPQETREAFTPDGWFRTGDTA-VYKDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDST 313
Cdd:cd05920 346 IRGYYRAPEHNARAFTPDGFYRTGDLVrRTPDGYLVVEGRIK-DQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDEL 424
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2113536441 314 WGQRVSAIVKLRDG--HTLSLKK-LKEWGravMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd05920 425 LGERSCAFVVLRDPppSAAQLRRfLRERG---LAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
2-374 |
6.35e-53 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 182.47 E-value: 6.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQN--LSAMVTALidEWSWTKSDCILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSPKEVW 79
Cdd:PRK03640 146 IMYTSGTTGKPKGVIQTYGNhwWSAVGSAL--NLGLTEDDCWLAAVPIFHISGL-SILMRSVIYGMRVVLVEKFDAEKIN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 80 EhflSTDSRSINVFMAVPTIYSKLIdyyeshlakpgiKDFVKAMCQQKIRLMVSGSSALPVPTLERWREiTGHTLLERYG 159
Cdd:PRK03640 223 K---LLQTGGVTIISVVSTMLQRLL------------ERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKE-KGIPVYQSYG 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 160 MTE-----IGMALTNPLNgpRVpGSVGNPFPGVGVRIAteipqKEGSsytvhaegdaagtevfPGFEDREGELQVRGPAV 234
Cdd:PRK03640 287 MTEtasqiVTLSPEDALT--KL-GSAGKPLFPCELKIE-----KDGV----------------VVPPFEEGEIVVKGPNV 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 235 FNEYWNKPQETREAFTpDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDST 313
Cdd:PRK03640 343 TKGYLNREDATRETFQ-DGWFKTGDIGYLDEEGFlYVLDRRS-DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDK 420
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2113536441 314 WGQRVSAIVKLrdGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLLAL 374
Cdd:PRK03640 421 WGQVPVAFVVK--SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQL 479
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1-371 |
6.81e-53 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 182.75 E-value: 6.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNL---SAMVTALIDewsWTKSDCILHVLPLHHVHGVvNKLLCPLWVGATCVMLP-EFSPK 76
Cdd:PRK06839 153 IICYTSGTTGKPKGAVLTQENMfwnALNNTFAID---LTMHDRSIVLLPLFHIGGI-GLFAFPTLFAGGVIIVPrKFEPT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 77 EVWEHFlstDSRSINVFMAVPTIYSKLIDyyESHLAKPGIkdfvkamcqQKIRLMVSGSSALPVPTLERWREiTGHTLLE 156
Cdd:PRK06839 229 KALSMI---EKHKVTVVMGVPTIHQALIN--CSKFETTNL---------QSVRWFYNGGAPCPEELMREFID-RGFLFGQ 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 157 RYGMTEigmalTNPL-------NGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQV 229
Cdd:PRK06839 294 GFGMTE-----TSPTvfmlseeDARRKVGSIGKPVLFCDYELI-----------------DENKNKVEVG---EVGELLI 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 230 RGPAVFNEYWNKPQETREAFTpDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIG 308
Cdd:PRK06839 349 RGPNVMKEYWNRPDATEETIQ-DGWLCTGDLARVDEDGFvYIVGRKK-EMIISGGENIYPLEVEQVINKLSDVYEVAVVG 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2113536441 309 APDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK06839 427 RQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
2-371 |
3.21e-52 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 179.57 E-value: 3.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSpkevwEH 81
Cdd:TIGR01923 116 LMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWLLSLPLYHISGL-SILFRWLIEGATLRIVDKFN-----QL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 FLSTDSRSINVFMAVPTIYSKLIDyyESHlakpgikdfvKAMCQQKIRLmvsGSSALPVPTLERWREiTGHTLLERYGMT 161
Cdd:TIGR01923 190 LEMIANERVTHISLVPTQLNRLLD--EGG----------HNENLRKILL---GGSAIPAPLIEEAQQ-YGLPIYLSYGMT 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 162 EigMA---LTNPLNGPRVPGSVGNPFPGVGVRIatEIPQKEGssytvhaegdaagtevfpgfedrEGELQVRGPAVFNEY 238
Cdd:TIGR01923 254 E--TCsqvTTATPEMLHARPDVGRPLAGREIKI--KVDNKEG-----------------------HGEIMVKGANLMKGY 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 239 WNkPQETREAFTPDGWFRTGDTAVYK-DNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQR 317
Cdd:TIGR01923 307 LY-QGELTPAFEQQGWFNTGDIGELDgEGFLYVLGRRD-DLIISGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQV 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2113536441 318 VSAIVKLRDghTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:TIGR01923 385 PVAYIVSES--DISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
4-374 |
4.26e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 177.29 E-value: 4.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLpefSP-------- 75
Cdd:cd05944 9 HTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLFHVNGSVVTLLTPLASGAHVVLA---GPagyrnpgl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 76 -KEVW---EHFLSTdsrsinVFMAVPTIYSKLidyyeshLAKPGIKDFvkamcqQKIRLMVSGSSALPVPTLERWREITG 151
Cdd:cd05944 86 fDNFWklvERYRIT------SLSTVPTVYAAL-------LQVPVNADI------SSLRFAMSGAAPLPVELRARFEDATG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 152 HTLLERYGMTEIGMALT-NPLNGPRVPGSVGNPFPGVGVRIATEipqkegssytvhaegDAAGTEVFPGFEDREGELQVR 230
Cdd:cd05944 147 LPVVEGYGLTEATCLVAvNPPDGPKRPGSVGLRLPYARVRIKVL---------------DGVGRLLRDCAPDEVGEICVA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 231 GPAVFNEYWNKpQETREAFTPDGWFRTGDTAVYKDNSY-WILGRtSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGA 309
Cdd:cd05944 212 GPGVFGGYLYT-EGNKNAFVADGWLNTGDLGRLDADGYlFITGR-AKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQ 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113536441 310 PDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRA-VMAPYCIPAELIRVEEIPRNQMGKINKKQLLAL 374
Cdd:cd05944 290 PDAHAGELPVAYVQLKPGAVVEEEELLAWARDhVPERAAVPKHIEVLEELPVTAVGKVFKPALRAD 355
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
2-375 |
5.84e-52 |
|
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: 175.60 E-value: 5.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCpLWVGATCVMLPEFSPKEVWEH 81
Cdd:cd17630 5 VILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRS-LLAGAELVLLERNQALAEDLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 FLSTDSRSInvfmaVPTIYSKLIDyyeSHLAKPGIKdfvkamcqqKIRLMVSGSSALPVPTLERWREiTGHTLLERYGMT 161
Cdd:cd17630 84 PPGVTHVSL-----VPTQLQRLLD---SGQGPAALK---------SLRAVLLGGAPIPPELLERAAD-RGIPLYTTYGMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 162 EIG-MALTNPLNGPRVpGSVGNPFPGVGVRIATEipqkegssytvhaegdaagtevfpgfedreGELQVRGPAVFNEYWN 240
Cdd:cd17630 146 ETAsQVATKRPDGFGR-GGVGVLLPGRELRIVED------------------------------GEIWVGGASLAMGYLR 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 241 KPqeTREAFTPDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQRVS 319
Cdd:cd17630 195 GQ--LVPEFNEDGWFTTKDLGELHADGRlTVLGRAD-NMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPV 271
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2113536441 320 AIVKLRDGHTLSlkKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLLALF 375
Cdd:cd17630 272 AVIVGRGPADPA--ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAWL 325
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
7-375 |
6.66e-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: 180.73 E-value: 6.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 7 GTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHH--------VHGVvnkllcpLWVGATCVMLPEFSPKEV 78
Cdd:COG1021 194 GTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAALPAAHnfplsspgVLGV-------LYAGGTVVLAPDPSPDTA 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 79 WE----HflstdsrSINVFMAVPTIYSKLIDYYESHLAKPGikdfvkamcqqKIRLMVSGSSALPVPTLERWREITGHTL 154
Cdd:COG1021 267 FPlierE-------RVTVTALVPPLALLWLDAAERSRYDLS-----------SLRVLQVGGAKLSPELARRVRPALGCTL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 155 LERYGMTEiGMALTNPLNGPR--VPGSVGNPF-PGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRG 231
Cdd:COG1021 329 QQVFGMAE-GLVNYTRLDDPEevILTTQGRPIsPDDEVRIV-----------------DEDGNPVPPG---EVGELLTRG 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 232 PAVFNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSY-WILGRtSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGAP 310
Cdd:COG1021 388 PYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYlVVEGR-AKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMP 466
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113536441 311 DSTWGQRVSAIVKLRdGHTLSLKKLKEWGRAV-MAPYCIPAELIRVEEIPRNQMGKINKKQLLALF 375
Cdd:COG1021 467 DEYLGERSCAFVVPR-GEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAAL 531
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
4-371 |
2.91e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 176.39 E-value: 2.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNLSAMVTA-LIDEW-SWTKSDCILHVLPLHHVHGVvnKLLCPLWVGATCVMLP--EFSPKEVW 79
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQMAFVITNhLADLMpGTTEQDASLVVAPLSHGAGI--HQLCQVARGAATVLLPseRFDPAEVW 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 80 EhfLSTDSRSINVFmAVPTIYSKLIDyyesHLAkpgikdfVKAMCQQKIRLMVSGSSALPVPTLERWREITGHTLLERYG 159
Cdd:PRK07470 248 A--LVERHRVTNLF-TVPTILKMLVE----HPA-------VDRYDHSSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 160 MTEIGMALT-------NPLNGPRVP-GSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRG 231
Cdd:PRK07470 314 LGEVTGNITvlppalhDAEDGPDARiGTCGFERTGMEVQIQ-----------------DDEGRELPPG---ETGEICVIG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 232 PAVFNEYWNKPQETREAFTpDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAP 310
Cdd:PRK07470 374 PAVFAGYYNNPEANAKAFR-DGWFRTGDLGHLDARGFlYITGRAS-DMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVP 451
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2113536441 311 DSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK07470 452 DPVWGEVGVAVCVARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
2-371 |
2.14e-49 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 173.72 E-value: 2.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNL------SAMVTALidewswTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSP 75
Cdd:PRK08008 178 ILFTSGTTSRPKGVVITHYNLrfagyySAWQCAL------RDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 76 KEVWehflstdsrsinvfmavptiySKLIDYyeshlakpgikdfvKAMCQQKIRLMVSGSSALPVPTLER---WREIT-- 150
Cdd:PRK08008 252 RAFW---------------------GQVCKY--------------RATITECIPMMIRTLMVQPPSANDRqhcLREVMfy 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 151 ---------------GHTLLERYGMTE-IGMALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGT 214
Cdd:PRK08008 297 lnlsdqekdafeerfGVRLLTSYGMTEtIVGIIGDRPGDKRRWPSIGRPGFCYEAEIR-----------------DDHNR 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 215 EVFPGfedREGELQVRGPA---VFNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEV 291
Cdd:PRK08008 360 PLPAG---EIGEICIKGVPgktIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVEL 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 292 ERHLLAHPSIADVAVIGAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK08008 437 ENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
1-371 |
3.19e-49 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 172.68 E-value: 3.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAM-----VTALIDEWSwtksdCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSP 75
Cdd:PRK09088 139 LILFTSGTSGQPKGVMLSERNLQQTahnfgVLGRVDAHS-----SFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEP 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 76 KEV--WehfLSTDSRSINVFMAVPTIYSKLidyyeshLAKPGIKdfvkAMCQQKIRLMVSGSSALPVPTLERWREiTGHT 153
Cdd:PRK09088 214 KRTlgR---LGDPALGITHYFCVPQMAQAF-------RAQPGFD----AAALRHLTALFTGGAPHAAEDILGWLD-DGIP 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 154 LLERYGMTEIGMALTNPLNGPRVP---GSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVR 230
Cdd:PRK09088 279 MVDGFGMSEAGTVFGMSVDCDVIRakaGAAGIPTPTVQTRVV-----------------DDQGNDCPAG---VPGELLLR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 231 GPAVFNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGA 309
Cdd:PRK09088 339 GPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFfWVVDRKK-DMFISGGENVYPAEIEAVLADHPGIRECAVVGM 417
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2113536441 310 PDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK09088 418 ADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
2-371 |
4.74e-49 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 173.40 E-value: 4.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEVWEh 81
Cdd:PRK06087 192 VLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLA- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 fLSTDSRSINVFMAVPTIYS--KLIDYYESHLAkpgikdfvkamcqqKIRLMVSGSSALPVPTLERWREiTGHTLLERYG 159
Cdd:PRK06087 271 -LLEQQRCTCMLGATPFIYDllNLLEKQPADLS--------------ALRFFLCGGTTIPKKVARECQQ-RGIKLLSVYG 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 160 MTE----IGMALTNPLngPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPAVF 235
Cdd:PRK06087 335 STEssphAVVNLDDPL--SRFMHTDGYAAAGVEIKVV-----------------DEARKTLPPG---CEGEEASRGPNVF 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 236 NEYWNKPQETREAFTPDGWFRTGDTAVYKDNSYW-ILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTW 314
Cdd:PRK06087 393 MGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIkITGRKK-DIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERL 471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2113536441 315 GQRVSAIVKLRDG-HTLSLKKLKEW-GRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK06087 472 GERSCAYVVLKAPhHSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
4-368 |
9.98e-49 |
|
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: 171.33 E-value: 9.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQnlSAMVTAL--IDEWSWTKSDCILHVLPLHHVHGvvnklLCPLW----VGATCVMLPEFSPKE 77
Cdd:cd12118 140 YTSGTTGRPKGVVYHHR--GAYLNALanILEWEMKQHPVYLWTLPMFHCNG-----WCFPWtvaaVGGTNVCLRKVDAKA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 VWEhflSTDSRSINVFMAVPTIYSKLIDYYESHlAKPGikdfvkamcQQKIRLMVSGSsALPVPTLERWREItGHTLLER 157
Cdd:cd12118 213 IYD---LIEKHKVTHFCGAPTVLNMLANAPPSD-ARPL---------PHRVHVMTAGA-PPPAAVLAKMEEL-GFDVTHV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTEI-GMALTNPLNgprvPGSVGNPFP---------GVGVRIATEIpqkegssyTVHaegDAAGTEVFPGFEDREGEL 227
Cdd:cd12118 278 YGLTETyGPATVCAWK----PEWDELPTEerarlkarqGVRYVGLEEV--------DVL---DPETMKPVPRDGKTIGEI 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 228 QVRGPAVFNEYWNKPQETREAFTpDGWFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVAVI 307
Cdd:cd12118 343 VFRGNIVMKGYLKNPEATAEAFR-GGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVV 421
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2113536441 308 GAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIrVEEIPRNQMGKINK 368
Cdd:cd12118 422 ARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVV-FGELPKTSTGKIQK 481
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
2-371 |
1.67e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 171.22 E-value: 1.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEVWEh 81
Cdd:PRK06145 154 LMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLA- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 flSTDSRSINVFMAVPTIYSKLidyyeshLAKPGIKDFVKAmcqqKIRLMVSGSSALPVPTLERWREI-TGHTLLERYGM 160
Cdd:PRK06145 233 --AIERHRLTCAWMAPVMLSRV-------LTVPDRDRFDLD----SLAWCIGGGEKTPESRIRDFTRVfTRARYIDAYGL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TEIGMALTNPLNGPRVP--GSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPAVFNEY 238
Cdd:PRK06145 300 TETCSGDTLMEAGREIEkiGSTGRALAHVEIRIA-----------------DGAGRWLPPN---MKGEICMRGPKVTKGY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 239 WNKPQETREAFTpDGWFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQRV 318
Cdd:PRK06145 360 WKDPEKTAEAFY-GDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERI 438
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2113536441 319 SAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK06145 439 TAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
3-371 |
2.60e-48 |
|
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: 170.79 E-value: 2.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 3 IYTSGTTGRPKGVLSTHQNLSAMV-TALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEF-SPKEVWE 80
Cdd:TIGR02262 167 LYSSGSTGMPKGVVHTHSNPYWTAeLYARNTLGIREDDVCFSAAKLFFAYGLGNALTFPMSVGATTVLMGERpTPDAVFD 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 HFLSTDSrsiNVFMAVPTIYSKLidyyeshLAKPGIKdfvkAMCQQKIRLMVSGSSALPVPTLERWREITGHTLLERYGM 160
Cdd:TIGR02262 247 RLRRHQP---TIFYGVPTLYAAM-------LADPNLP----SEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGS 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TEIGMALTNPLNGPRVPGSVGNPFPGVGVRIATEipqkegssytvhAEGDAAGTEVfpgfedreGELQVRGPAVFNEYWN 240
Cdd:TIGR02262 313 TEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGD------------GGQDVADGEP--------GELLISGPSSATMYWN 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 241 KPQETREAFTpDGWFRTGDTAVYKDNSYWIL-GRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQRVS 319
Cdd:TIGR02262 373 NRAKSRDTFQ-GEWTRSGDKYVRNDDGSYTYaGRTD-DMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPK 450
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2113536441 320 AIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:TIGR02262 451 AFVVLRPGQTALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKL 502
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
1-360 |
3.09e-48 |
|
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: 166.32 E-value: 3.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVhGVVNKLLCPLWVGATCVMLPEFSPKEVWE 80
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPLFHI-GTLMFTLATFHAGGTNVFVRRVDAEEVLE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 hfLSTDSRSINVFMAVPTIySKLIDyyeshLAKPGIKDFvkamcqqkirlmvsgSSALPVPTLERWREI--TGHTLLER- 157
Cdd:cd17636 83 --LIEAERCTHAFLLPPTI-DQIVE-----LNADGLYDL---------------SSLRSSPAAPEWNDMatVDTSPWGRk 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 ---YGMTEI-GMALTNPLNGPRVpGSVGNPFPGVGVRIateipqkegssytvhaeGDAAGTEVFPGfedREGELQVRGPA 233
Cdd:cd17636 140 pggYGQTEVmGLATFAALGGGAI-GGAGRPSPLVQVRI-----------------LDEDGREVPDG---EVGEIVARGPT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 234 VFNEYWNKPQETREAFTpDGWFRTGDtavykdnsywiLGRTSVD-----------IIKSGGYKISALEVERHLLAHPSIA 302
Cdd:cd17636 199 VMAGYWNRPEVNARRTR-GGWHHTND-----------LGRREPDgslsfvgpktrMIKSGAENIYPAEVERCLRQHPAVA 266
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2113536441 303 DVAVIGAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPR 360
Cdd:cd17636 267 DAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEFADALPR 324
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
4-375 |
8.12e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 170.61 E-value: 8.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNL------SAMVTALIDEwswtkSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKE 77
Cdd:PRK06178 216 YTGGTTGMPKGCEHTQRDMvytaaaAYAVAVVGGE-----DSVFLSFLPEFWIAGENFGLLFPLFSGATLVLLARWDAVA 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 VWEhflstdsrsinvfmAVP----TIYSKLIDYYESHLAKPGIKDFVKAMCQQKirLMVSGSSALPVPTLERWREITGHT 153
Cdd:PRK06178 291 FMA--------------AVEryrvTRTVMLVDNAVELMDHPRFAEYDLSSLRQV--RVVSFVKKLNPDYRQRWRALTGSV 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 154 LLE-RYGMTE--------IGMAlTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGFEdrE 224
Cdd:PRK06178 355 LAEaAWGMTEthtcdtftAGFQ-DDDFDLLSQPVFVGLPVPGTEFKIC-----------------DFETGELLPLGA--E 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 225 GELQVRGPAVFNEYWNKPQETREAFTpDGWFRTGDTAVYKDNSYW-ILGRTSvDIIKSGGYKISALEVERHLLAHPSIAD 303
Cdd:PRK06178 415 GEIVVRTPSLLKGYWNKPEATAEALR-DGWLHTGDIGKIDEQGFLhYLGRRK-EMLKVNGMSVFPSEVEALLGQHPAVLG 492
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2113536441 304 VAVIGAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAelIR-VEEIPRNQMGKINKKQLLALF 375
Cdd:PRK06178 493 SAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPE--IRiVDALPMTATGKVRKQDLQALA 563
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
1-307 |
9.29e-48 |
|
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: 168.39 E-value: 9.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEVwe 80
Cdd:cd05914 93 LINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHVVFLDKIPSAKI-- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 HFLSTDSRSINVFMAVP----------TIYSKLIDYYESHLAKPGIKDFVKAMCQQK--------IRLMVSGSSALPVPT 142
Cdd:cd05914 171 IALAFAQVTPTLGVPVPlviekifkmdIIPKLTLKKFKFKLAKKINNRKIRKLAFKKvheafggnIKEFVIGGAKINPDV 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 143 LERWREItGHTLLERYGMTEIGMALT-NPLNGPRVpGSVGNPFPGVGVRIATEIPQKEgssytvhaegdaagtevfpgfe 221
Cdd:cd05914 251 EEFLRTI-GFPYTIGYGMTETAPIISySPPNRIRL-GSAGKVIDGVEVRIDSPDPATG---------------------- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 222 drEGELQVRGPAVFNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSY-WILGRTSVDIIKSGGYKISALEVERHLLAHPS 300
Cdd:cd05914 307 --EGEIIVRGPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYlYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPF 384
|
....*..
gi 2113536441 301 IADVAVI 307
Cdd:cd05914 385 VLESLVV 391
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1-371 |
1.24e-47 |
|
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: 167.61 E-value: 1.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTH-------------QNL---SAMVTALIDEWSWtksdcilhvlplhhVHGVVNKLLCPLWVG 64
Cdd:cd05971 92 LIIYTSGTTGPPKGALHAHrvllghlpgvqfpFNLfprDGDLYWTPADWAW--------------IGGLLDVLLPSLYFG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 65 ATCVM--LPEFSPKEVWEhfLSTDSRSINVFMavPTIYSKLIDYYESHLAKPGIKdfvkamcqqkIRLMVSGSSALPVPT 142
Cdd:cd05971 158 VPVLAhrMTKFDPKAALD--LMSRYGVTTAFL--PPTALKMMRQQGEQLKHAQVK----------LRAIATGGESLGEEL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 143 LERWREITGHTLLERYGMTEIGMALTNPLN-GPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfe 221
Cdd:cd05971 224 LGWAREQFGVEVNEFYGQTECNLVIGNCSAlFPIKPGSMGKPIPGHRVAIV-----------------DDNGTPLPPG-- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 222 dREGELQVR--GPAVFNEYWNKPQETREAFTPDgWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAH 298
Cdd:cd05971 285 -EVGEIAVElpDPVAFLGYWNNPSATEKKMAGD-WLLTGDLGRKDSDGYfWYVGRDD-DVITSSGYRIGPAEIEECLLKH 361
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113536441 299 PSIADVAVIGAPDSTWGQRVSAIVKLRDGHTLS---LKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd05971 362 PAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSdalAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
2-371 |
3.23e-47 |
|
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: 166.39 E-value: 3.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLhHVHGVVNKLLCPLWVGATCVMLPEfspkEVW-- 79
Cdd:cd17649 99 VIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASF-NFDGAHEQLLPPLICGACVVLRPD----ELWas 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 80 --EHFLSTDSRSINVfMAVPTIY-SKLIDYYESHLAKPgikdfvkamcQQKIRLMVSGSSALPVPTLERWREItGHTLLE 156
Cdd:cd17649 174 adELAEMVRELGVTV-LDLPPAYlQQLAEEADRTGDGR----------PPSLRLYIFGGEALSPELLRRWLKA-PVRLFN 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 157 RYGMTEIGMALT-------NPLNGPRVPgsVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQV 229
Cdd:cd17649 242 AYGPTEATVTPLvwkceagAARAGASMP--IGRPLGGRSAYIL-----------------DADLNPVPVG---VTGELYI 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 230 RGPAVFNEYWNKPQETREAFTPDG-------WFRTGDTAVYKDN-SYWILGRtsVD-IIKSGGYKISALEVERHLLAHPS 300
Cdd:cd17649 300 GGEGLARGYLGRPELTAERFVPDPfgapgsrLYRTGDLARWRDDgVIEYLGR--VDhQVKIRGFRIELGEIEAALLEHPG 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2113536441 301 IADVAVIgAPDSTWGQRVSAIVKLRDGHTLS--LKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd17649 378 VREAAVV-ALDGAGGKQLVAYVVLRAAAAQPelRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1-371 |
8.50e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 167.26 E-value: 8.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSW-TKSDCILHVLPLHHVHGVVNkLLCPLWVGATCVMLP--EFSPKE 77
Cdd:PRK07786 178 LIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGAdINSDVGFVGVPLFHIAGIGS-MLPGLLLGAPTVIYPlgAFDPGQ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 ---VWEHflstdSRSINVFMaVPTiysklidYYESHLAKPGIKdfvkamcQQKIRLMVSGSSALPVP-TLERWREIT--G 151
Cdd:PRK07786 257 lldVLEA-----EKVTGIFL-VPA-------QWQAVCAEQQAR-------PRDLALRVLSWGAAPASdTLLRQMAATfpE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 152 HTLLERYGMTEIGmALTNPLNGP---RVPGSVGNPFPGVGVRIATEipqkegssytvhAEGDAAGTEVfpgfedreGELQ 228
Cdd:PRK07786 317 AQILAAFGQTEMS-PVTCMLLGEdaiRKLGSVGKVIPTVAARVVDE------------NMNDVPVGEV--------GEIV 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 229 VRGPAVFNEYWNKPQETREAFTpDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVI 307
Cdd:PRK07786 376 YRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYvWVVDRKK-DMIISGGENIYCAEVENVLASHPDIVEVAVI 453
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2113536441 308 GAPDSTWGQRVSAIVKLRDG-HTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK07786 454 GRADEKWGEVPVAVAAVRNDdAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTEL 518
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1-375 |
7.67e-46 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 164.67 E-value: 7.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATcVMLP---EFSPKE 77
Cdd:PRK05852 180 MIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGA-VLLPargRFSAHT 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 VWEHFLSTDSrsiNVFMAVPTIYSKLIDYYESHLAKPGikdfvkamcQQKIRLMVSGSSALPVPTLERWREITGHTLLER 157
Cdd:PRK05852 259 FWDDIKAVGA---TWYTAVPTIHQILLERAATEPSGRK---------PAALRFIRSCSAPLTAETAQALQTEFAAPVVCA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTEIgmalTNPLNGPRVPGSVGNPFPGVGVRIATeipQKEGSSYTVhaegdaAGTEVFPGFEDREGELQVRGPAVFNE 237
Cdd:PRK05852 327 FGMTEA----THQVTTTQIEGIGQTENPVVSTGLVG---RSTGAQIRI------VGSDGLPLPAGAVGEVWLRGTTVVRG 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 238 YWNKPQETREAFTpDGWFRTGDT-AVYKDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQ 316
Cdd:PRK05852 394 YLGDPTITAANFT-DGWLRTGDLgSLSAAGDLSIRGRIK-ELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGE 471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2113536441 317 RVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLLALF 375
Cdd:PRK05852 472 AVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAEQF 530
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
2-371 |
1.20e-45 |
|
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: 163.45 E-value: 1.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDE--WSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEVW 79
Cdd:cd05923 155 VFYTSGTTGLPKGAVIPQRAAESRVLFMSTQagLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADAL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 80 EhfLSTDSRSINVFmAVPTIYSKLIdyyeSHLAKPGIKdfvkamcQQKIRLMVSGSSALPVPTLERWREITGHTLLERYG 159
Cdd:cd05923 235 K--LIEQERVTSLF-ATPTHLDALA----AAAEFAGLK-------LSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 160 MTEIGMALTNPlnGPRvPGSVGNPFPGVGVRIAteipQKEGSSYTVHAEGDaagtevfpgfedrEGELQVR--GPAVFNE 237
Cdd:cd05923 301 TTEAMNSLYMR--DAR-TGTEMRPGFFSEVRIV----RIGGSPDEALANGE-------------EGELIVAaaADAAFTG 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 238 YWNKPQETREAFTpDGWFRTGDTAVYKDN-SYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQ 316
Cdd:cd05923 361 YLNQPEATAKKLQ-DGWYRTGDVGYVDPSgDVRILGRVD-DMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQ 438
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2113536441 317 RVSAIVKLRDGhTLSLKKLKEWGRAV-MAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd05923 439 SVTACVVPREG-TLSADELDQFCRASeLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
4-371 |
2.61e-45 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 163.45 E-value: 2.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSD----------CILHVLPLHHVHGVVNKLLCPLWVGATCVMLPef 73
Cdd:PRK12492 214 YTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqplmkegqeVMIAPLPLYHIYAFTANCMCMMVSGNHNVLIT-- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 74 SPKEVWEHFLSTDSRSINVFMAVPTIYSKLIDYyeshlakPGIK--DFvkamcqQKIRLMVSGSSALPVPTLERWREITG 151
Cdd:PRK12492 292 NPRDIPGFIKELGKWRFSALLGLNTLFVALMDH-------PGFKdlDF------SALKLTNSGGTALVKATAERWEQLTG 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 152 HTLLERYGMTEIG-MALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVR 230
Cdd:PRK12492 359 CTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVI-----------------DDDGNELPLG---ERGELCIK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 231 GPAVFNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGAP 310
Cdd:PRK12492 419 GPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVP 498
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2113536441 311 DSTWGQRVSAIVKLRDGhTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK12492 499 DERSGEAVKLFVVARDP-GLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
2-371 |
3.06e-45 |
|
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: 161.26 E-value: 3.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLH---HVHGvvnkLLCPLWVGATCVMLPE---FSP 75
Cdd:cd05945 102 IIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSfdlSVMD----LYPALASGATLVPVPRdatADP 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 76 KEVWEHFLSTDsrsINVFMAVPTIYSKLI---DYYESHLakPGIKDFVkaMCQQkirlmvsgssALPVPTLERWREIT-G 151
Cdd:cd05945 178 KQLFRFLAEHG---ITVWVSTPSFAAMCLlspTFTPESL--PSLRHFL--FCGE----------VLPHKTARALQQRFpD 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 152 HTLLERYGMTEIGMALT------NPLNG-PRVPgsVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedRE 224
Cdd:cd05945 241 ARIYNTYGPTEATVAVTyievtpEVLDGyDRLP--IGYAKPGAKLVIL-----------------DEDGRPVPPG---EK 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 225 GELQVRGPAVFNEYWNKPQETREAFTPD---GWFRTGDtAVYKDNS--YWILGRTSvDIIKSGGYKISALEVERHLLAHP 299
Cdd:cd05945 299 GELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGD-LVRLEADglLFYRGRLD-FQVKLNGYRIELEEIEAALRQVP 376
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2113536441 300 SIADVAVIGAPDSTWGQRVSAIVKLRDGHTLSL-KKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd05945 377 GVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLtKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
2-371 |
7.12e-45 |
|
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: 161.49 E-value: 7.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGvVNKLLCPLWVGATCVMLPEFSPKEVWEh 81
Cdd:TIGR03098 168 ILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYG-FNQLTTAFYVGATVVLHDYLLPRDVLK- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 flSTDSRSINVFMAVPTIYSKLidyyeSHLAKPgIKDFvkamcqQKIRLMVSGSSALPVPTLERWREITGHT-LLERYGM 160
Cdd:TIGR03098 246 --ALEKHGITGLAAVPPLWAQL-----AQLDWP-ESAA------PSLRYLTNSGGAMPRATLSRLRSFLPNArLFLMYGL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TEIGMALT-NPLNGPRVPGSVGNPFPGVGVRIateipqkegssytVHAEGDaagtEVFPGfedREGELQVRGPAVFNEYW 239
Cdd:TIGR03098 312 TEAFRSTYlPPEEVDRRPDSIGKAIPNAEVLV-------------LREDGS----ECAPG---EEGELVHRGALVAMGYW 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 240 NKPQETREAFTPDGWFRTG----DTAVYKDNSYW--------ILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVI 307
Cdd:TIGR03098 372 NDPEKTAERFRPLPPFPGElhlpELAVWSGDTVRrdeegflyFVGRRD-EMIKTSGYRVSPTEVEEVAYATGLVAEAVAF 450
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2113536441 308 GAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:TIGR03098 451 GVPDPTLGQAIVLVVTPPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
1-373 |
3.03e-44 |
|
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: 158.43 E-value: 3.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHqnlSAMVTalidEWSWTKsdcilHVLPLHH------------VHGVVNKLLCPLWVGATCV 68
Cdd:cd05969 93 LLHYTSGTTGTPKGVLHVH---DAMIF----YYFTGK-----YVLDLHPddiywctadpgwVTGTVYGIWAPWLNGVTNV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 69 MLP-EFSPkEVWEHFLstDSRSINVFMAVPTIYSKLIDYyeshlakpGIkDFVKAMCQQKIRLMVSGSSALPvPTLERW- 146
Cdd:cd05969 161 VYEgRFDA-ESWYGII--ERVKVTVWYTAPTAIRMLMKE--------GD-ELARKYDLSSLRFIHSVGEPLN-PEAIRWg 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 147 REITGHTLLERYGMTEIG-MALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREG 225
Cdd:cd05969 228 MEVFGVPIHDTWWQTETGsIMIANYPCMPIKPGSMGKPLPGVKAAVV-----------------DENGNELPPG---TKG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 226 ELQVRG--PAVFNEYWNKPQETREAFtPDGWFRTGDTAvYKDNS--YWILGRTSvDIIKSGGYKISALEVERHLLAHPSI 301
Cdd:cd05969 288 ILALKPgwPSMFRGIWNDEERYKNSF-IDGWYLTGDLA-YRDEDgyFWFVGRAD-DIIKTSGHRVGPFEVESALMEHPAV 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113536441 302 ADVAVIGAPDSTWGQRVSAIVKLRDGHTLSlKKLKE----WGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLLA 373
Cdd:cd05969 365 AEAGVIGKPDPLRGEIIKAFISLKEGFEPS-DELKEeiinFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLKA 439
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2-372 |
4.52e-44 |
|
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: 158.37 E-value: 4.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFS-PKEVWE 80
Cdd:cd05922 122 LLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGL-SVLNTHLLRGATLVLTNDGVlDDAFWE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 HFlsTDSRsINVFMAVPTIYSKLidyyeshlAKPGIKDfvkaMCQQKIRLMVSGSSALPVPTLERWRE-ITGHTLLERYG 159
Cdd:cd05922 201 DL--REHG-ATGLAGVPSTYAML--------TRLGFDP----AKLPSLRYLTQAGGRLPQETIARLRElLPGAQVYVMYG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 160 MTEI--GMALTNPLNGPRVPGSVGNPFPGVGVRIATEipqkegssytvhaegdaAGTEVFPGfedREGELQVRGPAVFNE 237
Cdd:cd05922 266 QTEAtrRMTYLPPERILEKPGSIGLAIPGGEFEILDD-----------------DGTPTPPG---EPGEIVHRGPNVMKG 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 238 YWNKPQETREAFTPDGWFRTGDTAVYKDNSYW-ILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDsTWGQ 316
Cdd:cd05922 326 YWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLfIVGRRD-RMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPD-PLGE 403
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2113536441 317 RVSAIVKLRDGHTLS--LKKLkewgRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLL 372
Cdd:cd05922 404 KLALFVTAPDKIDPKdvLRSL----AERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
1-366 |
7.10e-44 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 154.49 E-value: 7.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSPKEVWE 80
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFL-YGAISALYLGGTFIGQRKFNPKSWIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 hflsTDSR-SINVFMAVPTIYSKLIDYYESHLakpgikdfvkamcqqKIRLMVSGSSALPVPTLERWREITGHT-LLERY 158
Cdd:cd17633 83 ----KINQyNATVIYLVPTMLQALARTLEPES---------------KIKSIFSSGQKLFESTKKKLKNIFPKAnLIEFY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 159 GMTEIGMALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVfpgfedreGELQVRGPAVFNEY 238
Cdd:cd17633 144 GTSELSFITYNFNQESRPPNSVGRPFPNVEIEIR-----------------NADGGEI--------GKIFVKSEMVFSGY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 239 WNKpqetrEAFTPDGWFRTGDTAVYKDNSYWIL-GRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQR 317
Cdd:cd17633 199 VRG-----GFSNPDGWMSVGDIGYVDEEGYLYLvGRES-DMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEI 272
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2113536441 318 VSAIVKlrdGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKI 366
Cdd:cd17633 273 AVALYS---GDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKI 318
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
1-371 |
1.07e-43 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 159.19 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSPKEVWE 80
Cdd:PLN02860 176 LICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGL-SSALAMLMVGACHVLLPKFDAKAALQ 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 hflSTDSRSINVFMAVPTIYSKLIDYyeshLAKPGIKDfvkamCQQKIRLMVSGSSALPVPTLERWREITGHT-LLERYG 159
Cdd:PLN02860 255 ---AIKQHNVTSMITVPAMMADLISL----TRKSMTWK-----VFPSVRKILNGGGSLSSRLLPDAKKLFPNAkLFSAYG 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 160 MTEIGMALT-NPLNGPRVPgSVGNPFPGVGVRIATEIPQKEGSSYtvhaeGDAA-GTEVFPGFED--REGELQVRGPAVF 235
Cdd:PLN02860 323 MTEACSSLTfMTLHDPTLE-SPKQTLQTVNQTKSSSVHQPQGVCV-----GKPApHVELKIGLDEssRVGRILTRGPHVM 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 236 NEYWNKPQETREAFTPDGWFRTGDTAVYKD-NSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTW 314
Cdd:PLN02860 397 LGYWGQNSETASVLSNDGWLDTGDIGWIDKaGNLWLIGRSN-DRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRL 475
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2113536441 315 GQRVSAIVKLRDG------HTLSLKKLKEWGRAVMAPYC---------IPAELIRVEE-IPRNQMGKINKKQL 371
Cdd:PLN02860 476 TEMVVACVRLRDGwiwsdnEKENAKKNLTLSSETLRHHCreknlsrfkIPKLFVQWRKpFPLTTTGKIRRDEV 548
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
2-371 |
1.46e-43 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 158.78 E-value: 1.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNL---SAMVTaliDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGAtCVMLP--EFSPK 76
Cdd:PRK12583 206 IQYTSGTTGFPKGATLSHHNIlnnGYFVA---ESLGLTEHDRLCVPVPLYHCFGMVLANLGCMTVGA-CLVYPneAFDPL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 77 EVWEhflSTDSRSINVFMAVPTIYSklidyyeSHLAKPGIKDFVKAmcqqKIRLMVSGSSALPVPTLER-WREITGHTLL 155
Cdd:PRK12583 282 ATLQ---AVEEERCTALYGVPTMFI-------AELDHPQRGNFDLS----SLRTGIMAGAPCPIEVMRRvMDEMHMAEVQ 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 156 ERYGMTEIG-----MALTNPLngPRVPGSVGNPFPGVGVRIateipqkegssytVHAEGDAAGTevfpgfeDREGELQVR 230
Cdd:PRK12583 348 IAYGMTETSpvslqTTAADDL--ERRVETVGRTQPHLEVKV-------------VDPDGATVPR-------GEIGELCTR 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 231 GPAVFNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSYW-ILGRtSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGA 309
Cdd:PRK12583 406 GYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQGYVrIVGR-SKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGV 484
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2113536441 310 PDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK12583 485 PDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRM 546
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
4-371 |
2.87e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 158.00 E-value: 2.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNL-------SAMVTALIDEwswtKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPefSPK 76
Cdd:PRK05677 214 YTGGTTGVAKGAMLTHRNLvanmlqcRALMGSNLNE----GCEILIAPLPLYHIYAFTFHCMAMMLIGNHNILIS--NPR 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 77 EVwEHFLSTDSR-SINVFMAVPTIYSKLIDYyeshlakpgiKDFvKAMCQQKIRLMVSGSSALPVPTLERWREITGHTLL 155
Cdd:PRK05677 288 DL-PAMVKELGKwKFSGFVGLNTLFVALCNN----------EAF-RKLDFSALKLTLSGGMALQLATAERWKEVTGCAIC 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 156 ERYGMTEIG-MALTNPLNGPRVpGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPAV 234
Cdd:PRK05677 356 EGYGMTETSpVVSVNPSQAIQV-GTIGIPVPSTLCKVI-----------------DDDGNELPLG---EVGELCVKGPQV 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 235 FNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSYW-ILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDST 313
Cdd:PRK05677 415 MKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMrIVDRKK-DMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEK 493
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2113536441 314 WGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK05677 494 SGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
4-371 |
3.31e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 152.02 E-value: 3.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQN--LSAMVTALidEWSWTKSDCILHVLPLHHVHGvvnklLCPLW----VGATCVMLPEFSPKE 77
Cdd:PRK08162 189 YTSGTTGNPKGVVYHHRGayLNALSNIL--AWGMPKHPVYLWTLPMFHCNG-----WCFPWtvaaRAGTNVCLRKVDPKL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 VWEhfLSTDSRsINVFMAVPTIYSKLIDYYEShlAKPGIkdfvkamcQQKIRLMVSGSsALPVPTLERWREItGHTLLER 157
Cdd:PRK08162 262 IFD--LIREHG-VTHYCGAPIVLSALINAPAE--WRAGI--------DHPVHAMVAGA-APPAAVIAKMEEI-GFDLTHV 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTEI-GmaltnplngprvPGSVGNPFPGVGVRIATEIPQK---EGSSYtvHAEGDAA------GTEVfPGFEDREGEL 227
Cdd:PRK08162 327 YGLTETyG------------PATVCAWQPEWDALPLDERAQLkarQGVRY--PLQEGVTvldpdtMQPV-PADGETIGEI 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 228 QVRGPAVFNEYWNKPQETREAFTpDGWFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVAVI 307
Cdd:PRK08162 392 MFRGNIVMKGYLKNPKATEEAFA-GGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVV 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2113536441 308 GAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAElIRVEEIPRNQMGKINKKQL 371
Cdd:PRK08162 471 AKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKA-VVFGELPKTSTGKIQKFVL 533
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
2-375 |
1.64e-40 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 150.38 E-value: 1.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALI----DEWSWTKSDCI-LHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPK 76
Cdd:PLN02574 203 IMYSSGTTGASKGVVLTHRNLIAMVELFVrfeaSQYEYPGSDNVyLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDAS 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 77 EVWEhflSTDSRSINVFMAVPTIYSKLIdyyesHLAKPgikdfVKAMCQQKIRLMVSGSSALPVPTLERWREITGHT-LL 155
Cdd:PLN02574 283 DMVK---VIDRFKVTHFPVVPPILMALT-----KKAKG-----VCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVdFI 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 156 ERYGMTEIGMALTNPLNGPRVP--GSVGNPFPGVGVRIateipqkegssytVHAEgdaAGTEVFPGfedREGELQVRGPA 233
Cdd:PLN02574 350 QGYGMTESTAVGTRGFNTEKLSkySSVGLLAPNMQAKV-------------VDWS---TGCLLPPG---NCGELWIQGPG 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 234 VFNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDS 312
Cdd:PLN02574 411 VMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYlYIVDRLK-EIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDK 489
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2113536441 313 TWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLLALF 375
Cdd:PLN02574 490 ECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRSL 552
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
1-371 |
1.96e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 150.08 E-value: 1.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCpLWVGATCVMLPEFSPKEVWE 80
Cdd:PRK07788 211 IVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLA-MALGSTVVLRRRFDPEATLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 hflSTDSRSINVFMAVPTIYSKLIDYYESHLAKPGIkdfvkamcqQKIRLMVSGSSALPVPTLERWREITGHTLLERYGM 160
Cdd:PRK07788 290 ---DIAKHKATALVVVPVMLSRILDLGPEVLAKYDT---------SSLKIIFVSGSALSPELATRALEAFGPVLYNLYGS 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TEIGMA-LTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPAVFNEYW 239
Cdd:PRK07788 358 TEVAFAtIATPEDLAEAPGTVGRPPKGVTVKIL-----------------DENGNEVPRG---VVGRIFVGNGFPFEGYT 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 240 NKPQETREaftpDGWFRTGDTAVYKDNSYW-ILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQRV 318
Cdd:PRK07788 418 DGRDKQII----DGLLSSGDVGYFDEDGLLfVDGRDD-DMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRL 492
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2113536441 319 SAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK07788 493 RAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKREL 545
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
1-371 |
8.69e-40 |
|
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: 148.00 E-value: 8.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIY-TSGTTGRPKGVLSTHQNLSAMVTALIDEW-SWTKSDCILHVLPLHHVHGVVNKLLCPlWVGATCVM---LPEFSP 75
Cdd:cd05928 177 MAIYfTSGTTGSPKMAEHSHSSLGLGLKVNGRYWlDLTASDIMWNTSDTGWIKSAWSSLFEP-WIQGACVFvhhLPRFDP 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 76 KEvwehFLSTDSR-SINVFMAVPTIYSKLIDyyeshlakpgiKDFVKAMCQqKIRLMVSGSSALPVPTLERWREITGHTL 154
Cdd:cd05928 256 LV----ILKTLSSyPITTFCGAPTVYRMLVQ-----------QDLSSYKFP-SLQHCVTGGEPLNPEVLEKWKAQTGLDI 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 155 LERYGMTEIGMALTNPLNGPRVPGSVGNPFPGVGVRIATEipqkEGSSYTVHAEGDAaGTEVFPgfedregelqVRGPAV 234
Cdd:cd05928 320 YEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDD----NGNVLPPGTEGDI-GIRVKP----------IRPFGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 235 FNEYWNKPQETREAFTPDGWFrTGDTAVYKDNSY-WILGRtSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDST 313
Cdd:cd05928 385 FSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYfWFMGR-ADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPI 462
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2113536441 314 WGQRVSAIVKL------RDGHTLSlKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd05928 463 RGEVVKAFVVLapqflsHDPEQLT-KELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
2-371 |
1.77e-39 |
|
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: 146.28 E-value: 1.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLP-------LhhvhgvvnKLLCPLWVGATCVMLPE-- 72
Cdd:cd12116 131 VIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTyafdislL--------ELLLPLLAGARVVIAPRet 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 73 -FSPKEVWEHFlstDSRSINVFMAVPTIYSKLIDyyeshlAKPGIKDFVKAMCqqkirlmvsGSSALPvPTLERWREITG 151
Cdd:cd12116 203 qRDPEALARLI---EAHSITVMQATPATWRMLLD------AGWQGRAGLTALC---------GGEALP-PDLAARLLSRV 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 152 HTLLERYGMTEIGM-ALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGFedrEGELQVR 230
Cdd:cd12116 264 GSLWNLYGPTETTIwSTAARVTAAAGPIPIGRPLANTQVYVL-----------------DAALRPVPPGV---PGELYIG 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 231 GPAVFNEYWNKPQETREAFTPDG-------WFRTGDTAVYK-DNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIA 302
Cdd:cd12116 324 GDGVAQGYLGRPALTAERFVPDPfagpgsrLYRTGDLVRRRaDGRLEYLGRAD-GQVKIRGHRIELGEIEAALAAHPGVA 402
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2113536441 303 DVAVIGAPDSTwGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd12116 403 QAAVVVREDGG-DRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
2-368 |
2.20e-39 |
|
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: 143.17 E-value: 2.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDE-WSWTKSDCILHVLPLHHVHGVVNKLLCpLWVGATCVMLPEFSPKEVWE 80
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFFAVPDILQKEgLNWVVGDVTYLPLPATHIGGLWWILTC-LIHGGLCVTGGENTTYKSLF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 HFLSTDSRSINVFmaVPTIYSKLIDYYESHLAKpgikdfvkamcQQKIRLMVSGSSaLPVPTLERWREITGHT-LLERYG 159
Cdd:cd17635 85 KILTTNAVTTTCL--VPTLLSKLVSELKSANAT-----------VPSLRLIGYGGS-RAIAADVRFIEATGLTnTAQVYG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 160 MTEIGMALTNPL-NGPRVPGSVGNPFPGVGVRIATeipqkegssytvhaegdaagTEVFPGFEDREGELQVRGPAVFNEY 238
Cdd:cd17635 151 LSETGTALCLPTdDDSIEINAVGRPYPGVDVYLAA--------------------TDGIAGPSASFGTIWIKSPANMLGY 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 239 WNKPQETREAFTpDGWFRTGDTA-VYKDNSYWILGRTSVDIIKsGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQR 317
Cdd:cd17635 211 WNNPERTAEVLI-DGWVNTGDLGeRREDGFLFITGRSSESINC-GGVKIAPDEVERIAEGVSGVQECACYEISDEEFGEL 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2113536441 318 V-SAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINK 368
Cdd:cd17635 289 VgLAVVASAELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2-365 |
3.18e-39 |
|
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: 143.29 E-value: 3.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQN--LSAMVTALIDEWSWTKSDCILH------------VLPLHHVHGVVNKLLCPLWVGATC 67
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDifRMLMGGADFGTGEFTPSEDAHKaaaaaagtvmfpAPPLMHGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 68 VMLPEFSPKEVWEhflSTDSRSINVFMAVPTIYSK-LIDyyesHLAKPGIKDFvkamcqQKIRLMVSGSSALPVPTLERW 146
Cdd:cd05924 88 LPDDRFDPEEVWR---TIEKHKVTSMTIVGDAMARpLID----ALRDAGPYDL------SSLFAISSGGALLSPEVKQGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 147 REITGH-TLLERYGMTEIGMALTNpLNGPRVPGSvgNPFPGVGVRiateipqkegssyTVHAEGDaaGTEVFPGfEDREG 225
Cdd:cd05924 155 LELVPNiTLVDAFGSSETGFTGSG-HSAGSGPET--GPFTRANPD-------------TVVLDDD--GRVVPPG-SGGVG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 226 ELQVRGpAVFNEYWNKPQETREAF-TPDG--WFRTGDTA-VYKDNSYWILGRTSVdIIKSGGYKISALEVERHLLAHPSI 301
Cdd:cd05924 216 WIARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDRAtVEADGTVTLLGRGSV-CINTGGEKVFPEEVEEALKSHPAV 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2113536441 302 ADVAVIGAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGK 365
Cdd:cd05924 294 YDVLVVGRPDERWGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
2-371 |
3.60e-39 |
|
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: 144.76 E-value: 3.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDcilhVLPLHHVHGV---VNKLLCPLWVGATCVMLPEF---SP 75
Cdd:cd17643 98 VIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDD----VWTLFHSYAFdfsVWEIWGALLHGGRLVVVPYEvarSP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 76 KEVWEhfLSTDSRsINVFMAVPTIYSKLIDYyeshLAKPGIKdfvkamcQQKIRLMVSGSSALPVPTLERWREITGH--- 152
Cdd:cd17643 174 EDFAR--LLRDEG-VTVLNQTPSAFYQLVEA----ADRDGRD-------PLALRYVIFGGEALEAAMLRPWAGRFGLdrp 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 153 TLLERYGMTEIGMALT-NPLNGPRVPGS----VGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGEL 227
Cdd:cd17643 240 QLVNMYGITETTVHVTfRPLDAADLPAAaaspIGRPLPGLRVYVL-----------------DADGRPVPPG---VVGEL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 228 QVRGPAVFNEYWNKPQETREAFTPDGW-------FRTGDTAVYKDN-SYWILGRTSvDIIKSGGYKISALEVERHLLAHP 299
Cdd:cd17643 300 YVSGAGVARGYLGRPELTAERFVANPFggpgsrmYRTGDLARRLPDgELEYLGRAD-EQVKIRGFRIELGEIEAALATHP 378
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2113536441 300 SIADVAVIGAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd17643 379 SVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
4-371 |
3.72e-39 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 145.82 E-value: 3.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGV------LSTHQNLSAMvTALIDEWSWTKSDCI-LHVLPLHHV-----HGVVNKLlcplwvGATCVMLP 71
Cdd:PRK08276 147 YSSGTTGRPKGIkrplpgLDPDEAPGMM-LALLGFGMYGGPDSVyLSPAPLYHTaplrfGMSALAL------GGTVVVME 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 72 EFSPkevwEHFLSTDSR-SINVFMAVPTIYSKLidyyeshLAKPgikDFVKAMCQ-QKIRLMVSGSSALPVPTLERWREI 149
Cdd:PRK08276 220 KFDA----EEALALIERyRVTHSQLVPTMFVRM-------LKLP---EEVRARYDvSSLRVAIHAAAPCPVEVKRAMIDW 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 150 TGHTLLERYGMTE-IGMALTNPLNGPRVPGSVGNPFPGVgVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQ 228
Cdd:PRK08276 286 WGPIIHEYYASSEgGGVTVITSEDWLAHPGSVGKAVLGE-VRIL-----------------DEDGNELPPG---EIGTVY 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 229 VRGPAVFNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSYWIL-GRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVI 307
Cdd:PRK08276 345 FEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVGYLDEDGYLYLtDRKS-DMIISGGVNIYPQEIENLLVTHPKVADVAVF 423
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2113536441 308 GAPDSTWGQRVSAIVKLRDGHTLS---LKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK08276 424 GVPDEEMGERVKAVVQPADGADAGdalAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
4-371 |
3.78e-39 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 146.70 E-value: 3.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNLSAMVtALIDEW---SWTKSDCILHV-----LPLHHVHGV-VNKLLcPLWVGATCVMLPefS 74
Cdd:PRK07059 211 YTGGTTGVSKGATLLHRNIVANV-LQMEAWlqpAFEKKPRPDQLnfvcaLPLYHIFALtVCGLL-GMRTGGRNILIP--N 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 75 PKEVWEHFLSTDSRSINVFMAVPTIYSKLidyyeshLAKPGIK--DFvkamcqQKIRLMVSGSSALPVPTLERWREITGH 152
Cdd:PRK07059 287 PRDIPGFIKELKKYQVHIFPAVNTLYNAL-------LNNPDFDklDF------SKLIVANGGGMAVQRPVAERWLEMTGC 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 153 TLLERYGMTEIGMALT-NPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRG 231
Cdd:PRK07059 354 PITEGYGLSETSPVATcNPVDATEFSGTIGLPLPSTEVSIR-----------------DDDGNDLPLG---EPGEICIRG 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 232 PAVFNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSYW-ILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAP 310
Cdd:PRK07059 414 PQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTkIVDRKK-DMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVP 492
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2113536441 311 DSTWGQRVSAIVKLRDgHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK07059 493 DEHSGEAVKLFVVKKD-PALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
4-371 |
3.82e-39 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 146.74 E-value: 3.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNLSAMV-------TALIDEwswtKSDCILHVLPLHHVHGV-VNKLLCpLWVGATCVmlpefsp 75
Cdd:PRK08974 213 YTGGTTGVAKGAMLTHRNMLANLeqakaayGPLLHP----GKELVVTALPLYHIFALtVNCLLF-IELGGQNL------- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 76 kevwehfLSTDSRSINVFMA------------VPTIYSKLIDYYESHLAkpgikDFvkamcqQKIRLMVSGSSALPVPTL 143
Cdd:PRK08974 281 -------LITNPRDIPGFVKelkkypftaitgVNTLFNALLNNEEFQEL-----DF------SSLKLSVGGGMAVQQAVA 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 144 ERWREITGHTLLERYGMTEIGMALT-NPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfed 222
Cdd:PRK08974 343 ERWVKLTGQYLLEGYGLTECSPLVSvNPYDLDYYSGSIGLPVPSTEIKLV-----------------DDDGNEVPPG--- 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 223 REGELQVRGPAVFNEYWNKPQETREAFTpDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAHPSI 301
Cdd:PRK08974 403 EPGELWVKGPQVMLGYWQRPEATDEVIK-DGWLATGDIAVMDEEGFlRIVDRKK-DMILVSGFNVYPNEIEDVVMLHPKV 480
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 302 ADVAVIGAPDSTWGQRVSAIVKLRDgHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK08974 481 LEVAAVGVPSEVSGEAVKIFVVKKD-PSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
1-371 |
4.28e-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: 146.13 E-value: 4.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDE---WSWTKSDCILHVLPLHHVHGVVNkLLCPLWVGATCVMLPEFSPke 77
Cdd:cd17642 188 LIMNSSGSTGLPKGVQLTHKNIVARFSHARDPifgNQIIPDTAILTVIPFHHGFGMFT-TLGYLICGFRVVLMYKFEE-- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 vwEHFLST--DSRSINVFMaVPTIY-----SKLIDYYE-SHlakpgikdfvkamcqqkirLMVSGSSALPVPtlerwREI 149
Cdd:cd17642 265 --ELFLRSlqDYKVQSALL-VPTLFaffakSTLVDKYDlSN-------------------LHEIASGGAPLS-----KEV 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 150 tGHTLLER---------YGMTEIGMALTNPLNGPRVPGSVGNPFPGVGVRIateIPQKEGSSYTVhaegdaagtevfpgf 220
Cdd:cd17642 318 -GEAVAKRfklpgirqgYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKV---VDLDTGKTLGP--------------- 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 221 eDREGELQVRGPAVFNEYWNKPQETREAFTPDGWFRTGDTAVY-KDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHP 299
Cdd:cd17642 379 -NERGELCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYdEDGHFFIVDRLK-SLIKYKGYQVPPAELESILLQHP 456
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2113536441 300 SIADVAVIGAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWgravMAPYCIPAELIR-----VEEIPRNQMGKINKKQL 371
Cdd:cd17642 457 KIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEKEVMDY----VASQVSTAKRLRggvkfVDEVPKGLTGKIDRRKI 529
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
1-368 |
4.64e-39 |
|
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: 146.10 E-value: 4.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQ-NLSAMVTALIdeWSWTKSDCI-LHVLPLHHVHGVVNKLLCPlWVGATCVMLPE---FSP 75
Cdd:cd05970 189 LVYFSSGTTGMPKMVEHDFTyPLGHIVTAKY--WQNVREGGLhLTVADTGWGKAVWGKIYGQ-WIAGAAVFVYDydkFDP 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 76 KEVWEhflSTDSRSINVFMAVPTIYSKLIDYYESHLakpgikDFvkamcqQKIRLMVSGSSALPVPTLERWREITGHTLL 155
Cdd:cd05970 266 KALLE---KLSKYGVTTFCAPPTIYRFLIREDLSRY------DL------SSLRYCTTAGEALNPEVFNTFKEKTGIKLM 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 156 ERYGMTEIGMALTN-PLNGPRvPGSVGNPFPGVGVriatEIPQKEGSSYTVhaegdaagtevfpgfeDREGELQVRGP-- 232
Cdd:cd05970 331 EGFGQTETTLTIATfPWMEPK-PGSMGKPAPGYEI----DLIDREGRSCEA----------------GEEGEIVIRTSkg 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 233 ---AVFNEYWNKPQETREAFTpDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIG 308
Cdd:cd05970 390 kpvGLFGGYYKDAEKTAEVWH-DGYYHTGDAAWMDEDGYlWFVGRTD-DLIKSSGYRIGPFEVESALIQHPAVLECAVTG 467
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2113536441 309 APDSTWGQRVSAIVKLRDGHTLS---LKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINK 368
Cdd:cd05970 468 VPDPIRGQVVKATIVLAKGYEPSeelKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
4-371 |
2.89e-38 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 144.12 E-value: 2.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQN--LSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLwVGATCVML-PEFSPKEVWE 80
Cdd:PRK06018 184 YTSGTTGDPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPS-MGTKLVMPgAKLDGASVYE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 HFlstDSRSINVFMAVPTIYSKLIDYYESHLAK-PgikdfvkamcqqKIRLMVSGSSALPVPTLERWREItGHTLLERYG 159
Cdd:PRK06018 263 LL---DTEKVTFTAGVPTVWLMLLQYMEKEGLKlP------------HLKMVVCGGSAMPRSMIKAFEDM-GVEVRHAWG 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 160 MTEigmalTNPLngprvpGSVGN---PFPGVGVRIATEIPQKEG-SSYTVHAE-GDAAGTEVfPGFEDREGELQVRGPAV 234
Cdd:PRK06018 327 MTE-----MSPL------GTLAAlkpPFSKLPGDARLDVLQKQGyPPFGVEMKiTDDAGKEL-PWDGKTFGRLKVRGPAV 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 235 FNEYWnkpQETREAFTPDGWFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTW 314
Cdd:PRK06018 395 AAAYY---RVDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKW 471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2113536441 315 GQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK06018 472 DERPLLIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
4-371 |
3.23e-38 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 144.25 E-value: 3.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNLSA-MVTAliDEWSWTKS------DCILHVLPLHHVHGVVNKLLCPLWVGAtCVMLPEfSPK 76
Cdd:PRK08751 215 YTGGTTGVAKGAMLTHRNLVAnMQQA--HQWLAGTGkleegcEVVITALPLYHIFALTANGLVFMKIGG-CNHLIS-NPR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 77 EVWEHFLSTDSRSINVFMAVPTIYSKLidyyeshLAKPGIK--DFvkamcqQKIRLMVSGSSALPVPTLERWREITGHTL 154
Cdd:PRK08751 291 DMPGFVKELKKTRFTAFTGVNTLFNGL-------LNTPGFDqiDF------SSLKMTLGGGMAVQRSVAERWKQVTGLTL 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 155 LERYGMTEIG-MALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPA 233
Cdd:PRK08751 358 VEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIK-----------------DDAGTVLAIG---EIGELCIKGPQ 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 234 VFNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDS 312
Cdd:PRK08751 418 VMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFvYIVDRKK-DMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDE 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2113536441 313 TWGQRVSAIVKLRDgHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK08751 497 KSGEIVKVVIVKKD-PALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
2-368 |
4.15e-38 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 143.80 E-value: 4.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLS---AMVTALIDewsWTKSD--CIlhVLPLHHVHGVVNKLLCPLWVGATCV-MLPEFSP 75
Cdd:PRK08315 204 IQYTSGTTGFPKGATLTHRNILnngYFIGEAMK---LTEEDrlCI--PVPLYHCFGMVLGNLACVTHGATMVyPGEGFDP 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 76 KEVwehfLST--DSRSINVFmAVPTIYSKLIDYYE------SHLaKPGIkdfvkamcqqkirlMvSGSSAlPVPTLER-- 145
Cdd:PRK08315 279 LAT----LAAveEERCTALY-GVPTMFIAELDHPDfarfdlSSL-RTGI--------------M-AGSPC-PIEVMKRvi 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 146 ----WREITghtllERYGMTEigmalTNPL------NGP---RVpGSVGNPFPGVGVRIateipqkegssytVHAEgdaA 212
Cdd:PRK08315 337 dkmhMSEVT-----IAYGMTE-----TSPVstqtrtDDPlekRV-TTVGRALPHLEVKI-------------VDPE---T 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 213 GTEVFPGfedREGELQVRGPAVFNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSYW-ILGRTSvDIIKSGGYKISALEV 291
Cdd:PRK08315 390 GETVPRG---EQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMHTGDLAVMDEEGYVnIVGRIK-DMIIRGGENIYPREI 465
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2113536441 292 ERHLLAHPSIADVAVIGAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINK 368
Cdd:PRK08315 466 EEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQK 542
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
2-374 |
9.33e-38 |
|
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: 141.70 E-value: 9.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPE-FSPKEVWE 80
Cdd:cd05909 152 ILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTGCLWLPLLSGIKVVFHPNpLDYKKIPE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 hflSTDSRSINVFMAVPTIYSklidyyeshlakpGIKDFVKAMCQQKIRLMVSGSSALPVPTLERWREITGHTLLERYGM 160
Cdd:cd05909 232 ---LIYDKKATILLGTPTFLR-------------GYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGT 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TEIG--MALTNPlNGPRVPGSVGNPFPGVGVRIateipqkegssytVHAEGdaaGTEVFPGfedREGELQVRGPAVFNEY 238
Cdd:cd05909 296 TECSpvISVNTP-QSPNKEGTVGRPLPGMEVKI-------------VSVET---HEEVPIG---EGGLLLVRGPNVMLGY 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 239 WNKPQETREAFTpDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAH-PSIADVAVIGAPDSTWGQ 316
Cdd:cd05909 356 LNEPELTSFAFG-DGWYDTGDIGKIDGEGFlTITGRLS-RFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDGRKGE 433
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2113536441 317 RvsaIVKLRDGHTLSLKKLKEWGRAVMAP-YCIPAELIRVEEIPRNQMGKINKKQLLAL 374
Cdd:cd05909 434 K---IVLLTTTTDTDPSSLNDILKNAGISnLAKPSYIHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
2-306 |
9.43e-38 |
|
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: 140.09 E-value: 9.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVnKLLCPLWVGATCVMLPEfSPKEVWEH 81
Cdd:TIGR01733 125 VIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPE-DEERDDAA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 FLST--DSRSINVFMAVPTIYSKLIDyyESHLAKPGikdfvkamcqqkIRLMVSGSSALPVPTLERWREITGHT-LLERY 158
Cdd:TIGR01733 203 LLAAliAEHPVTVLNLTPSLLALLAA--ALPPALAS------------LRLVILGGEALTPALVDRWRARGPGArLINLY 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 159 GMTE-----IGMALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPA 233
Cdd:TIGR01733 269 GPTEttvwsTATLVDPDDAPRESPVPIGRPLANTRLYVL-----------------DDDLRPVPVG---VVGELYIGGPG 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 234 VFNEYWNKPQETREAFTPDG--------WFRTGDTAVYKDNSYW-ILGRTSvDIIKSGGYKISALEVERHLLAHPSIADV 304
Cdd:TIGR01733 329 VARGYLNRPELTAERFVPDPfaggdgarLYRTGDLVRYLPDGNLeFLGRID-DQVKIRGYRIELGEIEAALLRHPGVREA 407
|
..
gi 2113536441 305 AV 306
Cdd:TIGR01733 408 VV 409
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
4-375 |
9.98e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 142.54 E-value: 9.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQN--LSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLwVGATCVML-PEFSPKEVWE 80
Cdd:PRK07008 183 YTSGTTGNPKGALYSHRStvLHAYGAALPDAMGLSARDAVLPVVPMFHVNAWGLPYSAPL-TGAKLVLPgPDLDGKSLYE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 HFlstDSRSINVFMAVPTIYSKLIdyyeSHLAKPGIKdFvkamcqQKIRLMVSGSSALPVPTLERWREITGHTLLERYGM 160
Cdd:PRK07008 262 LI---EAERVTFSAGVPTVWLGLL----NHMREAGLR-F------STLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGM 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TEI---GMALTNPLNGPRVPGSV--------GNPFPGVGVRIAteipqkegssytvhaegDAAGTEVfPGFEDREGELQV 229
Cdd:PRK07008 328 TEMsplGTLCKLKWKHSQLPLDEqrkllekqGRVIYGVDMKIV-----------------GDDGREL-PWDGKAFGDLQV 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 230 RGPAVFNEYWnkpqetREAFTP--DGWFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVAVI 307
Cdd:PRK07008 390 RGPWVIDRYF------RGDASPlvDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACI 463
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113536441 308 GAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLLALF 375
Cdd:PRK07008 464 ACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQF 531
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
1-365 |
1.01e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 142.33 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNL--SAM-------VTALIDEWSWTKSDC------ILHVLPLHHVHG---VVNKLLCplw 62
Cdd:PRK07798 167 YLLYTGGTTGMPKGVMWRQEDIfrVLLggrdfatGEPIEDEEELAKRAAagpgmrRFPAPPLMHGAGqwaAFAALFS--- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 63 vGATCVMLP--EFSPKEVWEhflSTDSRSINVF------MAVPtiyskLIDyyesHLAKPGIKDFvkamcqQKIRLMVSG 134
Cdd:PRK07798 244 -GQTVVLLPdvRFDADEVWR---TIEREKVNVItivgdaMARP-----LLD----ALEARGPYDL------SSLFAIASG 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 135 SSALPVPTLERWREITGH-TLLERYGMTEIG-MALTNPLNGPRVPGsvGNPF-PGVGVRIAteipqkegssytvhaegDA 211
Cdd:PRK07798 305 GALFSPSVKEALLELLPNvVLTDSIGSSETGfGGSGTVAKGAVHTG--GPRFtIGPRTVVL-----------------DE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 212 AGTEVFPGfEDREGELQVRGPaVFNEYWNKPQETREAF-TPDG--WFRTGDTA-VYKDNSYWILGRTSVdIIKSGGYKIS 287
Cdd:PRK07798 366 DGNPVEPG-SGEIGWIARRGH-IPLGYYKDPEKTAETFpTIDGvrYAIPGDRArVEADGTITLLGRGSV-CINTGGEKVF 442
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113536441 288 ALEVERHLLAHPSIADVAVIGAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGK 365
Cdd:PRK07798 443 PEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
4-366 |
2.57e-37 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 141.57 E-value: 2.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQnlsAMVTALID-EWswtksdcilhVLPLHH------------VHGVVNKLLCPLWVGATCVML 70
Cdd:PRK04319 212 YTSGSTGKPKGVLHVHN---AMLQHYQTgKY----------VLDLHEddvywctadpgwVTGTSYGIFAPWLNGATNVID 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 71 -PEFSPkEVWEHFLstDSRSINVFMAVPTIYSKLIdyyeshlaKPGIkDFVKAMCQQKIRLMVSGSSALPvPTLERW-RE 148
Cdd:PRK04319 279 gGRFSP-ERWYRIL--EDYKVTVWYTAPTAIRMLM--------GAGD-DLVKKYDLSSLRHILSVGEPLN-PEVVRWgMK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 149 ITGHTLLERYGMTEIG-MALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPgfeDREGEL 227
Cdd:PRK04319 346 VFGLPIHDNWWMTETGgIMIANYPAMDIKPGSMGKPLPGIEAAIV-----------------DDQGNELPP---NRMGNL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 228 QVRG--PAVFNEYWNKPQETREAFTpDGWFRTGDTAvYKDNS--YWILGRTSvDIIKSGGYKISALEVERHLLAHPSIAD 303
Cdd:PRK04319 406 AIKKgwPSMMRGIWNNPEKYESYFA-GDWYVSGDSA-YMDEDgyFWFQGRVD-DVIKTSGERVGPFEVESKLMEHPAVAE 482
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113536441 304 VAVIGAPDSTWGQRVSAIVKLRDGHTLS--LKK-LKEWGRAVMAPYCIPAELIRVEEIPRNQMGKI 366
Cdd:PRK04319 483 AGVIGKPDPVRGEIIKAFVALRPGYEPSeeLKEeIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKI 548
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
2-373 |
3.26e-37 |
|
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: 143.07 E-value: 3.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHH---VHGvvnkLLCPLWVGATCVMLPE---FSP 75
Cdd:COG1020 622 VIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFdasVWE----IFGALLSGATLVLAPPearRDP 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 76 kEVWEHFLstDSRSINVFMAVPTIYSKLIDYYESHLAKPgikdfvkamcqqkiRLMVSGSSALPVPTLERWREITGHT-L 154
Cdd:COG1020 698 -AALAELL--ARHRVTVLNLTPSLLRALLDAAPEALPSL--------------RLVLVGGEALPPELVRRWRARLPGArL 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 155 LERYGMTE------IGMALTNPLNGPRVPgsVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGFedrEGELQ 228
Cdd:COG1020 761 VNLYGPTEttvdstYYEVTPPDADGGSVP--IGRPIANTRVYVL-----------------DAHLQPVPVGV---PGELY 818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 229 VRGPAVFNEYWNKPQETREAFTPDG-------WFRTGDTAVYKDN---SYwiLGRtsVDI-IKSGGYKISALEVERHLLA 297
Cdd:COG1020 819 IGGAGLARGYLNRPELTAERFVADPfgfpgarLYRTGDLARWLPDgnlEF--LGR--ADDqVKIRGFRIELGEIEAALLQ 894
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113536441 298 HPSIADVAVIGAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLLA 373
Cdd:COG1020 895 HPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPA 970
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
2-373 |
9.89e-37 |
|
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: 138.66 E-value: 9.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTH-----QNLSAMVTALIDEWSwtKSDCILHVLPLHHV--HGVVNKllcPLWVGATCVMLPEFS 74
Cdd:cd05929 130 MLYSGGTTGRPKGIKRGLpggppDNDTLMAAALGFGPG--ADSVYLSPAPLYHAapFRWSMT---ALFMGGTLVLMEKFD 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 75 PkevwEHFLSTDSR-SINVFMAVPTIYSKLIDYYEshlAKPGIKDFvkamcqQKIRLMVSGSSALPVPTLERWREITGHT 153
Cdd:cd05929 205 P----EEFLRLIERyRVTFAQFVPTMFVRLLKLPE---AVRNAYDL------SSLKRVIHAAAPCPPWVKEQWIDWGGPI 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 154 LLERYGMTE-IGMALTNPLNGPRVPGSVGNPFPGvGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGP 232
Cdd:cd05929 272 IWEYYGGTEgQGLTIINGEEWLTHPGSVGRAVLG-KVHIL-----------------DEDGNEVPPG---EIGEVYFANG 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 233 AVFnEYWNKPQETREAFTPDGWFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDS 312
Cdd:cd05929 331 PGF-EYTNDPEKTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDE 409
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2113536441 313 TWGQRVSAIV---KLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLLA 373
Cdd:cd05929 410 ELGQRVHAVVqpaPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
4-366 |
1.30e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 138.76 E-value: 1.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVH---GVVNKLlcplWVGATCVMLPEFSPKEVWE 80
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTLVHSLflyGAISTL----YVGQTVHLMRKFIPNQVLD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 HfLSTDSrsINVFMAVPTIYSKLIDyyeshlakpgikdfVKAMCQQKIRLMVSGSSaLPVPTLERWREITGH-TLLERYG 159
Cdd:PRK07638 226 K-LETEN--ISVMYTVPTMLESLYK--------------ENRVIENKMKIISSGAK-WEAEAKEKIKNIFPYaKLYEFYG 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 160 MTEIG-MALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPAVFNEY 238
Cdd:PRK07638 288 ASELSfVTALVDEESERRPNSVGRPFHNVQVRIC-----------------NEAGEEVQKG---EIGTVYVKSPQFFMGY 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 239 WNKPQETREaFTPDGWFRTGDTA-VYKDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQR 317
Cdd:PRK07638 348 IIGGVLARE-LNADGWMTVRDVGyEDEEGFIYIVGREK-NMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEK 425
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2113536441 318 VSAIVKlrdGHTLSlKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKI 366
Cdd:PRK07638 426 PVAIIK---GSATK-QQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKI 470
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
2-375 |
1.85e-36 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 139.53 E-value: 1.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQN--LSAMVTALIDEWSWTKSDCILHVLPLHHV--HGVvnkllcPL--WVGATCVMLP--EF 73
Cdd:PRK05620 186 ICYSTGTTGAPKGVVYSHRSlyLQSLSLRTTDSLAVTHGESFLCCVPIYHVlsWGV------PLaaFMSGTPLVFPgpDL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 74 SPkEVWEHFLSTDSRsiNVFMAVPTIYSKLIDYYESHlaKPgikdfvKAMCQQKIrlmVSGSSALPVPTLERWREITGHT 153
Cdd:PRK05620 260 SA-PTLAKIIATAMP--RVAHGVPTLWIQLMVHYLKN--PP------ERMSLQEI---YVGGSAVPPILIKAWEERYGVD 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 154 LLERYGMTEigmalTNPLngprvpGSVGNPFPGVG--VRIATEIPQKE---GSSYTVHAEGdaagtEVFPGFEDREGELQ 228
Cdd:PRK05620 326 VVHVWGMTE-----TSPV------GTVARPPSGVSgeARWAYRVSQGRfpaSLEYRIVNDG-----QVMESTDRNEGEIQ 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 229 VRGPAVFNEYWNKPQET----------------REAFTPDGWFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEVE 292
Cdd:PRK05620 390 VRGNWVTASYYHSPTEEgggaastfrgedvedaNDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLE 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 293 RHLLAHPSIADVAVIGAPDSTWGQRVSAIVKLRDGHTLSL---KKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKK 369
Cdd:PRK05620 470 NYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRetaERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKK 549
|
....*.
gi 2113536441 370 QLLALF 375
Cdd:PRK05620 550 DLRQHL 555
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
2-308 |
4.25e-36 |
|
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: 136.72 E-value: 4.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWvGATCVMLpefSPKevweh 81
Cdd:cd17640 93 IIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIWHSYERSAEYFIFAC-GCSQAYT---SIR----- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 FLSTDSRSIN--VFMAVPTIYSKL-IDYYESHLAKPGIKDFV--KAMCQQKIRLMVSGSSALPvPTLERWREITGHTLLE 156
Cdd:cd17640 164 TLKDDLKRVKphYIVSVPRLWESLySGIQKQVSKSSPIKQFLflFFLSGGIFKFGISGGGALP-PHVDTFFEAIGIEVLN 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 157 RYGMTEIGMALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGFEdrEGELQVRGPAVFN 236
Cdd:cd17640 243 GYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIV-----------------DPEGNVVLPPGE--KGIVWVRGPQVMK 303
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2113536441 237 EYWNKPQETREAFTPDGWFRTGDTA-VYKDNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVAVIG 308
Cdd:cd17640 304 GYYKNPEATSKVLDSDGWFNTGDLGwLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1-368 |
6.79e-36 |
|
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: 135.72 E-value: 6.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLP-EFSPKEVW 79
Cdd:cd05973 92 VMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEgGFSVESTW 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 80 ---EHFLSTDsrsinvFMAVPTIYSKLIdyyeshlakpgiKDFVKAMCQQKIRLMVSGSSALPV-PTLERW-REITGHTL 154
Cdd:cd05973 172 rviERLGVTN------LAGSPTAYRLLM------------AAGAEVPARPKGRLRRVSSAGEPLtPEVIRWfDAALGVPI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 155 LERYGMTEIGMALTN--PLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQV--- 229
Cdd:cd05973 234 HDHYGQTELGMVLANhhALEHPVHAGSAGRAMPGWRVAVL-----------------DDDGDELGPG---EPGRLAIdia 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 230 RGPAV-FNEYWNKPQETreaftPDG-WFRTGDTA-VYKDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAV 306
Cdd:cd05973 294 NSPLMwFRGYQLPDTPA-----IDGgYYLTGDTVeFDPDGSFSFIGRAD-DVITMSGYRIGPFDVESALIEHPAVAEAAV 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2113536441 307 IGAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAV---MAPYCIPAELIRVEEIPRNQMGKINK 368
Cdd:cd05973 368 IGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVkkrLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
2-371 |
9.34e-36 |
|
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: 136.25 E-value: 9.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLhhvhGV---VNKLLCPLWVGATCVMLPEFSPKEV 78
Cdd:cd17646 143 VIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPL----SFdvsVWELFWPLVAGARLVVARPGGHRDP 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 79 wEHFLST-DSRSINVFMAVPTIYSKLIDyyeshLAKPGikdfvkamCQQKIRLMVSGSSALPVPTLERWREITGHTLLER 157
Cdd:cd17646 219 -AYLAALiREHGVTTCHFVPSMLRVFLA-----EPAAG--------SCASLRRVFCSGEALPPELAARFLALPGAELHNL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTE--IGM---ALTNPLNGPRVPgsVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGFEdreGELQVRGP 232
Cdd:cd17646 285 YGPTEaaIDVthwPVRGPAETPSVP--IGRPVPNTRLYVL-----------------DDALRPVPVGVP---GELYLGGV 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 233 AVFNEYWNKPQETREAFTPDgWF-------RTGDTAVYK-DNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADV 304
Cdd:cd17646 343 QLARGYLGRPALTAERFVPD-PFgpgsrmyRTGDLARWRpDGALEFLGRSD-DQVKIRGFRVEPGEIEAALAAHPAVTHA 420
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113536441 305 AVIGAPDSTWGQRVSAIVKLRDGHT-LSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd17646 421 VVVARAAPAGAARLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
2-371 |
1.61e-35 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 136.43 E-value: 1.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQN---LSAMVTALIDewsWTKSDCILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEFSPKEV 78
Cdd:PRK06155 185 ILYTSGTTGPSKGVCCPHAQfywWGRNSAEDLE---IGADDVLYTTLPLFHTNAL-NAFFQALLAGATYVLEPRFSASGF 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 79 WEHFLSTDSRSINVFMAVPTIYsklidyyeshLAKPGIKDfvkamcQQKIRLMVSGSSALPVPTLERWREITGHTLLERY 158
Cdd:PRK06155 261 WPAVRRHGATVTYLLGAMVSIL----------LSQPARES------DRAHRVRVALGPGVPAALHAAFRERFGVDLLDGY 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 159 GMTEIGMALTNPLNGPRvPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRG--PAVF- 235
Cdd:PRK06155 325 GSTETNFVIAVTHGSQR-PGSMGRLAPGFEARVV-----------------DEHDQELPDG---EPGELLLRAdePFAFa 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 236 NEYWNKPQETREAFTpDGWFRTGDTAVYK-DNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTW 314
Cdd:PRK06155 384 TGYFGMPEKTVEAWR-NLWFHTGDRVVRDaDGWFRFVDRIK-DAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELG 461
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2113536441 315 GQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK06155 462 EDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-371 |
5.01e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 137.01 E-value: 5.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLhHVHGVVNKLLCPLWVGATCVM------LPEFSP 75
Cdd:PRK12316 2151 VIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSF-SFDGAHEQWFHPLLNGARVLIrddelwDPEQLY 2229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 76 KEVWEHFLSTdsrsinvfMAVPTIYSKLIdyyESHLAKPGikdfvkamCQQKIRLMVSGSSALPVPTLER-WREITGHTL 154
Cdd:PRK12316 2230 DEMERHGVTI--------LDFPPVYLQQL---AEHAERDG--------RPPAVRVYCFGGEAVPAASLRLaWEALRPVYL 2290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 155 LERYGMTEigmALTNPLN---GPRVPGsvGNPFPGVGVRIATEipqkegSSYTVHAEGDAAGTEVFpgfedreGELQVRG 231
Cdd:PRK12316 2291 FNGYGPTE---AVVTPLLwkcRPQDPC--GAAYVPIGRALGNR------RAYILDADLNLLAPGMA-------GELYLGG 2352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 232 PAVFNEYWNKPQETREAFTPDGW-------FRTGDTAVYK-DNSYWILGRtsVD-IIKSGGYKISALEVERHLLAHPSIA 302
Cdd:PRK12316 2353 EGLARGYLNRPGLTAERFVPDPFsasgerlYRTGDLARYRaDGVVEYLGR--IDhQVKIRGFRIELGEIEARLQAHPAVR 2430
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2113536441 303 DVAVIgAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK12316 2431 EAVVV-AQDGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKAL 2498
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
1-375 |
8.54e-35 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 131.32 E-value: 8.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTA----LIDEWSWtksdciLHVLPLHHVHGVvNKLLCPLWVGATCVMLpefspk 76
Cdd:PRK07824 39 LVVATSGTTGTPKGAMLTAAALTASADAthdrLGGPGQW------LLALPAHHIAGL-QVLVRSVIAGSEPVEL------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 77 EVWEHFLSTDSRSINVFMAVPTIYSKLIdyyESHLAKpGIKDFVKAMCQQKIRLMVSGSSALPVPTLERWREItGHTLLE 156
Cdd:PRK07824 106 DVSAGFDPTALPRAVAELGGGRRYTSLV---PMQLAK-ALDDPAATAALAELDAVLVGGGPAPAPVLDAAAAA-GINVVR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 157 RYGMTEIGmaltnplngprvPGSV--GNPFPGVGVRIAteipqkegssytvhaegdaagtevfpgfedrEGELQVRGPAV 234
Cdd:PRK07824 181 TYGMSETS------------GGCVydGVPLDGVRVRVE-------------------------------DGRIALGGPTL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 235 FNEYWNKPQEtrEAFTPDGWFRTGDTAVYKDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTW 314
Cdd:PRK07824 218 AKGYRNPVDP--DPFAEPGWFRTDDLGALDDGVLTVLGRAD-DAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRL 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2113536441 315 GQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLLALF 375
Cdd:PRK07824 295 GQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRRF 355
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
2-259 |
1.04e-34 |
|
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: 133.88 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEW----SWTKSDCILHVLPLHHV--HGVVNKLLCplwVGAtCVmlpefsp 75
Cdd:cd05927 119 ICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILeilnKINPTDVYISYLPLAHIfeRVVEALFLY---HGA-KI------- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 76 kevweHFLSTDSRSI---------NVFMAVPTIYSKLID-YYESHLAKPGIKDF-------------------------- 119
Cdd:cd05927 188 -----GFYSGDIRLLlddikalkpTVFPGVPRVLNRIYDkIFNKVQAKGPLKRKlfnfalnyklaelrsgvvraspfwdk 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 120 -----VKAMCQQKIRLMVSGSSALPVPTLERWREITGHTLLERYGMTEI--GMALTNPlnGPRVPGSVGNPFPGVGVRIA 192
Cdd:cd05927 263 lvfnkIKQALGGNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECtaGATLTLP--GDTSVGHVGGPLPCAEVKLV 340
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2113536441 193 tEIPQKEgssYtvhaegDAAGtevfpgfEDREGELQVRGPAVFNEYWNKPQETREAFTPDGWFRTGD 259
Cdd:cd05927 341 -DVPEMN---Y------DAKD-------PNPRGEVCIRGPNVFSGYYKDPEKTAEALDEDGWLHTGD 390
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
5-375 |
1.82e-34 |
|
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: 133.18 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 5 TSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEfspkevwEHFLS 84
Cdd:cd05906 175 TSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLRAVYLGCQQVHVPT-------EEILA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 85 --------TDSRSINVFMAVPTIYSKLIDYYESHLAKPGikDFvkamcqQKIRLMVSGSSALPVPTLERWREitghtLLE 156
Cdd:cd05906 248 dplrwldlIDRYRVTITWAPNFAFALLNDLLEEIEDGTW--DL------SSLRYLVNAGEAVVAKTIRRLLR-----LLE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 157 RY-----------GMTEI--GMALTNPLNGPRVPG-----SVGNPFPGVGVRIateipqkegssytVHAEGdaagtEVFP 218
Cdd:cd05906 315 PYglppdairpafGMTETcsGVIYSRSFPTYDHSQalefvSLGRPIPGVSMRI-------------VDDEG-----QLLP 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 219 gfEDREGELQVRGPAVFNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSYWILGRTSvDIIKSGGYKISALEVERHL--- 295
Cdd:cd05906 377 --EGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLGFLDNGNLTITGRTK-DTIIVNGVNYYSHEIEAAVeev 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 296 --LAHPSIADVAVIGAPDST-------------WGQRVSAIVKLRDghtlslKKLKEWGRAvmAPYCIPaelIRVEEIPR 360
Cdd:cd05906 454 pgVEPSFTAAFAVRDPGAETeelaiffvpeydlQDALSETLRAIRS------VVSREVGVS--PAYLIP---LPKEEIPK 522
|
410
....*....|....*
gi 2113536441 361 NQMGKINKKQLLALF 375
Cdd:cd05906 523 TSLGKIQRSKLKAAF 537
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
1-373 |
3.78e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 132.50 E-value: 3.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEvwe 80
Cdd:PRK07867 156 MLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAAGASIALRRKFSASG--- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 hFLStDSRSINVFMAvpTIYSKLIDYYESHLAKPGIKDfvkamcqQKIRLMVsGSSALPvPTLERWREITGHTLLERYGM 160
Cdd:PRK07867 233 -FLP-DVRRYGATYA--NYVGKPLSYVLATPERPDDAD-------NPLRIVY-GNEGAP-GDIARFARRFGCVVVDGFGS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TEIGMALTNPLNGPrvPGSVGNPFPGVGVR---IATEIPQkegssytvhAEGDAAGTevfPGFEDREGEL-QVRGPAVFN 236
Cdd:PRK07867 300 TEGGVAITRTPDTP--PGALGPLPPGVAIVdpdTGTECPP---------AEDADGRL---LNADEAIGELvNTAGPGGFE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 237 EYWNKPQETREAFTpDGWFRTGDTAvYKD-NSY-WILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTW 314
Cdd:PRK07867 366 GYYNDPEADAERMR-GGVYWSGDLA-YRDaDGYaYFAGRLG-DWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVV 442
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2113536441 315 GQRVSAIVKLRDGHTLSLKKLKEW--GRAVMAPYCIPAeLIRV-EEIPRNQMGKINKKQLLA 373
Cdd:PRK07867 443 GDQVMAALVLAPGAKFDPDAFAEFlaAQPDLGPKQWPS-YVRVcAELPRTATFKVLKRQLSA 503
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
2-371 |
5.26e-34 |
|
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: 130.45 E-value: 5.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHhVHGVVNKLLCPLWVGATCVMLPEfspkevweh 81
Cdd:cd17652 98 VIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSRVLQFASPS-FDASVWELLMALLAGATLVLAPA--------- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 flstdsrsiNVFMAVPTIYSKLIDYYESHLA-KPGIKDFVKAMCQQKIRLMVSGSSALPVPTLERWReiTGHTLLERYGM 160
Cdd:cd17652 168 ---------EELLPGEPLADLLREHRITHVTlPPAALAALPPDDLPDLRTLVVAGEACPAELVDRWA--PGRRMINAYGP 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TE--IGMALTNPLNGPRVPgSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGFEdreGELQVRGPAVFNEY 238
Cdd:cd17652 237 TEttVCATMAGPLPGGGVP-PIGRPVPGTRVYVL-----------------DARLRPVPPGVP---GELYIAGAGLARGY 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 239 WNKPQETREAFTPDGW-------FRTGDTAVYK-DNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAP 310
Cdd:cd17652 296 LNRPGLTAERFVADPFgapgsrmYRTGDLARWRaDGQLEFLGRAD-DQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRD 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2113536441 311 DSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd17652 375 DRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1-371 |
8.78e-34 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 131.42 E-value: 8.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNkLLCPLWVGATCVMLPEFSPKEVWE 80
Cdd:PRK13382 200 VILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIVAPMFHAWGFSQ-LVLAASLACTIVTRRRFDPEATLD 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 hfLSTDSRSINVFMaVPTIYSKLIDYYESHLAKPGikdfvkamcQQKIRLMVSGSSALPVPTLERWREITGHTLLERYGM 160
Cdd:PRK13382 279 --LIDRHRATGLAV-VPVMFDRIMDLPAEVRNRYS---------GRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNA 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TEIGMALT-NPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPAVFNEYw 239
Cdd:PRK13382 347 TEAGMIATaTPADLRAAPDTAGRPAEGTEIRIL-----------------DQDFREVPTG---EVGTIFVRNDTQFDGY- 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 240 nKPQETREafTPDGWFRTGDTAVYKDNS-YWILGRtSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQRV 318
Cdd:PRK13382 406 -TSGSTKD--FHDGFMASGDVGYLDENGrLFVVGR-DDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRL 481
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2113536441 319 SAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK13382 482 AAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
2-371 |
6.79e-33 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 128.21 E-value: 6.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLhHVHGVVNKLLCPLWVGATCVMLPEfspKEVW-- 79
Cdd:cd17655 142 VIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASI-SFDASVTEIFASLLSGNTLYIVRK---ETVLdg 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 80 EHFLST-DSRSINVFMAVPTiysklidyYESHLAKPGIKDFVkamcqqKIRLMVSGSSALPVPTLERWREITGH--TLLE 156
Cdd:cd17655 218 QALTQYiRQNRITIIDLTPA--------HLKLLDAADDSEGL------SLKHLIVGGEALSTELAKKIIELFGTnpTITN 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 157 RYGMTE------IGMALTNPLNGPRVPgsVGNPFPGVGVRIATEI--PQKEGSSytvhaegdaagtevfpgfedreGELQ 228
Cdd:cd17655 284 AYGPTEttvdasIYQYEPETDQQVSVP--IGKPLGNTRIYILDQYgrPQPVGVA----------------------GELY 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 229 VRGPAVFNEYWNKPQETREAFTPDGW------FRTGDTAVY-KDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSI 301
Cdd:cd17655 340 IGGEGVARGYLNRPELTAEKFVDDPFvpgermYRTGDLARWlPDGNIEFLGRID-HQVKIRGYRIELGEIEARLLQHPDI 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2113536441 302 ADVAVIGAPDSTWGQRVSA-IVKLRDghtLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd17655 419 KEAVVIARKDEQGQNYLCAyIVSEKE---LPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
2-375 |
1.53e-32 |
|
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: 127.72 E-value: 1.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTAL---IDEWSwTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLP------- 71
Cdd:cd17639 93 IMYTSGSTGNPKGVMLTHGNLVAGIAGLgdrVPELL-GPDDRYLAYLPLAHIFELAAENVCLYRGGTIGYGSPrtltdks 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 72 ---------EFSPK------EVWEHFLSTDSRSINvfmAVPTIYSKLIDY-YESHLA--KPGIKDF---------VKAMC 124
Cdd:cd17639 172 krgckgdltEFKPTlmvgvpAIWDTIRKGVLAKLN---PMGGLKRTLFWTaYQSKLKalKEGPGTPlldelvfkkVRAAL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 125 QQKIRLMVSGSSALPVPTlERWREITGHTLLERYGMTEI--GMALTNPlnGPRVPGSVGNPFPGVGVRIaTEIPqkEGSS 202
Cdd:cd17639 249 GGRLRYMLSGGAPLSADT-QEFLNIVLCPVIQGYGLTETcaGGTVQDP--GDLETGRVGPPLPCCEIKL-VDWE--EGGY 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 203 YTvhaegDAAgtevfpgfEDReGELQVRGPAVFNEYWNKPQETREAFTPDGWFRTGDTA-VYKDNSYWILGRTSvDIIKS 281
Cdd:cd17639 323 ST-----DKP--------PPR-GEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGeFHPDGTLKIIDRKK-DLVKL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 282 --GGYkiSALE-VERHLLAHPSIADVAVIGAPDSTwgqRVSAIVklrdghTLSLKKLKEWGRAVMAPYCIPAELI---RV 355
Cdd:cd17639 388 qnGEY--IALEkLESIYRSNPLVNNICVYADPDKS---YPVAIV------VPNEKHLTKLAEKHGVINSEWEELCedkKL 456
|
410 420
....*....|....*....|
gi 2113536441 356 EEIPRNQMGKINKKQLLALF 375
Cdd:cd17639 457 QKAVLKSLAETARAAGLEKF 476
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
4-373 |
2.18e-32 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 127.40 E-value: 2.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNLSAMVTALID----EWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEVW 79
Cdd:PLN02246 186 YSSGTTGLPKGVMLTHKGLVTSVAQQVDgenpNLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILIMPKFEIGALL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 80 EhflSTDSRSINVFMAVPTIYSKLidyyeshlAKpgiKDFVKAMCQQKIRLMVSGSSALPvPTLER--WREITGHTLLER 157
Cdd:PLN02246 266 E---LIQRHKVTIAPFVPPIVLAI--------AK---SPVVEKYDLSSIRMVLSGAAPLG-KELEDafRAKLPNAVLGQG 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTEIGMALTNPLngprvpGSVGNPFPgvgvriateipQKEGSSYTV--HAEGDAAGTEVfpGFE---DREGELQVRGP 232
Cdd:PLN02246 331 YGMTEAGPVLAMCL------AFAKEPFP-----------VKSGSCGTVvrNAELKIVDPET--GASlprNQPGEICIRGP 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 233 AVFNEYWNKPQETREAFTPDGWFRTGDTA-VYKDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPD 311
Cdd:PLN02246 392 QIMKGYLNDPEATANTIDKDGWLHTGDIGyIDDDDELFIVDRLK-ELIKYKGFQVAPAELEALLISHPSIADAAVVPMKD 470
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2113536441 312 STWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLLA 373
Cdd:PLN02246 471 EVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRA 532
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
2-373 |
3.11e-32 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 127.05 E-value: 3.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDE---W-SWTKSDCILHVLPLHHVHGVVNKLLCpLWVGATCVMLPE--FSP 75
Cdd:PRK05857 174 MIFTSGTTGEPKAVLLANRTFFAVPDILQKEglnWvTWVVGETTYSPLPATHIGGLWWILTC-LMHGGLCVTGGEntTSL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 76 KEVwehflsTDSRSINVFMAVPTIYSKLIdyYESHLAkpgikdfvkAMCQQKIRLMVSGSSALPVPTLeRWREITGHTLL 155
Cdd:PRK05857 253 LEI------LTTNAVATTCLVPTLLSKLV--SELKSA---------NATVPSLRLVGYGGSRAIAADV-RFIEATGVRTA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 156 ERYGMTEIG-MALTNPLNGPRVP----GSVGNPFPGVGVRIATEipqkEGSSYTVHAEGDAAGTevfpgfedreGELQVR 230
Cdd:PRK05857 315 QVYGLSETGcTALCLPTDDGSIVkieaGAVGRPYPGVDVYLAAT----DGIGPTAPGAGPSASF----------GTLWIK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 231 GPAVFNEYWNKPQETREAFTpDGWFRTGD-TAVYKDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGA 309
Cdd:PRK05857 381 SPANMLGYWNNPERTAEVLI-DGWVNTGDlLERREDGFFYIKGRSS-EMIICGGVNIAPDEVDRIAEGVSGVREAACYEI 458
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2113536441 310 PDSTWGQRVS-AIVKLRDGHTLSLKKLKewgRAVMAPY-------CIPAELIRVEEIPRNQMGKINKKQLLA 373
Cdd:PRK05857 459 PDEEFGALVGlAVVASAELDESAARALK---HTIAARFrresepmARPSTIVIVTDIPRTQSGKVMRASLAA 527
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
1-374 |
3.79e-32 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 128.12 E-value: 3.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPefSPkevwe 80
Cdd:PRK08633 786 TIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLPLLEGIKVVYHP--DP----- 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 hflsTDSRSI---------NVFMAVPTIyskLIDYYESHLAKPgiKDFvkamcqQKIRLMVSGSSALPVPTLERWREITG 151
Cdd:PRK08633 859 ----TDALGIaklvakhraTILLGTPTF---LRLYLRNKKLHP--LMF------ASLRLVVAGAEKLKPEVADAFEEKFG 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 152 HTLLERYGMTEigmalTNP---LNGPRV------------PGSVGNPFPGVGVRIateipqkegssytVHAEgdaAGTEV 216
Cdd:PRK08633 924 IRILEGYGATE-----TSPvasVNLPDVlaadfkrqtgskEGSVGMPLPGVAVRI-------------VDPE---TFEEL 982
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 217 FPGfedREGELQVRGPAVFNEYWNKPQETREAFT---PDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKIS--ALE 290
Cdd:PRK08633 983 PPG---EDGLILIGGPQVMKGYLGDPEKTAEVIKdidGIGWYVTGDKGHLDEDGFlTITDRYS-RFAKIGGEMVPlgAVE 1058
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 291 VERHLLAHPSIADVAVIGAPDSTWGQRVSAIVKLRDGHTLSLKK-LKEWGravMAPYCIPAELIRVEEIPRNQMGKINKK 369
Cdd:PRK08633 1059 EELAKALGGEEVVFAVTAVPDEKKGEKLVVLHTCGAEDVEELKRaIKESG---LPNLWKPSRYFKVEALPLLGSGKLDLK 1135
|
....*..
gi 2113536441 370 QL--LAL 374
Cdd:PRK08633 1136 GLkeLAL 1142
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
1-373 |
3.89e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 126.68 E-value: 3.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEvwe 80
Cdd:PRK13388 154 MLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVASGAAVALPAKFSASG--- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 hFLStDSRSINV-FMavpTIYSKLIDYYeshLAKPGIKDfvkamcQQKIRLMVS-GSSALPvPTLERWREITGHTLLERY 158
Cdd:PRK13388 231 -FLD-DVRRYGAtYF---NYVGKPLAYI---LATPERPD------DADNPLRVAfGNEASP-RDIAEFSRRFGCQVEDGY 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 159 GMTEIGMALTNPLNGPrvPGSVGNPFPGVGV---RIATEIPQkegssytvhAEGDAAGTEVFPgfEDREGEL-QVRGPAV 234
Cdd:PRK13388 296 GSSEGAVIVVREPGTP--PGSIGRGAPGVAIynpETLTECAV---------ARFDAHGALLNA--DEAIGELvNTAGAGF 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 235 FNEYWNKPQETREAFTpDGWFRTGDTAvYKDNSYWIL--GRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDS 312
Cdd:PRK13388 363 FEGYYNNPEATAERMR-HGMYWSGDLA-YRDADGWIYfaGRTA-DWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDE 439
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113536441 313 TWGQRVSAIVKLRDGHTLSLKKLKEWGRA------VMAPycipaELIRV-EEIPRNQMGKINKKQLLA 373
Cdd:PRK13388 440 RVGDQVMAALVLRDGATFDPDAFAAFLAAqpdlgtKAWP-----RYVRIaADLPSTATNKVLKRELIA 502
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
2-366 |
8.64e-32 |
|
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: 126.59 E-value: 8.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLstHQNLSAMVTALI----------DEWSWTKSDC--------IlhvlplhhVHGvvnkllcPLWV 63
Cdd:TIGR02188 242 ILYTSGSTGKPKGVL--HTTGGYLLYAAMtmkyvfdikdGDIFWCTADVgwitghsyI--------VYG-------PLAN 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 64 GATCVML---PEF-SPKEVWEhflSTDSRSINVFMAVPTIYSKLIDYYESHLAKPGIKdfvkamcqqKIRLMvsGSSALP 139
Cdd:TIGR02188 305 GATTVMFegvPTYpDPGRFWE---IIEKHKVTIFYTAPTAIRALMRLGDEWVKKHDLS---------SLRLL--GSVGEP 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 140 V-PTLERW-REITGHT---LLERYGMTEIGMALTNPLNG--PRVPGSVGNPFPGVGVRIATEipqkEGSSYT-VHAEGDA 211
Cdd:TIGR02188 371 InPEAWMWyYKVVGKErcpIVDTWWQTETGGIMITPLPGatPTKPGSATLPFFGIEPAVVDE----EGNPVEgPGEGGYL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 212 AGTEVFPGfedregelQVRGpavfneYWNKPQETREAFTPD--GWFRTGDTAVY-KDNSYWILGRTSvDIIKSGGYKISA 288
Cdd:TIGR02188 447 VIKQPWPG--------MLRT------IYGDHERFVDTYFSPfpGYYFTGDGARRdKDGYIWITGRVD-DVINVSGHRLGT 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 289 LEVERHLLAHPSIADVAVIGAPDSTWGQRVSAIVKLRDGHTLSL---KKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGK 365
Cdd:TIGR02188 512 AEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDelrKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGK 591
|
.
gi 2113536441 366 I 366
Cdd:TIGR02188 592 I 592
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
2-371 |
1.90e-31 |
|
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: 124.24 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNlsamVTALIDEWSW---TKSDCILHVLPL------HHVHGvvnkllcPLWVGATCVMLPE 72
Cdd:cd12117 141 VMYTSGSTGRPKGVAVTHRG----VVRLVKNTNYvtlGPDDRVLQTSPLafdastFEIWG-------ALLNGARLVLAPK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 73 fspkevwEHFLSTDS-------RSINVFMAVPTIYSKLIDYYESHLAKpgikdfvkamcqqkIRLMVSGSSALPVPTLER 145
Cdd:cd12117 210 -------GTLLDPDAlgaliaeEGVTVLWLTAALFNQLADEDPECFAG--------------LRELLTGGEVVSPPHVRR 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 146 WREITGH-TLLERYGMTE-IGMALTNPLN-GPRVPGSV--GNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGf 220
Cdd:cd12117 269 VLAACPGlRLVNGYGPTEnTTFTTSHVVTeLDEVAGSIpiGRPIANTRVYVL-----------------DEDGRPVPPG- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 221 edREGELQVRGPAVFNEYWNKPQETREAFTPDGW------FRTGDTAVYK-DNSYWILGRTSvDIIKSGGYKISALEVER 293
Cdd:cd12117 331 --VPGELYVGGDGLALGYLNRPALTAERFVADPFgpgerlYRTGDLARWLpDGRLEFLGRID-DQVKIRGFRIELGEIEA 407
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113536441 294 HLLAHPSIADVAVIGAPDSTWGQRVSAIVKLRdgHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd12117 408 ALRAHPGVREAVVVVREDAGGDKRLVAYVVAE--GALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
4-371 |
2.73e-31 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 124.75 E-value: 2.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGvvnkllcplWV--------GATCVMLPEFSP 75
Cdd:PLN03102 193 YTSGTTADPKGVVISHRGAYLSTLSAIIGWEMGTCPVYLWTLPMFHCNG---------WTftwgtaarGGTSVCMRHVTA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 76 KEVWEHFlstDSRSINVFMAVPTIYSKLID---YYESHLAKPgikdfvkamcqqkIRLMVSGSSalPVPTLERWREITGH 152
Cdd:PLN03102 264 PEIYKNI---EMHNVTHMCCVPTVFNILLKgnsLDLSPRSGP-------------VHVLTGGSP--PPAALVKKVQRLGF 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 153 TLLERYGMTEIgmaltnplNGPRVPGSVGNPFPGVGVRIATEIPQKEGSSYTVHAEGDAAGTEVF---PGFEDREGELQV 229
Cdd:PLN03102 326 QVMHAYGLTEA--------TGPVLFCEWQDEWNRLPENQQMELKARQGVSILGLADVDVKNKETQesvPRDGKTMGEIVI 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 230 RGPAVFNEYWNKPQETREAFTpDGWFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGA 309
Cdd:PLN03102 398 KGSSIMKGYLKNPKATSEAFK-HGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAM 476
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2113536441 310 PDSTWGQRVSAIVKLRDGHT----------LSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PLN03102 477 PHPTWGETPCAFVVLEKGETtkedrvdklvTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
5-370 |
2.82e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 124.47 E-value: 2.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 5 TSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVvNKLLCPLWVGATCVMLPEF----SPKEVWE 80
Cdd:PRK06164 189 TSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGF-STLLGALAGGAPLVCEPVFdaarTARALRR 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 HflstdsRSINVFmAVPTIYSKLIDyyeshlAKPGIKDFVKAmcqqkiRLMVSGSSALPVPTLERWREITGHTLLERYGM 160
Cdd:PRK06164 268 H------RVTHTF-GNDEMLRRILD------TAGERADFPSA------RLFGFASFAPALGELAALARARGVPLTGLYGS 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 161 TEI-----GMALTNPLNGPRVPGsvGNPF-PGVGVRIAteipqkegssytvhaegDAAGTEVFPGFEdrEGELQVRGPAV 234
Cdd:PRK06164 329 SEVqalvaLQPATDPVSVRIEGG--GRPAsPEARVRAR-----------------DPQDGALLPDGE--SGEIEIRAPSL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 235 FNEYWNKPQETREAFTPDGWFRTGDTAVYK-DNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGApDST 313
Cdd:PRK06164 388 MRGYLDNPDATARALTDDGYFRTGDLGYTRgDGQFVYQTRMG-DSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA-TRD 465
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2113536441 314 WGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQ 370
Cdd:PRK06164 466 GKTVPVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESANGAKIQ 522
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1-371 |
3.81e-31 |
|
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: 123.61 E-value: 3.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHhVHGVVNKLLCPLWVGATCVMLPE---FSPKE 77
Cdd:cd17651 140 YVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLG-FDVSVQEIFSTLCAGATLVLPPEevrTDPPA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 VWeHFLSTDSRSInVFMavPTIYSKLIDYYESHLAKPGikdfvkamcqQKIRLMVSGSSALPV-PTLERW-REITGHTLL 155
Cdd:cd17651 219 LA-AWLDEQRISR-VFL--PTVALRALAEHGRPLGVRL----------AALRYLLTGGEQLVLtEDLREFcAGLPGLRLH 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 156 ERYGMTE----IGMALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRG 231
Cdd:cd17651 285 NHYGPTEthvvTALSLPGDPAAWPAPPPIGRPIDNTRVYVL-----------------DAALRPVPPG---VPGELYIGG 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 232 PAVFNEYWNKPQETREAFTPDGW------FRTGDTAVY-KDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADV 304
Cdd:cd17651 345 AGLARGYLNRPELTAERFVPDPFvpgarmYRTGDLARWlPDGELEFLGRAD-DQVKIRGFRIELGEIEAALARHPGVREA 423
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2113536441 305 AVIGAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd17651 424 VVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
2-309 |
6.78e-31 |
|
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: 122.96 E-value: 6.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATcVMLPEfspkevweh 81
Cdd:cd05932 142 LIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVL-VAFAE--------- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 flSTDSRSINVFMAVPT---------------IYSKLIDYYESHLAK-PGIKDFVK-----AMCQQKIRLMVSGSSALPV 140
Cdd:cd05932 212 --SLDTFVEDVQRARPTlffsvprlwtkfqqgVQDKIPQQKLNLLLKiPVVNSLVKrkvlkGLGLDQCRLAGCGSAPVPP 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 141 PTLERWREItGHTLLERYGMTEiGMALTNpLNGP--RVPGSVGNPFPGVGVRIateipqkegssytvhaegdaagtevfp 218
Cdd:cd05932 290 ALLEWYRSL-GLNILEAYGMTE-NFAYSH-LNYPgrDKIGTVGNAGPGVEVRI--------------------------- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 219 gfeDREGELQVRGPAVFNEYWNKPQETREAFTPDGWFRTGDT-AVYKDNSYWILGRTSvDIIK-SGGYKISALEVERHLL 296
Cdd:cd05932 340 ---SEDGEILVRSPALMMGYYKDPEATAEAFTADGFLRTGDKgELDADGNLTITGRVK-DIFKtSKGKYVAPAPIENKLA 415
|
330
....*....|...
gi 2113536441 297 AHPSIADVAVIGA 309
Cdd:cd05932 416 EHDRVEMVCVIGS 428
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
2-371 |
2.56e-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: 120.49 E-value: 2.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGvVNKLLCPLWVGATCVMLpefSPKEVWEH 81
Cdd:cd17653 110 IIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDAC-IGEIFSTLCNGGTLVLA---DPSDPFAH 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 flstDSRSINVFMAVPTIYSKLidyyeshlaKPgiKDFvkamcqQKIRLMVSGSSALPVPTLERWREitGHTLLERYGMT 161
Cdd:cd17653 186 ----VARTVDALMSTPSILSTL---------SP--QDF------PNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPT 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 162 EIGMALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVfpgFEDREGELQVRGPAVFNEYWNK 241
Cdd:cd17653 243 ECTISSTMTELLPGQPVTIGKPIPNSTCYIL-----------------DADLQPV---PEGVVGEICISGVQVARGYLGN 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 242 PQETREAFTPDGW------FRTGDTAVY-KDNSYWILGRTSVDiIKSGGYKISALEVERHLLA-HPSIADVAVIGAPDSt 313
Cdd:cd17653 303 PALTASKFVPDPFwpgsrmYRTGDYGRWtEDGGLEFLGREDNQ-VKVRGFRINLEEIEEVVLQsQPEVTQAAAIVVNGR- 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2113536441 314 wgqrvsaIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd17653 381 -------LVAFVTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
1-366 |
2.84e-30 |
|
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: 121.92 E-value: 2.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALI---------DEWsWTKSDCILHVLPLHHVHGvvnkllcPLWVGATCVML- 70
Cdd:cd17634 236 FILYTSGTTGKPKGVLHTTGGYLVYAATTMkyvfdygpgDIY-WCTADVGWVTGHSYLLYG-------PLACGATTLLYe 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 71 --PEF-SPKEVWEhflSTDSRSINVFMAVPTIYSKLidyyeshlaKPGIKDFVKAMCQQKIRLMVS-GSSALPVPTLERW 146
Cdd:cd17634 308 gvPNWpTPARMWQ---VVDKHGVNILYTAPTAIRAL---------MAAGDDAIEGTDRSSLRILGSvGEPINPEAYEWYW 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 147 REITGH--TLLERYGMTEIGMALTNPLNG--PRVPGSVGNPFPGVGVRIATEipqkEGSSYTVHAEGDAAGTEVFPGfed 222
Cdd:cd17634 376 KKIGKEkcPVVDTWWQTETGGFMITPLPGaiELKAGSATRPVFGVQPAVVDN----EGHPQPGGTEGNLVITDPWPG--- 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 223 regelQVRGpavfneYWNKPQETREAF--TPDGWFRTGDTA-VYKDNSYWILGRtSVDIIKSGGYKISALEVERHLLAHP 299
Cdd:cd17634 449 -----QTRT------LFGDHERFEQTYfsTFKGMYFSGDGArRDEDGYYWITGR-SDDVINVAGHRLGTAEIESVLVAHP 516
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 300 SIADVAVIGAPDSTWGQRVSAIVKLRDGHTLS---LKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKI 366
Cdd:cd17634 517 KVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSpelYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
1-371 |
3.32e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 121.26 E-value: 3.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAM---VTaLIDEWSWTKSDCILHVLPLHHVHGvVNKLLCPLWVGATCVMLPEFSPKE 77
Cdd:PRK13383 178 IVLLTSGTTGKPKGVPRAPQLRSAVgvwVT-ILDRTRLRTGSRISVAMPMFHGLG-LGMLMLTIALGGTVLTHRHFDAEA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 VwehFLSTDSRSINVFMAVPTIYSKLIDyyeshlakpgIKDFVKAMCQ-QKIRLMVSGSSALPvPTL-ERWREITGHTLL 155
Cdd:PRK13383 256 A---LAQASLHRADAFTAVPVVLARILE----------LPPRVRARNPlPQLRVVMSSGDRLD-PTLgQRFMDTYGDILY 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 156 ERYGMTEIGM-ALTNPLNGPRVPGSVGNPFPGVGVRIATEIPQKEGSSYT--VHAEGDAAGTevfpGFEDREGELQVrgp 232
Cdd:PRK13383 322 NGYGSTEVGIgALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTgrIFVGGELAGT----RYTDGGGKAVV--- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 233 avfneywnkpqetreaftpDGWFRTGDTAvYKDNS--YWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAP 310
Cdd:PRK13383 395 -------------------DGMTSTGDMG-YLDNAgrLFIVGRED-DMIISGGENVYPRAVENALAAHPAVADNAVIGVP 453
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2113536441 311 DSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK13383 454 DERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
2-371 |
8.48e-30 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 119.80 E-value: 8.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLS-AMVTALIDEWSWTKSDCILHVL--PLHH----VHGVVNKLLcplwvGATCVMLPEFS 74
Cdd:PRK12406 157 MIYTSGTTGHPKGVRRAAPTPEqAAAAEQMRALIYGLKPGIRALLtgPLYHsapnAYGLRAGRL-----GGVLVLQPRFD 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 75 PKEVWEhfLSTDSRSINVFMaVPTIYSKLIDYYESHLAKPGIkdfvkamcqQKIRLMVSGSSALPVPTLERWREITGHTL 154
Cdd:PRK12406 232 PEELLQ--LIERHRITHMHM-VPTMFIRLLKLPEEVRAKYDV---------SSLRHVIHAAAPCPADVKRAMIEWWGPVI 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 155 LERYGMTEIG-MALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPA 233
Cdd:PRK12406 300 YEYYGSTESGaVTFATSEDALSHPGTVGKAAPGAELRFV-----------------DEDGRPLPQG---EIGEIYSRIAG 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 234 V--FNeYWNKPqETREAFTPDGWFRTGDTA-VYKDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAP 310
Cdd:PRK12406 360 NpdFT-YHNKP-EKRAEIDRGGFITSGDVGyLDADGYLFLCDRKR-DMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIP 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2113536441 311 DSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK12406 437 DAEFGEALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
2-366 |
5.45e-29 |
|
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: 118.05 E-value: 5.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLsaMV-TALIDEWS---------WTKSDC--------IlhvlplhhVHGvvnkllcPLWV 63
Cdd:cd05966 236 ILYTSGSTGKPKGVVHTTGGY--LLyAATTFKYVfdyhpddiyWCTADIgwitghsyI--------VYG-------PLAN 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 64 GATCVML------PEFSpkEVWEhflSTDSRSINVFMAVPTIYSKLIDYYESHLAKPGIKDFvkamcqqkiRLMvsGSSA 137
Cdd:cd05966 299 GATTVMFegtptyPDPG--RYWD---IVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSL---------RVL--GSVG 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 138 LPV-PTLERW-REITGH---TLLERYGMTEIGMALTNPLNG--PRVPGSVGNPFPGVGVRIateipqkegssytVHAEGD 210
Cdd:cd05966 363 EPInPEAWMWyYEVIGKercPIVDTWWQTETGGIMITPLPGatPLKPGSATRPFFGIEPAI-------------LDEEGN 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 211 AAGTEVfpgfedrEGELQVRG--PAVFNEYWNKPQETREAFTPD--GWFRTGDTAVY-KDNSYWILGRTSvDIIKSGGYK 285
Cdd:cd05966 430 EVEGEV-------EGYLVIKRpwPGMARTIYGDHERYEDTYFSKfpGYYFTGDGARRdEDGYYWITGRVD-DVINVSGHR 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 286 ISALEVERHLLAHPSIADVAVIGAPDSTWGQRVSAIVKLRDGHTLS---LKKLKEWGRAVMAPYCIPAELIRVEEIPRNQ 362
Cdd:cd05966 502 LGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSdelRKELRKHVRKEIGPIATPDKIQFVPGLPKTR 581
|
....
gi 2113536441 363 MGKI 366
Cdd:cd05966 582 SGKI 585
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
2-371 |
3.30e-28 |
|
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: 115.06 E-value: 3.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNkLLCPLWVGATCVMLPEFSPKEV--W 79
Cdd:cd12114 131 VIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYD-IFGALSAGATLVLPDEARRRDPahW 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 80 EHFLSTdsRSINVFMAVPTIYSKLIDYYESHLAKPgikdfvkamcqQKIRL-MVSGSsALPVPTLERWREITGH-TLLER 157
Cdd:cd12114 210 AELIER--HGVTLWNSVPALLEMLLDVLEAAQALL-----------PSLRLvLLSGD-WIPLDLPARLRALAPDaRLISL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTEIGM-ALTNPLN-GPRVPGSV--GNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGFEdreGELQVRGPA 233
Cdd:cd12114 276 GGATEASIwSIYHPIDeVPPDWRSIpyGRPLANQRYRVL-----------------DPRGRDCPDWVP---GELWIGGRG 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 234 VFNEYWNKPQETREAFTPDG----WFRTGDTAVYKDNSYWI-LGRtsVDI-IKSGGYKISALEVERHLLAHPSIADVAVI 307
Cdd:cd12114 336 VALGYLGDPELTAARFVTHPdgerLYRTGDLGRYRPDGTLEfLGR--RDGqVKVRGYRIELGEIEAALQAHPGVARAVVV 413
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2113536441 308 GAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd12114 414 VLGDPGGKRLAAFVVPDNDGTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
4-373 |
1.49e-27 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 113.79 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQN--LSAMVTALIdeWSWTKSDCILHVLPLHHVHGvvnklLCPLWVGA----TCVMLPEFSPKE 77
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGayLMALSNALI--WGMNEGAVYLWTLPMFHCNG-----WCFTWTLAalcgTNICLRQVTAKA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 VWEhflSTDSRSINVFMAVPTIYSKLIDYYESHLAKPgikdfvkamCQQKIRLMVSGssALPVPTLERWREITGHTLLER 157
Cdd:PLN02479 275 IYS---AIANYGVTHFCAAPVVLNTIVNAPKSETILP---------LPRVVHVMTAG--AAPPPSVLFAMSEKGFRVTHT 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTEIgmaltnplNGPRVPGSVGNPFPGVGVRIATEIPQKEGSSYtVHAEG----DAAGTEVFPGFEDREGELQVRGPA 233
Cdd:PLN02479 341 YGLSET--------YGPSTVCAWKPEWDSLPPEEQARLNARQGVRY-IGLEGldvvDTKTMKPVPADGKTMGEIVMRGNM 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 234 VFNEYWNKPQETREAFTpDGWFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDST 313
Cdd:PLN02479 412 VMKGYLKNPKANEEAFA-NGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDER 490
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2113536441 314 WGQRVSAIVKLRDGHTLSLKK-----LKEWGRAVMAPYCIPAELIrVEEIPRNQMGKINKKQLLA 373
Cdd:PLN02479 491 WGESPCAFVTLKPGVDKSDEAalaedIMKFCRERLPAYWVPKSVV-FGPLPKTATGKIQKHVLRA 554
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
3-375 |
1.56e-27 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 112.78 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 3 IYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILhVLPLHHVHGVVnKLLCPLWVGATCVMLP--EFSPKEVW- 79
Cdd:PRK07445 126 IPTGGSSGQIRFAIHTWETLTASVQGFQRYFQLQQVNSFC-VLPLYHVSGLM-QFMRSFLTGGKLVILPykRLKSGQELp 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 80 ----EHFLSTdsrsinvfmaVPTIYSKLIDYYESHLAkpgikdfvkamcQQKIRLmVSGSSAlpvptlerWREitghtLL 155
Cdd:PRK07445 204 pnpsDFFLSL----------VPTQLQRLLQLRPQWLA------------QFRTIL-LGGAPA--------WPS-----LL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 156 ER-----------YGMTEI-GMALT-NP---LNGPRvpgSVGNPFPGVGVRIateipqkegSSYTVhaegdaagtevfpg 219
Cdd:PRK07445 248 EQarqlqlrlaptYGMTETaSQIATlKPddfLAGNN---SSGQVLPHAQITI---------PANQT-------------- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 220 fedreGELQVRGPAVFNEYWNKPQETREAFTPD--GWFRtgdtavyKDNSYWILGRTSVDIIkSGGYKISALEVERHLLA 297
Cdd:PRK07445 302 -----GNITIQAQSLALGYYPQILDSQGIFETDdlGYLD-------AQGYLHILGRNSQKII-TGGENVYPAEVEAAILA 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113536441 298 HPSIADVAVIGAPDSTWGQRVSAIVKLRDGhTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLLALF 375
Cdd:PRK07445 369 TGLVQDVCVLGLPDPHWGEVVTAIYVPKDP-SISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIA 445
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
4-373 |
1.75e-27 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 113.97 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNLSAMVTALI-DEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEVwEHF 82
Cdd:PRK06060 152 YTSGTTGPPKAAIHRHADPLTFVDAMCrKALRLTPEDTGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEA-AAI 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 83 LSTDSRSiNVFMAVPTIYSKLIDYyeshlakpgikdfVKAMCQQKIRLMVSGSSALPVPTLERWREITGHT-LLERYGMT 161
Cdd:PRK06060 231 LSARFGP-SVLYGVPNFFARVIDS-------------CSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIpILDGIGST 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 162 EIGMA-LTNPLNGPRvPGSVGNPFPGVGVRIateipqkegssytVHAEGDAAGtevfPGFEdreGELQVRGPAVFNEYWN 240
Cdd:PRK06060 297 EVGQTfVSNRVDEWR-LGTLGRVLPPYEIRV-------------VAPDGTTAG----PGVE---GDLWVRGPAIAKGYWN 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 241 KPQETreaFTPDGWFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQRVSA 320
Cdd:PRK06060 356 RPDSP---VANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQA 432
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2113536441 321 IVKLRDGHTLSLKKLKEWGRAV---MAPYCIPAELIRVEEIPRNQMGKINKKQLLA 373
Cdd:PRK06060 433 FLVATSGATIDGSVMRDLHRGLlnrLSAFKVPHRFAVVDRLPRTPNGKLVRGALRK 488
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
2-371 |
7.41e-27 |
|
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: 110.99 E-value: 7.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLhhVHGVVNKLLCPLWV-GATCVMLPE---FSPKE 77
Cdd:cd17644 111 VIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASI--AFDVAAEEIYVTLLsGATLVLRPEemrSSLED 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 VWEHflsTDSRSINVFMAVPTIYSKLIDyyeshlakpgikDFVKAMCQ--QKIRLMVSGSSALPVPTLERWREITGH--T 153
Cdd:cd17644 189 FVQY---IQQWQLTVLSLPPAYWHLLVL------------ELLLSTIDlpSSLRLVIVGGEAVQPELVRQWQKNVGNfiQ 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 154 LLERYGMTEIGMA-----LTNPLNGPRVPGSVGNPFPGVGVRIATEIPQkegssytvhaegdaagtEVFPGFEdreGELQ 228
Cdd:cd17644 254 LINVYGPTEATIAatvcrLTQLTERNITSVPIGRPIANTQVYILDENLQ-----------------PVPVGVP---GELH 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 229 VRGPAVFNEYWNKPQETREAFTPDGW--------FRTGDTAVY-KDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHP 299
Cdd:cd17644 314 IGGVGLARGYLNRPELTAEKFISHPFnsseserlYKTGDLARYlPDGNIEYLGRID-NQVKIRGFRIELGEIEAVLSQHN 392
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2113536441 300 SIADVAVIGAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd17644 393 DVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
2-371 |
1.08e-26 |
|
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: 111.64 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALI---------DEWsWTKSDcilhvlplhhVHGVV-NKLLC--PLWVGATCVM 69
Cdd:cd05967 235 ILYTSGTTGKPKGVVRDNGGHAVALNWSMrniygikpgDVW-WAASD----------VGWVVgHSYIVygPLLHGATTVL 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 70 ---LPEFSPKE-VWehFLSTDSRSINVFMAVPTIYSKLidyyesHLAKPGIKdFVKAMCQQKIRLMVSGSSALPVPTLER 145
Cdd:cd05967 304 yegKPVGTPDPgAF--WRVIEKYQVNALFTAPTAIRAI------RKEDPDGK-YIKKYDLSSLRTLFLAGERLDPPTLEW 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 146 WREITGHTLLERYGMTEIGMALTNPLNG----PRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfe 221
Cdd:cd05967 375 AENTLGVPVIDHWWQTETGWPITANPVGleplPIKAGSPGKPVPGYQVQVL-----------------DEDGEPVGPN-- 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 222 dREGELQVRGP---AVFNEYWNKPQETREAF--TPDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHL 295
Cdd:cd05967 436 -ELGNIVIKLPlppGCLLTLWKNDERFKKLYlsKFPGYYDTGDAGYKDEDGYlFIMGRTD-DVINVAGHRLSTGEMEESV 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 296 LAHPSIADVAVIGAPDSTWGQRVSAIVKLRDGHTLSLKKLKE----WGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd05967 514 LSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEKelvaLVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTL 593
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2-371 |
1.94e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 111.79 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLhHVHGVVNKLLCPLWVGATCVMLPE---FSPKEV 78
Cdd:PRK12467 661 VIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTF-AFDLGVTELFGALASGATLHLLPPdcaRDAEAF 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 79 WEHFlstDSRSINVFMAVPTIYSKLIDyyeshlakpgikDFVKAMCQQKIRLMVSGsSALPVPTLERWREIT-GHTLLER 157
Cdd:PRK12467 740 AALM---ADQGVTVLKIVPSHLQALLQ------------ASRVALPRPQRALVCGG-EALQVDLLARVRALGpGARLINH 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTE--IGMALTNPLNGPRVPGSV--GNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGFedrEGELQVRGPA 233
Cdd:PRK12467 804 YGPTEttVGVSTYELSDEERDFGNVpiGQPLANLGLYIL-----------------DHYLNPVPVGV---VGELYIGGAG 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 234 VFNEYWNKPQETREAFTPDGW-------FRTGDTAVY-KDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVA 305
Cdd:PRK12467 864 LARGYHRRPALTAERFVPDPFgadggrlYRTGDLARYrADGVIEYLGRMD-HQVKIRGFRIELGEIEARLLAQPGVREAV 942
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 306 VIGAPDSTWGQRVSAIVKLR--DG--HTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK12467 943 VLAQPGDAGLQLVAYLVPAAvaDGaeHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
2-259 |
2.91e-26 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 110.57 E-value: 2.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCpLWVGATCvmlpEFSPKEVWEh 81
Cdd:PLN02736 226 ICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSDVHISYLPLAHIYERVNQIVM-LHYGVAV----GFYQGDNLK- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 fLSTDSRSI--NVFMAVPTIYSKLID----------------YYESHLAK----------PGIKD---F--VKAMCQQKI 128
Cdd:PLN02736 300 -LMDDLAALrpTIFCSVPRLYNRIYDgitnavkesgglkerlFNAAYNAKkqalengknpSPMWDrlvFnkIKAKLGGRV 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 129 RLMVSGSSALPVPTLERWREITGHTLLERYGMTEIGMALTNPLNGPRVPGSVGNPFPGVGVRIAtEIPQKEgssYTVhae 208
Cdd:PLN02736 379 RFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLV-DVPEMN---YTS--- 451
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2113536441 209 gdaagtevfpgfEDR---EGELQVRGPAVFNEYWNKPQETREAFTPDGWFRTGD 259
Cdd:PLN02736 452 ------------EDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGD 493
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1-374 |
3.03e-26 |
|
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: 108.81 E-value: 3.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQ-----NLSAM---------VTALIDEWSWTKsdcilhvlplhhvHGVVNkLLCPLWVGAT 66
Cdd:cd05974 89 LLYFTSGTTSKPKLVEHTHRsypvgHLSTMywiglkpgdVHWNISSPGWAK-------------HAWSC-FFAPWNAGAT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 67 CVML--PEFSPKEVWEhflSTDSRSINVFMAVPTIYSKLIdyyESHLAKPGIKdfvkamcqqkIRLMVSGSSALPVPTLE 144
Cdd:cd05974 155 VFLFnyARFDAKRVLA---ALVRYGVTTLCAPPTVWRMLI---QQDLASFDVK----------LREVVGAGEPLNPEVIE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 145 RWREITGHTLLERYGMTEIGMALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVfpgfedRE 224
Cdd:cd05974 219 QVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALL-----------------DPDGAPA------TE 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 225 GELQV-----RGPAVFNEYWNKPQETREAFTpDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAH 298
Cdd:cd05974 276 GEVALdlgdtRPVGLMKGYAGDPDKTAHAMR-GGYYRTGDIAMRDEDGYlTYVGRAD-DVFKSSDYRISPFELESVLIEH 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 299 PSIADVAVIGAPDSTWGQRVSAIVKLRDGHTLS---LKKLKEWGRAVMAPYcipAELIRVE--EIPRNQMGKINKKQLLA 373
Cdd:cd05974 354 PAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSpetALEIFRFSRERLAPY---KRIRRLEfaELPKTISGKIRRVELRR 430
|
.
gi 2113536441 374 L 374
Cdd:cd05974 431 R 431
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
2-371 |
3.60e-26 |
|
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: 108.94 E-value: 3.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVtalidewSWTKSDCilhvlPLHHVHGV-----------VNKLLCPLWVGATCVM- 69
Cdd:cd12115 110 VIYTSGSTGRPKGVAIEHRNAAAFL-------QWAAAAF-----SAEELAGVlastsicfdlsVFELFGPLATGGKVVLa 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 70 -----LPEF-SPKEVwehflstdsRSINvfmAVPTIYSKLIDyyesHLAKPGIkdfVKAMCqqkirlmVSGSsALPVPTL 143
Cdd:cd12115 178 dnvlaLPDLpAAAEV---------TLIN---TVPSAAAELLR----HDALPAS---VRVVN-------LAGE-PLPRDLV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 144 ER-WREITGHTLLERYGMTEigmALTNPLNGPRVPG-----SVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVF 217
Cdd:cd12115 231 QRlYARLQVERVVNLYGPSE---DTTYSTVAPVPPGasgevSIGRPLANTQAYVL-----------------DRALQPVP 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 218 PGFEdreGELQVRGPAVFNEYWNKPQETREAFTPDGW------FRTGDTAVYK-DNSYWILGRTSvDIIKSGGYKISALE 290
Cdd:cd12115 291 LGVP---GELYIGGAGVARGYLGRPGLTAERFLPDPFgpgarlYRTGDLVRWRpDGLLEFLGRAD-NQVKVRGFRIELGE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 291 VERHLLAHPSIADVAVIGAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQ 370
Cdd:cd12115 367 IEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSA 446
|
.
gi 2113536441 371 L 371
Cdd:cd12115 447 L 447
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1-317 |
3.83e-26 |
|
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: 109.11 E-value: 3.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPefspkevwe 80
Cdd:cd05908 110 FIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMP--------- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 hflstdsrsINVFMAVPTIYSKLIDYYE-SHLAKP--GIKDFVKAMCQQK--------IRLMVSGSSALPVPTLErwrEI 149
Cdd:cd05908 181 ---------TRLFIRRPILWLKKASEHKaTIVSSPnfGYKYFLKTLKPEKandwdlssIRMILNGAEPIDYELCH---EF 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 150 TGH---------TLLERYGMTEIGMALTNP-LNGPRVPGSVGNPFPGVGVRIAtEIPQKEGSSYTVHAEGDA-AGTEVFP 218
Cdd:cd05908 249 LDHmskyglkrnAILPVYGLAEASVGASLPkAQSPFKTITLGRRHVTHGEPEP-EVDKKDSECLTFVEVGKPiDETDIRI 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 219 GFEDRE-------GELQVRGPAVFNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSYWILGRTSvDIIKSGGYKISALEV 291
Cdd:cd05908 328 CDEDNKilpdgyiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLGFIRNGRLVITGREK-DIIFVNGQNVYPHDI 406
|
330 340
....*....|....*....|....*...
gi 2113536441 292 ERHL--LAHPSIADVAVIGAPDSTWGQR 317
Cdd:cd05908 407 ERIAeeLEGVELGRVVACGVNNSNTRNE 434
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
2-371 |
4.36e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 109.40 E-value: 4.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVL--------STHQNLSAMVTALideWSWTKSDCILHVLPLHHVH-----GVVNKLlcplwvGATCV 68
Cdd:PRK13391 159 MLYSSGTTGRPKGIKrplpeqppDTPLPLTAFLQRL---WGFRSDMVYLSPAPLYHSApqravMLVIRL------GGTVI 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 69 MLPEFSPkevwEHFLS-TDSRSINVFMAVPTIYSKLidyyeshLAKPgiKDFVKAMCQQKIRLMVSGSSALPVPTLERWR 147
Cdd:PRK13391 230 VMEHFDA----EQYLAlIEEYGVTHTQLVPTMFSRM-------LKLP--EEVRDKYDLSSLEVAIHAAAPCPPQVKEQMI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 148 EITGHTLLERYGMTE-IGMALTNPLNGPRVPGSVGNPFPGVgVRIAteipqkegssytvhaegDAAGTEVFPGfedREGE 226
Cdd:PRK13391 297 DWWGPIIHEYYAATEgLGFTACDSEEWLAHPGTVGRAMFGD-LHIL-----------------DDDGAELPPG---EPGT 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 227 LQVRGPAVFnEYWNKPQETREAFTPDG-WFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVA 305
Cdd:PRK13391 356 IWFEGGRPF-EYLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAA 434
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2113536441 306 VIGAPDSTWGQRVSAIVKLRDGHTLS---LKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK13391 435 VFGVPNEDLGEEVKAVVQPVDGVDPGpalAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
1-371 |
7.49e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 108.56 E-value: 7.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVL------STHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVH-----GVVNKLlcplwvGATCVM 69
Cdd:PRK13390 152 VMLYSSGTTGFPKGIQpdlpgrDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAplrwcSMVHAL------GGTVVL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 70 LPEFSPKEVWEHflsTDSRSINVFMAVPTIYSKLIDyyeshlakpgIKDFVKAMCQ-QKIRLMVSGSSALPVPTLERWRE 148
Cdd:PRK13390 226 AKRFDAQATLGH---VERYRITVTQMVPTMFVRLLK----------LDADVRTRYDvSSLRAVIHAAAPCPVDVKHAMID 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 149 ITGHTLLERYGMTEI-GMALTNPLNGPRVPGSVGNPFPGvgvriateipqkegssyTVHAeGDAAGTEVFPGfedREGEL 227
Cdd:PRK13390 293 WLGPIVYEYYSSTEAhGMTFIDSPDWLAHPGSVGRSVLG-----------------DLHI-CDDDGNELPAG---RIGTV 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 228 QVRGPAVFNEYWNKPQETREAFTPDG--WFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVA 305
Cdd:PRK13390 352 YFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVA 431
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2113536441 306 VIGAPDSTWGQRVSAIVKLRDGHTLS---LKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK13390 432 VIGVPDPEMGEQVKAVIQLVEGIRGSdelARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2-374 |
7.67e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 109.87 E-value: 7.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPlHHVHGVVNKLLCPLWVGATCVMLPeFSPKEVWEH 81
Cdd:PRK12467 1723 VIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTS-FAFDVSVWELFWPLINGARLVIAP-PGAHRDPEQ 1800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 FLSTDSRS-INVFMAVPTIYSKLIDYYEsHLAKPgikdfvkamcqQKIRLMVSGSSALPVPTLERWREITGHT-LLERYG 159
Cdd:PRK12467 1801 LIQLIERQqVTTLHFVPSMLQQLLQMDE-QVEHP-----------LSLRRVVCGGEALEVEALRPWLERLPDTgLFNLYG 1868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 160 MTEIGMALTNplngprVPGSVGNPFPGVGVRIATEIPQKegSSYTVhaegDAAGTEVFPGFedrEGELQVRGPAVFNEYW 239
Cdd:PRK12467 1869 PTETAVDVTH------WTCRRKDLEGRDSVPIGQPIANL--STYIL----DASLNPVPIGV---AGELYLGGVGLARGYL 1933
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 240 NKPQETREAFTPDGW-------FRTGDTAVYK-DNSYWILGRtsVD-IIKSGGYKISALEVERHLLAHPSIADVAVIgAP 310
Cdd:PRK12467 1934 NRPALTAERFVADPFgtvgsrlYRTGDLARYRaDGVIEYLGR--IDhQVKIRGFRIELGEIEARLREQGGVREAVVI-AQ 2010
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2113536441 311 DSTWGQRVSAIVKLRDGHTL--------SLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLLAL 374
Cdd:PRK12467 2011 DGANGKQLVAYVVPTDPGLVdddeaqvaLRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAP 2082
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
4-325 |
1.15e-25 |
|
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: 108.28 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGaTCVMLPE----------- 72
Cdd:cd17641 165 TTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIGEQMYSVGQALVCG-FIVNFPEepetmmedlre 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 73 ------FSPKEVWEHFLS------TDSRSINVFM----------AVPTIYS----KLIDYYESHLAKPGIKDFVKA-MCQ 125
Cdd:cd17641 244 igptfvLLPPRVWEGIAAdvrarmMDATPFKRFMfelgmklglrALDRGKRgrpvSLWLRLASWLADALLFRPLRDrLGF 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 126 QKIRLMVSGSSALPVPTLERWREItGHTLLERYGMTEIGMALTNPLNGPRVPGSVGNPFPGVGVRIateipqkegssytv 205
Cdd:cd17641 324 SRLRSAATGGAALGPDTFRFFHAI-GVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI-------------- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 206 haegdaagtevfpgfeDREGELQVRGPAVFNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSYW-ILGRTSvDIIK-SGG 283
Cdd:cd17641 389 ----------------DEVGEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLvVIDRAK-DVGTtSDG 451
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2113536441 284 YKISALEVERHLLAHPSIADVAVIGAPDstwgQRVSAIVKLR 325
Cdd:cd17641 452 TRFSPQFIENKLKFSPYIAEAVVLGAGR----PYLTAFICID 489
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
4-366 |
1.18e-25 |
|
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: 108.09 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSpkevwehfl 83
Cdd:cd05931 156 YTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAA--------- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 84 stdsrsinvFMAVPTIYSKLIDYYE-SHLAKPgikDFVKAMCQQKIR-----------LMVSGSSALPV--PTLERWRE- 148
Cdd:cd05931 227 ---------FLRRPLRWLRLISRYRaTISAAP---NFAYDLCVRRVRdedlegldlssWRVALNGAEPVrpATLRRFAEa 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 149 -----ITGHTLLERYGMTEIGMALTNP---------------LNGPRVPG-----------SVGNPFPGVGVRIateipq 197
Cdd:cd05931 295 fapfgFRPEAFRPSYGLAEATLFVSGGppgtgpvvlrvdrdaLAGRAVAVaaddpaarelvSCGRPLPDQEVRI------ 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 198 kegssytVHAEGdaaGTEVFPGfedREGELQVRGPAVFNEYWNKPQETREAFTP------DGWFRTGDTAVYKDNSYWIL 271
Cdd:cd05931 369 -------VDPET---GRELPDG---EVGEIWVRGPSVASGYWGRPEATAETFGAlaatdeGGWLRTGDLGFLHDGELYIT 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 272 GRTSvDIIKSGGYKISALEVERHL-LAHPSI--ADVAVIGAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGR-AVMAPYC 347
Cdd:cd05931 436 GRLK-DLIIVRGRNHYPQDIEATAeEAHPALrpGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRaAVAREHG 514
|
410 420
....*....|....*....|..
gi 2113536441 348 IPAE---LIRVEEIPRNQMGKI 366
Cdd:cd05931 515 VAPAdvvLVRPGSIPRTSSGKI 536
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-371 |
1.98e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 108.51 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLhHVHGVVNKLLCPLWVGATCVMLPEFSPKEVWEH 81
Cdd:PRK12316 3201 VIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTF-SFDVFVEELFWPLMSGARVVLAGPEDWRDPALL 3279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 FLSTDSRSINVFMAVPTIYSKLidyyeshLAKPGIKDFVkamcqqKIRLMVSGSSALPVPTLERWreITGHTLLERYGMT 161
Cdd:PRK12316 3280 VELINSEGVDVLHAYPSMLQAF-------LEEEDAHRCT------SLKRIVCGGEALPADLQQQV--FAGLPLYNLYGPT 3344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 162 EIGMALTNPLNGPRVPGS--VGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGfedREGELQVRGPAVFNEYW 239
Cdd:PRK12316 3345 EATITVTHWQCVEEGKDAvpIGRPIANRACYIL-----------------DGSLEPVPVG---ALGELYLGGEGLARGYH 3404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 240 NKPQETREAFTPDGW------FRTGDTAVYK-DNSYWILGRTSVDiIKSGGYKISALEVERHLLAHPSIADVAVIGAPds 312
Cdd:PRK12316 3405 NRPGLTAERFVPDPFvpgerlYRTGDLARYRaDGVIEYIGRVDHQ-VKIRGFRIELGEIEARLLEHPWVREAVVLAVD-- 3481
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2113536441 313 twGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK12316 3482 --GRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKAL 3538
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-371 |
6.81e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 106.97 E-value: 6.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLhHVHGVVNKLLCPLWVGATCVM------LPEFSP 75
Cdd:PRK12316 4699 VIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSF-SFDGSHEGLYHPLINGASVVIrddslwDPERLY 4777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 76 KEVWEHflstdsrSINVFMAVPTIYSKLIDYYESHLAKPgikdfvkamcqqKIRLMVSGSSALPVPTLER-WREITGHTL 154
Cdd:PRK12316 4778 AEIHEH-------RVTVLVFPPVYLQQLAEHAERDGEPP------------SLRVYCFGGEAVAQASYDLaWRALKPVYL 4838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 155 LERYGMTEIGM-ALTNPLNGPRVPGSVGNPfpgvgvrIATEIPQKEGSSYTVHAEGDAAGTevfpgfedrEGELQVRGPA 233
Cdd:PRK12316 4839 FNGYGPTETTVtVLLWKARDGDACGAAYMP-------IGTPLGNRSGYVLDGQLNPLPVGV---------AGELYLGGEG 4902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 234 VFNEYWNKPQETREAFTPDGW-------FRTGDTAVYK-DNSYWILGRtsVD-IIKSGGYKISALEVERHLLAHPSIADV 304
Cdd:PRK12316 4903 VARGYLERPALTAERFVPDPFgapggrlYRTGDLARYRaDGVIDYLGR--VDhQVKIRGFRIELGEIEARLREHPAVREA 4980
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2113536441 305 AVIGAPDSTWGQRVSAIVKlRDGHTLSLK--------KLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK12316 4981 VVIAQEGAVGKQLVGYVVP-QDPALADADeaqaelrdELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
2-371 |
1.06e-24 |
|
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: 104.47 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSwtksdciLHVLPLHHVHGV-------VNKLLCPLWVGATCVMLPE-- 72
Cdd:cd17650 98 VIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYE-------LDSFPVRLLQMAsfsfdvfAGDFARSLLNGGTLVICPDev 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 73 -FSPKEVWEHFLstdSRSINVFMAVPTIYSKLIDYYESHLAKPgikdfvkamcqQKIRLMVSGSSALPVPTL-ERWREIT 150
Cdd:cd17650 171 kLDPAALYDLIL---KSRITLMESTPALIRPVMAYVYRNGLDL-----------SAMRLLIVGSDGCKAQDFkTLAARFG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 151 GHT-LLERYGMTEIGMALT------NPLNGPR-VPgsVGNPFPGVGVRI--ATEIPQKEGSSytvhaegdaagtevfpgf 220
Cdd:cd17650 237 QGMrIINSYGVTEATIDSTyyeegrDPLGDSAnVP--IGRPLPNTAMYVldERLQPQPVGVA------------------ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 221 edreGELQVRGPAVFNEYWNKPQETREAFTPDGW------FRTGDTAVYK-DNSYWILGRTSvDIIKSGGYKISALEVER 293
Cdd:cd17650 297 ----GELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRaDGNVELLGRVD-HQVKIRGFRIELGEIES 371
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113536441 294 HLLAHPSIADVAVIGAPDSTWGQRVSAIVKLRdgHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd17650 372 QLARHPAIDEAVVAVREDKGGEARLCAYVVAA--ATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
2-366 |
1.16e-24 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 105.61 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSThqnlSA--MV-TALIDEWswtksdcilhVLPLH----------------H---VHGvvnkllc 59
Cdd:PRK00174 250 ILYTSGSTGKPKGVLHT----TGgyLVyAAMTMKY----------VFDYKdgdvywctadvgwvtgHsyiVYG------- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 60 PLWVGATCVML---PEF-SPKEVWEhflSTDSRSINVFMAVPT-IYSklidyyeshLAKPGiKDFVKAMCQQKIRLMvsG 134
Cdd:PRK00174 309 PLANGATTLMFegvPNYpDPGRFWE---VIDKHKVTIFYTAPTaIRA---------LMKEG-DEHPKKYDLSSLRLL--G 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 135 SSALPV-PTLERW-REITGHtllER------YGMTEIGMALTNPLNG--PRVPGSVGNPFPGVGVRIATEipqkEGSSYT 204
Cdd:PRK00174 374 SVGEPInPEAWEWyYKVVGG---ERcpivdtWWQTETGGIMITPLPGatPLKPGSATRPLPGIQPAVVDE----EGNPLE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 205 VHAEGDAAGTEVFPGfedregelQVRGpavfneYWNKPQETREAFTPD--GWFRTGDTAVY-KDNSYWILGRTSvDIIKS 281
Cdd:PRK00174 447 GGEGGNLVIKDPWPG--------MMRT------IYGDHERFVKTYFSTfkGMYFTGDGARRdEDGYYWITGRVD-DVLNV 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 282 GGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQRVSAIVKLRDGHTLS--LKK-LKEWGRAVMAPYCIPAELIRVEEI 358
Cdd:PRK00174 512 SGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSdeLRKeLRNWVRKEIGPIAKPDVIQFAPGL 591
|
....*...
gi 2113536441 359 PRNQMGKI 366
Cdd:PRK00174 592 PKTRSGKI 599
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-373 |
5.78e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 104.27 E-value: 5.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVnKLLCPLWVGATCVMLPE---FSPKEV 78
Cdd:PRK12316 660 VIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVW-EFFWPLMSGARLVVAAPgdhRDPAKL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 79 WEhflSTDSRSINVFMAVPTIYSKLidyyeshLAKPGIKDFVkamcqqKIRLMVSGSSALPVPTLER--WREITGHtLLE 156
Cdd:PRK12316 739 VE---LINREGVDTLHFVPSMLQAF-------LQDEDVASCT------SLRRIVCSGEALPADAQEQvfAKLPQAG-LYN 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 157 RYGMTEIGMALTN----PLNGPRVPgsVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGFedrEGELQVRGP 232
Cdd:PRK12316 802 LYGPTEAAIDVTHwtcvEEGGDSVP--IGRPIANLACYIL-----------------DANLEPVPVGV---LGELYLAGR 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 233 AVFNEYWNKPQETREAFTPDGW------FRTGDTAVYK-DNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVA 305
Cdd:PRK12316 860 GLARGYHGRPGLTAERFVPSPFvagermYRTGDLARYRaDGVIEYAGRID-HQVKLRGLRIELGEIEARLLEHPWVREAA 938
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113536441 306 VIGAPdstwGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLLA 373
Cdd:PRK12316 939 VLAVD----GKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPA 1002
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
2-335 |
7.50e-24 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 103.05 E-value: 7.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVnkllcplwVGATCVmLPEFSPKevweH 81
Cdd:PRK09274 179 ILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLFALFGPA--------LGMTSV-IPDMDPT----R 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 FLSTDSRSI----------NVFMAvPTIYSKLIDYYESHLAK-PGIKdfvkamcqqkiRLMVSGSSAlPVPTLERWREIT 150
Cdd:PRK09274 246 PATVDPAKLfaaierygvtNLFGS-PALLERLGRYGEANGIKlPSLR-----------RVISAGAPV-PIAVIERFRAML 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 151 GHT--LLERYGMTE------IGM--ALTNPLNGPRVPGS--VGNPFPGVGVRI--ATEIPQKEGSSYTVHAEGdaagtEV 216
Cdd:PRK09274 313 PPDaeILTPYGATEalpissIESreILFATRAATDNGAGicVGRPVDGVEVRIiaISDAPIPEWDDALRLATG-----EI 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 217 fpgfedreGELQVRGPAVFNEYWNKPQETREAFTPDG----WFRTGDTAvYKDNS--YWILGRTSVDIIKSGG--YKIsa 288
Cdd:PRK09274 388 --------GEIVVAGPMVTRSYYNRPEATRLAKIPDGqgdvWHRMGDLG-YLDAQgrLWFCGRKAHRVETAGGtlYTI-- 456
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2113536441 289 lEVERHLLAHPSIADVAVIGAPDSTwGQRVSAIVKLRDGHTLSLKKL 335
Cdd:PRK09274 457 -PCERIFNTHPGVKRSALVGVGVPG-AQRPVLCVELEPGVACSKSAL 501
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
4-371 |
4.35e-23 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 100.82 E-value: 4.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNLSA-MVTALIDewswTKSDCI-----LHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKe 77
Cdd:PLN02330 191 FSSGTTGISKGVMLTHRNLVAnLCSSLFS----VGPEMIgqvvtLGLIPFFHIYGITGICCATLRNKGKVVVMSRFELR- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 VWEHFLSTdsRSINVFMAVPTIYSKLIDyyeshlaKPGIKDFvkAMCQQKIRLMVSGSSALPVPTLERW-REITGHTLLE 156
Cdd:PLN02330 266 TFLNALIT--QEVSFAPIVPPIILNLVK-------NPIVEEF--DLSKLKLQAIMTAAAPLAPELLTAFeAKFPGVQVQE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 157 RYGMTE---IGMALTNPLNGPRVP--GSVGNPFPGVGVRIateIPQKEGSSytvhaegdaagtevFPgfEDREGELQVRG 231
Cdd:PLN02330 335 AYGLTEhscITLTHGDPEKGHGIAkkNSVGFILPNLEVKF---IDPDTGRS--------------LP--KNTPGELCVRS 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 232 PAVFNEYWNKPQETREAFTPDGWFRTGDTA-VYKDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAP 310
Cdd:PLN02330 396 QCVMQGYYNNKEETDRTIDEDGWLHTGDIGyIDDDGDIFIVDRIK-ELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLP 474
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2113536441 311 DSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PLN02330 475 DEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
2-367 |
2.43e-22 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 98.88 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNL---SAMVTALIDewsWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPefSPKev 78
Cdd:PRK06814 798 ILFTSGSEGTPKGVVLSHRNLlanRAQVAARID---FSPEDKVFNALPVFHSFGLTGGLVLPLLSGVKVFLYP--SPL-- 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 79 weHFlstdsRSIN--VFMAVPTI----------YSKLIDYYeshlakpgikDFvkamcqQKIRLMVSGSSALPVPTLERW 146
Cdd:PRK06814 871 --HY-----RIIPelIYDTNATIlfgtdtflngYARYAHPY----------DF------RSLRYVFAGAEKVKEETRQTW 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 147 REITGHTLLERYGMTEIG--MALTNPLNGPrvPGSVGNPFPGVGVRIateipqkegssytvhaegdaagtEVFPGFEDrE 224
Cdd:PRK06814 928 MEKFGIRILEGYGVTETApvIALNTPMHNK--AGTVGRLLPGIEYRL-----------------------EPVPGIDE-G 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 225 GELQVRGPAVFNEYW--NKPQETREAftPDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAHPSI 301
Cdd:PRK06814 982 GRLFVRGPNVMLGYLraENPGVLEPP--ADGWYDTGDIVTIDEEGFiTIKGRAK-RFAKIAGEMISLAAVEELAAELWPD 1058
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2113536441 302 ADVAVIGAPDSTWGQRvsaIVKLRDGHTLSLKKLKEWGRAVMAP-YCIPAELIRVEEIPRNQMGKIN 367
Cdd:PRK06814 1059 ALHAAVSIPDARKGER---IILLTTASDATRAAFLAHAKAAGASeLMVPAEIITIDEIPLLGTGKID 1122
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
4-373 |
5.21e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 96.64 E-value: 5.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPK------- 76
Cdd:PRK08308 108 YSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHSYGLICGVLAALTRGSKPVIITNKNPKfalnilr 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 77 EVWEHFLstdsrsinvfMAVPTIYSKLidyyeSHLAKPGikdfvkamcQQKIRLMVSGSsALPVPTLERWREITGHtLLE 156
Cdd:PRK08308 188 NTPQHIL----------YAVPLMLHIL-----GRLLPGT---------FQFHAVMTSGT-PLPEAWFYKLRERTTY-MMQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 157 RYGMTEIG-MALTNPLngpRVPGSVGNPFPGVGVRIateipqkeGSSytvhaegdaagtevfpgfEDREGELQVRgpavf 235
Cdd:PRK08308 242 QYGCSEAGcVSICPDM---KSHLDLGNPLPHVSVSA--------GSD------------------ENAPEEIVVK----- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 236 neywnkpQETREAFTPDGWFRTGDTAVYkdnsywILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWG 315
Cdd:PRK08308 288 -------MGDKEIFTKDLGYKSERGTLH------FMGRMD-DVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAG 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2113536441 316 QRVSAIVKLRdgHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLLA 373
Cdd:PRK08308 354 ERVKAKVISH--EEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
2-371 |
9.63e-22 |
|
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: 96.08 E-value: 9.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILhVLPLHHVHGVVNKLLCPLWVGATCVMLPEfspkevweh 81
Cdd:cd17645 109 VIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSL-VYASFSFDASAWEIFPHLTAGAALHVVPS--------- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 flstdSRSINVfmavptiySKLIDYYESH------LAKPGIKDFVkAMCQQKIRLMVSGSSALPVPtlerwrEITGHTLL 155
Cdd:cd17645 179 -----ERRLDL--------DALNDYFNQEgitisfLPTGAAEQFM-QLDNQSLRVLLTGGDKLKKI------ERKGYKLV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 156 ERYGMTEIG-MALTNPLNGPRVPGSVGNPFPGVGVRIATEIPQkegssytVHAEGDAagtevfpgfedreGELQVRGPAV 234
Cdd:cd17645 239 NNYGPTENTvVATSFEIDKPYANIPIGKPIDNTRVYILDEALQ-------LQPIGVA-------------GELCIAGEGL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 235 FNEYWNKPQETREAFTPDGW------FRTGDTAVY-KDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVI 307
Cdd:cd17645 299 ARGYLNRPELTAEKFIVHPFvpgermYRTGDLAKFlPDGNIEFLGRLD-QQVKIRGYRIEPGEIEPFLMNHPLIELAAVL 377
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2113536441 308 GAPDSTWGQRVSAIVKLRDghTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd17645 378 AKEDADGRKYLVAYVTAPE--EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2-371 |
1.01e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 97.54 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLhHVHGVVNKLLCPLWVGATCVMLP--EFSPKEVW 79
Cdd:PRK12467 3242 VIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSF-SFDGAQERFLWTLICGGCLVVRDndLWDPEELW 3320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 80 EHFLstdSRSINVFMAVPTiysklidYYESHLAKPGIKDFvkamcqQKIRLMVSGSSALPVPTLER-WREITGHTLLERY 158
Cdd:PRK12467 3321 QAIH---AHRISIACFPPA-------YLQQFAEDAGGADC------ASLDIYVFGGEAVPPAAFEQvKRKLKPRGLTNGY 3384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 159 GMTEIG---MALTNPLNGprVPGSVGNPfpgVGVRIAteipqkEGSSYTVHAEGDAAGTEVFpgfedreGELQVRGPAVF 235
Cdd:PRK12467 3385 GPTEAVvtvTLWKCGGDA--VCEAPYAP---IGRPVA------GRSIYVLDGQLNPVPVGVA-------GELYIGGVGLA 3446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 236 NEYWNKPQETREAFTPDGW-------FRTGDTAVYKDN---SYwiLGRtsVD-IIKSGGYKISALEVERHLLAHPSIADV 304
Cdd:PRK12467 3447 RGYHQRPSLTAERFVADPFsgsggrlYRTGDLARYRADgviEY--LGR--IDhQVKIRGFRIELGEIEARLLQHPSVREA 3522
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2113536441 305 AVIgAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK12467 3523 VVL-ARDGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
1-273 |
4.85e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 94.66 E-value: 4.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALiDEWSwtkSDCI---------LHVLPLHHV--HGVVNKLL---CPLWVGAT 66
Cdd:PTZ00216 268 LIMYTSGTTGDPKGVMHTHGSLTAGILAL-EDRL---NDLIgppeedetyCSYLPLAHImeFGVTNIFLargALIGFGSP 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 67 ----------CVMLPEFSPKevwehflstdsrsinVFMAVPTIYSKLIDYYESHLAKPG-----------------IKD- 118
Cdd:PTZ00216 344 rtltdtfarpHGDLTEFRPV---------------FLIGVPRIFDTIKKAVEAKLPPVGslkrrvfdhayqsrlraLKEg 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 119 ----------F--VKAMCQQKIRLMVSGSSALPVPTLERWREITGhTLLERYGMTEI----GMALTNPLNgprvPGSVGN 182
Cdd:PTZ00216 409 kdtpywnekvFsaPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFG-MVIQGWGLTETvccgGIQRTGDLE----PNAVGQ 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 183 PFPGVGVRIA-------TEIPqkegssytvhaegdaagtevfpgfEDReGELQVRGPAVFNEYWNKPQETREAFTPDGWF 255
Cdd:PTZ00216 484 LLKGVEMKLLdteeykhTDTP------------------------EPR-GEILLRGPFLFKGYYKQEELTREVLDEDGWF 538
|
330
....*....|....*....
gi 2113536441 256 RTGDTA-VYKDNSYWILGR 273
Cdd:PTZ00216 539 HTGDVGsIAANGTLRIIGR 557
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
2-308 |
1.24e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 93.57 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNL---SAMVTALIDEWSWTKSDCILHVLPLHHVHGvVNKLLCP-LWVGATcVMLPEFSPke 77
Cdd:PRK12582 225 YLFTSGSTGMPKAVINTQRMMcanIAMQEQLRPREPDPPPPVSLDWMPWNHTMG-GNANFNGlLWGGGT-LYIDDGKP-- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 VWEHFLST--DSRSIN--VFMAVPTIYSKLIDYYEshlakpgiKDfvKAMCQ---QKIRLMVSGSSALPVPTLERWRE-- 148
Cdd:PRK12582 301 LPGMFEETirNLREISptVYGNVPAGYAMLAEAME--------KD--DALRRsffKNLRLMAYGGATLSDDLYERMQAla 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 149 --ITGH--TLLERYGMTEIGMALTNPLNGPRVPGSVGNPFPGVGVRIAteiPQkeGSSYtvhaegdaagtevfpgfedre 224
Cdd:PRK12582 371 vrTTGHriPFYTGYGATETAPTTTGTHWDTERVGLIGLPLPGVELKLA---PV--GDKY--------------------- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 225 gELQVRGPAVFNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSYWIL-----GRTSVDIIKSGGYKISALEVERHLLA-- 297
Cdd:PRK12582 425 -EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVDPDDPEKglifdGRVAEDFKLSTGTWVSVGTLRPDAVAac 503
|
330
....*....|.
gi 2113536441 298 HPSIADVAVIG 308
Cdd:PRK12582 504 SPVIHDAVVAG 514
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2-371 |
1.45e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 94.08 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHhVHGVVNKLLCPLWVGATCVML-------PEFS 74
Cdd:PRK05691 1278 VIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPIS-FDVSVWECFWPLITGCRLVLAgpgehrdPQRI 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 75 PKEVWEHFLSTdsrsinvFMAVPTIYSKLIDyyeshlaKPGIkdfvkAMCQqKIRLMVSGSSALPVPTLERWRE-ITGHT 153
Cdd:PRK05691 1357 AELVQQYGVTT-------LHFVPPLLQLFID-------EPLA-----AACT-SLRRLFSGGEALPAELRNRVLQrLPQVQ 1416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 154 LLERYGMTEIGMALTN----PLNGPRVPgsVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPGFEdreGELQV 229
Cdd:PRK05691 1417 LHNRYGPTETAINVTHwqcqAEDGERSP--IGRPLGNVLCRVL-----------------DAELNLLPPGVA---GELCI 1474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 230 RGPAVFNEYWNKPQETREAFTPDGW-------FRTGDTAVYK-DNSYWILGRTSVDIiKSGGYKISALEVERHLLAHPSI 301
Cdd:PRK05691 1475 GGAGLARGYLGRPALTAERFVPDPLgedgarlYRTGDRARWNaDGALEYLGRLDQQV-KLRGFRVEPEEIQARLLAQPGV 1553
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 302 ADVAVIgAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK05691 1554 AQAAVL-VREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
210-374 |
2.21e-20 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 92.36 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 210 DAAGTEVFPGfedREGELQVRGPAVFNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSYW-ILGRTSvDIIKSGGYKISA 288
Cdd:PRK10946 369 DADGNPLPQG---EVGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYItVVGREK-DQINRGGEKIAA 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 289 LEVERHLLAHPSIADVAVIGAPDSTWGQRVSAIVKLRDG-HTLSLKK-LKEWGravMAPYCIPAELIRVEEIPRNQMGKI 366
Cdd:PRK10946 445 EEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPlKAVQLRRfLREQG---IAEFKLPDRVECVDSLPLTAVGKV 521
|
....*...
gi 2113536441 367 NKKQLLAL 374
Cdd:PRK10946 522 DKKQLRQW 529
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
2-372 |
6.16e-20 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 91.11 E-value: 6.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCpLWVGATCVMLPE---FSPKEV 78
Cdd:PRK04813 148 IIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPT-LASGGTLVALPKdmtANFKQL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 79 WEHFLSTDsrsINVFMAVPT---IYSKLIDYYESHLakPGIKDFVkaMCQQkirlmvsgssALPVPTLErwreitghTLL 155
Cdd:PRK04813 227 FETLPQLP---INVWVSTPSfadMCLLDPSFNEEHL--PNLTHFL--FCGE----------ELPHKTAK--------KLL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 156 ER---------YGMTEIGMALT------NPLN-GPRVPgsVGNPFPGVGVRIATEipqkegssytvhaegdaAGTEVFPG 219
Cdd:PRK04813 282 ERfpsatiyntYGPTEATVAVTsieitdEMLDqYKRLP--IGYAKPDSPLLIIDE-----------------EGTKLPDG 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 220 fedREGELQVRGPAVFNEYWNKPQETREAF-TPDGW--FRTGDTAVYKDNSYWILGRtsVDI-IKSGGYKISALEVERHL 295
Cdd:PRK04813 343 ---EQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGYLEDGLLFYQGR--IDFqIKLNGYRIELEEIEQNL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 296 LAHPSIAD-VAVIGAPDSTWGQRVSAIVkLRDGH-------TLSLKK-LKEwgraVMAPYCIPAELIRVEEIPRNQMGKI 366
Cdd:PRK04813 418 RQSSYVESaVVVPYNKDHKVQYLIAYVV-PKEEDferefelTKAIKKeLKE----RLMEYMIPRKFIYRDSLPLTPNGKI 492
|
....*.
gi 2113536441 367 NKKQLL 372
Cdd:PRK04813 493 DRKALI 498
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
2-375 |
1.66e-19 |
|
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: 89.52 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSD------------CILHVLplhhvhgvvnkllCPLWVGAT-CV 68
Cdd:cd05918 111 VIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESrvlqfasytfdvSILEIF-------------TTLAAGGClCI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 69 MlpefSPKEVWEHFLSTDSRS-INVFMAVPTIySKLIDyyeshlakPgiKDFVKamcqqkIRLMVSGSSALPVPTLERWR 147
Cdd:cd05918 178 P----SEEDRLNDLAGFINRLrVTWAFLTPSV-ARLLD--------P--EDVPS------LRTLVLGGEALTQSDVDTWA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 148 EitGHTLLERYGMTE--IGMALTNPLNGPRvPGSVGNPFPGVgvriateipqkegsSYTVHaegdaagtevfPGFEDR-- 223
Cdd:cd05918 237 D--RVRLINAYGPAEctIAATVSPVVPSTD-PRNIGRPLGAT--------------CWVVD-----------PDNHDRlv 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 224 ----EGELQVRGPAVFNEYWNKPQETREAFTPD-GW------------FRTGDTAVY-KDNSYWILGRTSvDIIKSGGYK 285
Cdd:cd05918 289 pigaVGELLIEGPILARGYLNDPEKTAAAFIEDpAWlkqegsgrgrrlYRTGDLVRYnPDGSLEYVGRKD-TQVKIRGQR 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 286 ISALEVERHLLAHPSIAD---VAVIGAPDSTWGQRVSAIVKLRDGHTLS-----------------LKKLKEWGRAVMAP 345
Cdd:cd05918 368 VELGEIEHHLRQSLPGAKevvVEVVKPKDGSSSPQLVAFVVLDGSSSGSgdgdslflepsdefralVAELRSKLRQRLPS 447
|
410 420 430
....*....|....*....|....*....|
gi 2113536441 346 YCIPAELIRVEEIPRNQMGKINKKQLLALF 375
Cdd:cd05918 448 YMVPSVFLPLSHLPLTASGKIDRRALRELA 477
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
2-371 |
1.73e-19 |
|
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: 89.46 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILH-VLPLHHV--HGVVNKLLcplwVGATCVMLPEFSPKEV 78
Cdd:cd17656 133 IIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDKVLQfATCSFDVcyQEIFSTLL----SGGTLYIIREETKRDV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 79 WEHFLSTDSRSINVfMAVPTIYSKLIdyYESHLAKPGIKDFVKAMCQQKIRLMVSGssalpvpTLERWREITGHTLLERY 158
Cdd:cd17656 209 EQLFDLVKRHNIEV-VFLPVAFLKFI--FSEREFINRFPTCVKHIITAGEQLVITN-------EFKEMLHEHNVHLHNHY 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 159 GMTEIGMALTNPLN-GPRVP--GSVGNPFPGVGVRIATE--IPQKEGSSytvhaegdaagtevfpgfedreGELQVRGPA 233
Cdd:cd17656 279 GPSETHVVTTYTINpEAEIPelPPIGKPISNTWIYILDQeqQLQPQGIV----------------------GELYISGAS 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 234 VFNEYWNKPQETREAFTPDGW------FRTGDTAVY-KDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAV 306
Cdd:cd17656 337 VARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYlPDGNIEFLGRAD-HQVKIRGYRIELGEIEAQLLNHPGVSEAVV 415
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2113536441 307 IGAPDSTWGQRVSAIVKLRdgHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd17656 416 LDKADDKGEKYLCAYFVME--QELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
2-265 |
8.68e-19 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 88.01 E-value: 8.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSD--CILHVLPLHHVHG---VVNKLLC-------------PLWV 63
Cdd:PRK08180 214 FLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEppVLVDWLPWNHTFGgnhNLGIVLYnggtlyiddgkptPGGF 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 64 GATCVMLPEFSPkevwehflstdsrsiNVFMAVPTIYSKLIDYYEshlakpgiKDfvKAMCQ---QKIRLMVSGSSALPV 140
Cdd:PRK08180 294 DETLRNLREISP---------------TVYFNVPKGWEMLVPALE--------RD--AALRRrffSRLKLLFYAGAALSQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 141 PTLERWREITGHTLLER------YGMTEIGMALTNpLNGPRV-PGSVGNPFPGVGVRIateipqkegssytVHAEGDAag 213
Cdd:PRK08180 349 DVWDRLDRVAEATCGERirmmtgLGMTETAPSATF-TTGPLSrAGNIGLPAPGCEVKL-------------VPVGGKL-- 412
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2113536441 214 tevfpgfedregELQVRGPAVFNEYWNKPQETREAFTPDGWFRTGDTAVYKD 265
Cdd:PRK08180 413 ------------EVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVD 452
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2-346 |
1.04e-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: 87.13 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVnkllcplwVGATCVmLPEFSPkevweh 81
Cdd:cd05910 90 ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLFALFGPA--------LGLTSV-IPDMDP------ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 flstdSRSINVFMAVptIYSKLIDYYESH-LAKPGIKDFVKAMCQQK------IRLMVSGSSALPVPTLERWREITGHT- 153
Cdd:cd05910 155 -----TRPARADPQK--LVGAIRQYGVSIvFGSPALLERVARYCAQHgitlpsLRRVLSAGAPVPIALAARLRKMLSDEa 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 154 -LLERYGMTE------IG----MALTNPLNGPRVPGSVGNPFPGVGVRIateIPQKEGSsytVHAEGDAagTEVFPGfed 222
Cdd:cd05910 228 eILTPYGATEalpvssIGsrelLATTTAATSGGAGTCVGRPIPGVRVRI---IEIDDEP---IAEWDDT--LELPRG--- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 223 REGELQVRGPAVFNEYWNKPQETREAFTPDG----WFRTGDTAvYKDNS--YWILGRTSVDIIKSGGyKISALEVERHLL 296
Cdd:cd05910 297 EIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLG-YLDDEgrLWFCGRKAHRVITTGG-TLYTEPVERVFN 374
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2113536441 297 AHPSIADVAVIGApDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPY 346
Cdd:cd05910 375 THPGVRRSALVGV-GKPGCQLPVLCVEPLPGTITPRARLEQELRALAKDY 423
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
4-371 |
1.13e-18 |
|
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: 87.49 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQN--LSAMVTALIDEWSWTKSDCILHVLPLHHVHGvvnklLCPLWV----GATCVMLPEFSPKE 77
Cdd:cd05915 160 YTTGTTGLPKGVVYSHRAlvLHSLAASLVDGTALSEKDVVLPVVPMFHVNA-----WCLPYAatlvGAKQVLPGPRLDPA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 VWehFLSTDSRSINVFMAVPTIYSKLIDyyeshlakpgIKDFVKAMCQQKIRLMVSGSSalPVPTLERWREITGHTLLER 157
Cdd:cd05915 235 SL--VELFDGEGVTFTAGVPTVWLALAD----------YLESTGHRLKTLRRLVVGGSA--APRSLIARFERMGVEVRQG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTEIGMALTNPLNGPRvpgsvgnpFPGVGVRIATEIPQKEGSSYTVHAEGDAAGTEVFPGFEDREGE-LQVRGPAVFN 236
Cdd:cd05915 301 YGLTETSPVVVQNFVKSH--------LESLSEEEKLTLKAKTGLPIPLVRLRVADEEGRPVPKDGKALGeVQLKGPWITG 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 237 EYWNKPQETREAFTPDGWFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQ 316
Cdd:cd05915 373 GYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQE 452
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2113536441 317 RVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd05915 453 RPLAVVVPRGEKPTPEELNEHLLKAGFAKWQLPDAYVFAEEIPRTSAGKFLKRAL 507
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1-375 |
1.49e-18 |
|
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: 87.16 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSamVTALID---EWSWTKSDCILHVLPLHHVHGVVnKLLCPLWVGATCVM---LPEF- 73
Cdd:cd05968 240 MIIYTSGTTGKPKGTVHVHAGFP--LKAAQDmyfQFDLKPGDLLTWFTDLGWMMGPW-LIFGGLILGATMVLydgAPDHp 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 74 SPKEVWEhflSTDSRSINVFMAVPTIYSKLIDYYESHLAKPGIKdfvkamcqqkiRLMVSGSSALPVpTLERWREITGHT 153
Cdd:cd05968 317 KADRLWR---MVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLS-----------SLRVLGSTGEPW-NPEPWNWLFETV 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 154 LLERY------GMTEI-GMALTNPLNGPRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVFPgfedREGE 226
Cdd:cd05968 382 GKGRNpiinysGGTEIsGGILGNVLIKPIKPSSFNGPVPGMKADVL-----------------DESGKPARP----EVGE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 227 LQVRGP--AVFNEYWNKPQETREAF---TPDGWFRtGDTAVYKDNSYW-ILGRtSVDIIKSGGYKISALEVERHLLAHPS 300
Cdd:cd05968 441 LVLLAPwpGMTRGFWRDEDRYLETYwsrFDNVWVH-GDFAYYDEEGYFyILGR-SDDTINVAGKRVGPAEIESVLNAHPA 518
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113536441 301 IADVAVIGAPDSTWGQRVSAIVKLRDGHTLS---LKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLLALF 375
Cdd:cd05968 519 VLESAAIGVPHPVKGEAIVCFVVLKPGVTPTealAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAAY 596
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
2-371 |
2.14e-18 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 86.88 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLstHQNLSAMV-TALIDEWS---------WTKSDCILHVLPLHHVHGvvnkllcPLWVGATCVML- 70
Cdd:PLN02654 280 LLYTSGSTGKPKGVL--HTTGGYMVyTATTFKYAfdykptdvyWCTADCGWITGHSYVTYG-------PMLNGATVLVFe 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 71 --PEF-SPKEVWEhflSTDSRSINVFMAVPTIYSKLIdyyeshlaKPGiKDFVKAMCQQKIRLMvsGSSALPV-PTLERW 146
Cdd:PLN02654 351 gaPNYpDSGRCWD---IVDKYKVTIFYTAPTLVRSLM--------RDG-DEYVTRHSRKSLRVL--GSVGEPInPSAWRW 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 147 -REITGHT---LLERYGMTEIGMALTNPLNG--PRVPGSVGNPFPGVGVRIAteipqkegssytvhaegDAAGTEVfpgf 220
Cdd:PLN02654 417 fFNVVGDSrcpISDTWWQTETGGFMITPLPGawPQKPGSATFPFFGVQPVIV-----------------DEKGKEI---- 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 221 edrEGE----LQVRG--PAVFNE-YWNKPQETREAFTP-DGWFRTGDTAVY-KDNSYWILGRTSvDIIKSGGYKISALEV 291
Cdd:PLN02654 476 ---EGEcsgyLCVKKswPGAFRTlYGDHERYETTYFKPfAGYYFSGDGCSRdKDGYYWLTGRVD-DVINVSGHRIGTAEV 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 292 ERHLLAHPSIADVAVIGAPDSTWGQRVSAIVKLRDG--HTLSLKK-LKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINK 368
Cdd:PLN02654 552 ESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGvpYSEELRKsLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMR 631
|
...
gi 2113536441 369 KQL 371
Cdd:PLN02654 632 RIL 634
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
290-365 |
2.34e-18 |
|
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: 78.74 E-value: 2.34e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113536441 290 EVERHLLAHPSIADVAVIGAPDSTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGK 365
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
2-308 |
2.49e-18 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 86.43 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTA-----LIDEWSWTKSDCILHVLPLHHVHGVVNKLLCpLWVGATCvmlpefspk 76
Cdd:PLN02861 225 IMYTSGTTGEPKGVILTNRAIIAEVLStdhllKVTDRVATEEDSYFSYLPLAHVYDQVIETYC-ISKGASI--------- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 77 EVWE---HFLSTDSRSI--NVFMAVPTIY------------------SKLIDY------------YESHLAKPGIKDFVK 121
Cdd:PLN02861 295 GFWQgdiRYLMEDVQALkpTIFCGVPRVYdriytgimqkissggmlrKKLFDFaynyklgnlrkgLKQEEASPRLDRLVF 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 122 AMCQQ----KIRLMVSGSSALPVPTLERWREITGHTLLERYGMTE-IGMALTNPLNGPRVPGSVGNPFPGVGVRIATeIP 196
Cdd:PLN02861 375 DKIKEglggRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTEsCGGCFTSIANVFSMVGTVGVPMTTIEARLES-VP 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 197 QKegssytvhaeGDAAGTEVfpgfedREGELQVRGPAVFNEYWNKPQETREAFTpDGWFRTGDTAVYKDN-SYWILGRTS 275
Cdd:PLN02861 454 EM----------GYDALSDV------PRGEICLRGNTLFSGYHKRQDLTEEVLI-DGWFHTGDIGEWQPNgAMKIIDRKK 516
|
330 340 350
....*....|....*....|....*....|....
gi 2113536441 276 vDIIK-SGGYKISALEVERHLLAHPSIADVAVIG 308
Cdd:PLN02861 517 -NIFKlSQGEYVAVENLENTYSRCPLIASIWVYG 549
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
2-371 |
2.65e-18 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 87.02 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQnlsAMVTALI---DEWSWTKSDCILHVLPL-HHVHgvVNKLLCPLWVGATCVMLPEFS--- 74
Cdd:PRK10252 603 IIFTSGSTGRPKGVMVGQT---AIVNRLLwmqNHYPLTADDVVLQKTPCsFDVS--VWEFFWPFIAGAKLVMAEPEAhrd 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 75 PKEVWEHFlstDSRSINVFMAVPTIYSklidyyeSHLAKPGIKDFVKAmCQQKIRLMVSGSsALPVPTLERWREITGHTL 154
Cdd:PRK10252 678 PLAMQQFF---AEYGVTTTHFVPSMLA-------AFVASLTPEGARQS-CASLRQVFCSGE-ALPADLCREWQQLTGAPL 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 155 LERYGMTEIGMALTN-PLNGPRVPGSVGNPFP------GVGVRIAteipqkegssytvhaegDAAGTEVFPGFEdreGEL 227
Cdd:PRK10252 746 HNLYGPTEAAVDVSWyPAFGEELAAVRGSSVPigypvwNTGLRIL-----------------DARMRPVPPGVA---GDL 805
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 228 QVRGPAVFNEYWNKPQETREAFTPDGW------FRTGDTAVYKDN---SYwiLGRtSVDIIKSGGYKISALEVERHLLAH 298
Cdd:PRK10252 806 YLTGIQLAQGYLGRPDLTASRFIADPFapgermYRTGDVARWLDDgavEY--LGR-SDDQLKIRGQRIELGEIDRAMQAL 882
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2113536441 299 PSIADVA----VIGAPDSTWG--QRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:PRK10252 883 PDVEQAVthacVINQAAATGGdaRQLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2-373 |
3.14e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 86.76 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHhVHGVVNKLLCPLWVGATCVMLPE--FSPKE-- 77
Cdd:PRK05691 2338 LIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSIN-FDAASERLLVPLLCGARVVLRAQgqWGAEEic 2416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 --VWEHflstdsrSINVFMAVPTIYSKLIDYyeshLAKPGikdfvkamCQQKIRLMVSGSSALPVPTLERWREITGHTLL 155
Cdd:PRK05691 2417 qlIREQ-------QVSILGFTPSYGSQLAQW----LAGQG--------EQLPVRMCITGGEALTGEHLQRIRQAFAPQLF 2477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 156 -ERYGMTE-IGMALTNpLNGPRVPGSVGNPFPG--VGVRIAteipqkegssYTVHAegDAAgteVFPgfEDREGELQVRG 231
Cdd:PRK05691 2478 fNAYGPTEtVVMPLAC-LAPEQLEEGAASVPIGrvVGARVA----------YILDA--DLA---LVP--QGATGELYVGG 2539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 232 PAVFNEYWNKPQETREAFTPDGW-------FRTGDTAVYKDN---SYwiLGRTSVDIiKSGGYKISALEVERHLLAHPSI 301
Cdd:PRK05691 2540 AGLAQGYHDRPGLTAERFVADPFaadggrlYRTGDLVRLRADglvEY--VGRIDHQV-KIRGFRIELGEIESRLLEHPAV 2616
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113536441 302 ADVAVIgAPDSTWGQR-----VSAIVKLRDGHTLSLKK-LKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQLLA 373
Cdd:PRK05691 2617 REAVVL-ALDTPSGKQlagylVSAVAGQDDEAQAALREaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPA 2693
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
2-371 |
9.36e-18 |
|
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: 84.37 E-value: 9.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEW--SWTKSDCIL----HVLPLHhvhgvVNKLLCPLWVGATCVMLPE--- 72
Cdd:cd17648 99 AIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYfgRDNGDEAVLffsnYVFDFF-----VEQMTLALLNGQKLVVPPDemr 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 73 FSPKEVWEHflsTDSRSINVFMAVPTIYSkLIDYYE-SHLAkpgikdfvkamcqqkiRLMVSGSsALPVPTLERWREITG 151
Cdd:cd17648 174 FDPDRFYAY---INREKVTYLSGTPSVLQ-QYDLARlPHLK----------------RVDAAGE-EFTAPVFEKLRSRFA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 152 HTLLERYGMTEIgmALTNP----LNGPRVPGSVGNPFPGVgvriateipqkegssyTVHAEGDAAGTEVFPGFedreGEL 227
Cdd:cd17648 233 GLIINAYGPTET--TVTNHkrffPGDQRFDKSLGRPVRNT----------------KCYVLNDAMKRVPVGAV----GEL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 228 QVRGPAVFNEYWNKPQETREAFTPDGW--------------FRTGDTAVYKDNSYW-ILGRTSVDIiKSGGYKISALEVE 292
Cdd:cd17648 291 YLGGDGVARGYLNRPELTAERFLPNPFqteqerargrnarlYKTGDLVRWLPSGELeYLGRNDFQV-KIRGQRIEPGEVE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 293 RHLLAHPSIADVAVIGA--PDSTWGQRVSAIVK--LRDGHTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINK 368
Cdd:cd17648 370 AALASYPGVRECAVVAKedASQAQSRIQKYLVGyyLPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDV 449
|
...
gi 2113536441 369 KQL 371
Cdd:cd17648 450 RAL 452
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
4-273 |
1.58e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 84.83 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNLSAmvtaliDEW--------SWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLpefSP 75
Cdd:PRK05691 173 YTSGSTALPKGVQVSHGNLVA------NEQlirhgfgiDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLM---SP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 76 kevwehflstdsrsiNVFMAVPTIYSKLIDYYESHLAkpGIKDFVKAMCQQKI-------------RLMVSGSSALPVPT 142
Cdd:PRK05691 244 ---------------AYFLERPLRWLEAISEYGGTIS--GGPDFAYRLCSERVsesalerldlsrwRVAYSGSEPIRQDS 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 143 LERWRE------ITGHTLLERYGMTEIGMALTNPLNGPRVP------------------GSV----GNPFPGVGVRIAte 194
Cdd:PRK05691 307 LERFAEkfaacgFDPDSFFASYGLAEATLFVSGGRRGQGIPaleldaealarnraepgtGSVlmscGRSQPGHAVLIV-- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 195 ipqkegssytvhaegDAAGTEVFPgfEDREGELQVRGPAVFNEYWNKPQETREAFTP-DG--WFRTGDTAVYKDNSYWIL 271
Cdd:PRK05691 385 ---------------DPQSLEVLG--DNRVGEIWASGPSIAHGYWRNPEASAKTFVEhDGrtWLRTGDLGFLRDGELFVT 447
|
..
gi 2113536441 272 GR 273
Cdd:PRK05691 448 GR 449
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
1-308 |
1.78e-17 |
|
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: 83.95 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLS----AMVTALIDEWSWTKSDCILHVLPLHHVHG-VVNKLLCPLWVGATCvmlpeFSP 75
Cdd:cd05933 154 TLIYTSGTTGMPKGVMLSHDNITwtakAASQHMDLRPATVGQESVVSYLPLSHIAAqILDIWLPIKVGGQVY-----FAQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 76 KEVWEHFLSTDSRSI--NVFMAVPTIYSKLIDYYESHLAKPGI---KDFVKAM---CQQKIRLMvSGSSALPVP------ 141
Cdd:cd05933 229 PDALKGTLVKTLREVrpTAFMGVPRVWEKIQEKMKAVGAKSGTlkrKIASWAKgvgLETNLKLM-GGESPSPLFyrlakk 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 142 -TLERWREITG----HTLL----------------------ERYGMTEIGMALT-NPLNGPRVpGSVGNPFPGVGVRIat 193
Cdd:cd05933 308 lVFKKVRKALGldrcQKFFtgaapisretlefflslnipimELYGMSETSGPHTiSNPQAYRL-LSCGKALPGCKTKI-- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 194 EIPQKEGSsytvhaegdaagtevfpgfedreGELQVRGPAVFNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSY-WILG 272
Cdd:cd05933 385 HNPDADGI-----------------------GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFlYITG 441
|
330 340 350
....*....|....*....|....*....|....*..
gi 2113536441 273 RTSVDIIKSGGYKISALEVERHLLAH-PSIADVAVIG 308
Cdd:cd05933 442 RIKELIITAGGENVPPVPIEDAVKKElPIISNAMLIG 478
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
3-265 |
2.12e-17 |
|
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: 83.64 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 3 IYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSD--CILHVLPLHHVHGVVNKLLCPLWVGATCVM---LPefSPKE 77
Cdd:cd05921 171 LFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYNGGTLYIddgKP--MPGG 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 VWEHFLSTDSRSINVFMAVPTIYSKLIDYYEshlakpgiKDfvKAMCQ---QKIRLMVSGSSALPVPTLERWREI----T 150
Cdd:cd05921 249 FEETLRNLREISPTVYFNVPAGWEMLVAALE--------KD--EALRRrffKRLKLMFYAGAGLSQDVWDRLQALavatV 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 151 GH--TLLERYGMTEIGMALTNPLNGPRVPGSVGNPFPGVGVRIATeipqkEGSSYtvhaegdaagtevfpgfedregELQ 228
Cdd:cd05921 319 GEriPMMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLVP-----SGGKY----------------------EVR 371
|
250 260 270
....*....|....*....|....*....|....*..
gi 2113536441 229 VRGPAVFNEYWNKPQETREAFTPDGWFRTGDTAVYKD 265
Cdd:cd05921 372 VKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAD 408
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
1-357 |
3.67e-17 |
|
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: 82.72 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMvTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEVWE 80
Cdd:cd05938 148 LYIYTSGTTGLPKAARISHLRVLQC-SGFLSLCGVTADDVIYITLPLYHSSGFLLGIGGCIELGATCVLKPKFSASQFWD 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 hflstDSRSINVfmavpTIysklIDYyeshlakpgIKDFVKAMCQQ---------KIRLMVsGSSALPvptlERWREIT- 150
Cdd:cd05938 227 -----DCRKHNV-----TV----IQY---------IGELLRYLCNQpqspndrdhKVRLAI-GNGLRA----DVWREFLr 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 151 --GHT-LLERYGMTEIGMALtnpLNGPRVPGSVGN---------PFPGVGVRIATEIPQKEGSSYTVHAEGDAAGTEVFP 218
Cdd:cd05938 279 rfGPIrIREFYGSTEGNIGF---FNYTGKIGAVGRvsylykllfPFELIKFDVEKEEPVRDAQGFCIPVAKGEPGLLVAK 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 219 gfedregelqVRGPAVFNEYWNKPQET-----REAFTP-DGWFRTGDTAVY-KDNSYWILGRTSvDIIKSGGYKISALEV 291
Cdd:cd05938 356 ----------ITQQSPFLGYAGDKEQTekkllRDVFKKgDVYFNTGDLLVQdQQNFLYFHDRVG-DTFRWKGENVATTEV 424
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2113536441 292 ERHLLAHPSIADVAVIGAPDSTWGQRVS-AIVKLRDGHTLSLKKLKEWGRAVMAPYCIPaELIRVEE 357
Cdd:cd05938 425 ADVLGLLDFLQEVNVYGVTVPGHEGRIGmAAVKLKPGHEFDGKKLYQHVREYLPAYARP-RFLRIQD 490
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
1-371 |
8.69e-16 |
|
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: 78.63 E-value: 8.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEVWE 80
Cdd:cd05937 91 ILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYHGTAAFLGACNCLMSGGTLALSRKFSASQFWK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 HFLstDSRSiNVFMAVptiySKLIDYYEShlAKPGIKDFvkamcQQKIRlMVSGSSALPvPTLERWREITG-HTLLERYG 159
Cdd:cd05937 171 DVR--DSGA-TIIQYV----GELCRYLLS--TPPSPYDR-----DHKVR-VAWGNGLRP-DIWERFRERFNvPEIGEFYA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 160 MTEIGMALTNPLNGPRVPGSVGN---------PFPGVGVRIATEIPQKEGSSYTVHAEGDAAGtevfpgfedREGELQVR 230
Cdd:cd05937 235 ATEGVFALTNHNVGDFGAGAIGHhglirrwkfENQVVLVKMDPETDDPIRDPKTGFCVRAPVG---------EPGEMLGR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 231 GPAV----FNEYWNKPQET-----REAFTP-DGWFRTGDTAVYKDNSYW-ILGRTSvDIIKSGGYKISALEVERHLLAHP 299
Cdd:cd05937 306 VPFKnreaFQGYLHNEDATesklvRDVFRKgDIYFRTGDLLRQDADGRWyFLDRLG-DTFRWKSENVSTTEVADVLGAHP 384
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113536441 300 SIADVAVIGA--PDSTwGQRVSAIVKLRDGHT----LSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd05937 385 DIAEANVYGVkvPGHD-GRAGCAAITLEESSAvpteFTKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
1-359 |
2.91e-15 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 77.44 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPefSP---KE 77
Cdd:PRK08043 369 LILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAEVFLYP--SPlhyRI 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 VWEhfLSTDsRSINVFMAVPTIyskLIDYyeSHLAKPgiKDFVkamcqqKIRLMVSGSSALPVPTLERWREITGHTLLER 157
Cdd:PRK08043 447 VPE--LVYD-RNCTVLFGTSTF---LGNY--ARFANP--YDFA------RLRYVVAGAEKLQESTKQLWQDKFGLRILEG 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTEIgmALTNPLNGPRV--PGSVGNPFPGVGVRIateIPqkegssytvhaegdaagtevFPGFEDrEGELQVRGPAVF 235
Cdd:PRK08043 511 YGVTEC--APVVSINVPMAakPGTVGRILPGMDARL---LS--------------------VPGIEQ-GGRLQLKGPNIM 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 236 NEY--------WNKPQ-ETREAFTPDGWFRTGDTAVYKDNSY-WILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVA 305
Cdd:PRK08043 565 NGYlrvekpgvLEVPTaENARGEMERGWYDTGDIVRFDEQGFvQIQGRAK-RFAKIAGEMVSLEMVEQLALGVSPDKQHA 643
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2113536441 306 VIGAPDSTWGQrvsAIVKLRDGHTLSLKKLKEWGRAVMAP-YCIPAELIRVEEIP 359
Cdd:PRK08043 644 TAIKSDASKGE---ALVLFTTDSELTREKLQQYAREHGVPeLAVPRDIRYLKQLP 695
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
2-338 |
7.62e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 75.68 E-value: 7.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGvvnklLCPLW----VGATCVmLPEFSPke 77
Cdd:PRK09029 140 MTLTSGSTGLPKAAVHTAQAHLASAEGVLSLMPFTAQDSWLLSLPLFHVSG-----QGIVWrwlyAGATLV-VRDKQP-- 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 78 vWEHFLSTDSR-SInvfmaVPTIYSKLIDYYESHLAkpgikdfvkamcQQKIRLmvsGSSALPVPTLERWREITGHTLLE 156
Cdd:PRK09029 212 -LEQALAGCTHaSL-----VPTQLWRLLDNRSEPLS------------LKAVLL---GGAAIPVELTEQAEQQGIRCWCG 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 157 rYGMTEigMALT------NPLNGprvpgsVGNPFPGVGVRIAteipqkegssytvhaegdaagtevfpgfedrEGELQVR 230
Cdd:PRK09029 271 -YGLTE--MASTvcakraDGLAG------VGSPLPGREVKLV-------------------------------DGEIWLR 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 231 GPAVFNEYWNKPQetreaFTP----DGWFRTGDTAVYKDNSYWILGRTSVDIIkSGGYKISALEVERHLLAHPSIADVAV 306
Cdd:PRK09029 311 GASLALGYWRQGQ-----LVPlvndEGWFATRDRGEWQNGELTILGRLDNLFF-SGGEGIQPEEIERVINQHPLVQQVFV 384
|
330 340 350
....*....|....*....|....*....|..
gi 2113536441 307 IGAPDSTWGQRVSAIVKLRDghTLSLKKLKEW 338
Cdd:PRK09029 385 VPVADAEFGQRPVAVVESDS--EAAVVNLAEW 414
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
3-355 |
1.38e-13 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 71.83 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 3 IYTSGTTGRPKGVLSTH---QNLSAMVTALIDEwswTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEVW 79
Cdd:PRK08279 205 IYTSGTTGLPKAAVMSHmrwLKAMGGFGGLLRL---TPDDVLYCCLPLYHNTGGTVAWSSVLAAGATLALRRKFSASRFW 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 80 EhflstDSR--SINVFMAVptiySKLIDYYESHLAKPGIKDfvkamcqQKIRLMVsGSSALPvptlERWREITG----HT 153
Cdd:PRK08279 282 D-----DVRryRATAFQYI----GELCRYLLNQPPKPTDRD-------HRLRLMI-GNGLRP----DIWDEFQQrfgiPR 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 154 LLERYGMTEIGMALTNPLNGP----RVPGSVGNPFPGVGVRIATEIPQKegssytvhaegDAAG--TEVFPGfEDRE--G 225
Cdd:PRK08279 341 ILEFYAASEGNVGFINVFNFDgtvgRVPLWLAHPYAIVKYDVDTGEPVR-----------DADGrcIKVKPG-EVGLliG 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 226 ELQVRGPavFNEYwNKPQET-----REAFTP-DGWFRTGDTAVYKDNSYWILgrtsVDII------KsgGYKISALEVER 293
Cdd:PRK08279 409 RITDRGP--FDGY-TDPEASekkilRDVFKKgDAWFNTGDLMRDDGFGHAQF----VDRLgdtfrwK--GENVATTEVEN 479
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2113536441 294 HLLAHPSIADVAVIGA--PDsTWGQRVSAIVKLRDGHTLSLKKLKEWGRAVMAPYCIPAeLIRV 355
Cdd:PRK08279 480 ALSGFPGVEEAVVYGVevPG-TDGRAGMAAIVLADGAEFDLAALAAHLYERLPAYAVPL-FVRL 541
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
2-273 |
3.01e-13 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 71.21 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALID-----EWSWTKSDCILHVLPLHHVHGVVNKLlCPLWVGATCvmlpEFSPK 76
Cdd:PLN02614 228 IMYTSGTTGDPKGVMISNESIVTLIAGVIRllksaNAALTVKDVYLSYLPLAHIFDRVIEE-CFIQHGAAI----GFWRG 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 77 EVweHFLSTDSRSI--NVFMAVPTI----YSKL-------------------------IDYYESHL-AKPGIKDFVKAMC 124
Cdd:PLN02614 303 DV--KLLIEDLGELkpTIFCAVPRVldrvYSGLqkklsdggflkkfvfdsafsykfgnMKKGQSHVeASPLCDKLVFNKV 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 125 QQ----KIRLMVSGSSALPVPTLERWREITGHTLLERYGMTE--IGMALTNPlNGPRVPGSVGNPFPGVGVRIATeIPQk 198
Cdd:PLN02614 381 KQglggNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTEscAGTFVSLP-DELDMLGTVGPPVPNVDIRLES-VPE- 457
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2113536441 199 egssytvhAEGDAAGTEVfpgfedrEGELQVRGPAVFNEYWNKPQETREAFTpDGWFRTGDTAVYK-DNSYWILGR 273
Cdd:PLN02614 458 --------MEYDALASTP-------RGEICIRGKTLFSGYYKREDLTKEVLI-DGWLHTGDVGEWQpNGSMKIIDR 517
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
2-371 |
5.12e-13 |
|
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: 69.81 E-value: 5.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCpLWVGATCVMLPEfSPKEVWEH 81
Cdd:cd17654 123 VIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLS-LSSGATLLIVPT-SVKVLPSK 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 82 FL-STDSR-SINVFMAVPTIYSKlidyyeshLAKPGIKDFVKAMcQQKIRLMVSGSSALPVPT-LERWREITGHT-LLER 157
Cdd:cd17654 201 LAdILFKRhRITVLQATPTLFRR--------FGSQSIKSTVLSA-TSSLRVLALGGEPFPSLViLSSWRGKGNRTrIFNI 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 YGMTEIGM-ALTNPLNGPRVPGSVGnpFPGVGVRIatEIPQKEGSSYTvhaegdaagTEVFPGFEDREGELQvrgpavfn 236
Cdd:cd17654 272 YGITEVSCwALAYKVPEEDSPVQLG--SPLLGTVI--EVRDQNGSEGT---------GQVFLGGLNRVCILD-------- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 237 EYWNKPQETreaftpdgWFRTGDTAVYKDNSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSIADVAVigapdsTW-- 314
Cdd:cd17654 331 DEVTVPKGT--------MRATGDFVTVKDGELFFLGRKD-SQIKRRGKRINLDLIQQVIESCLGVESCAV------TLsd 395
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2113536441 315 GQR-----VSAIVKLRDGHTLSLKKLkewgravmAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd17654 396 QQRliafiVGESSSSRIHKELQLTLL--------SSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
2-322 |
1.37e-12 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 69.07 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTAlID------EWSWTKSDCILHVLPLHHV-------------------HGVVNK 56
Cdd:PLN02430 225 IMYTSGTSGDPKGVVLTHEAVATFVRG-VDlfmeqfEDKMTHDDVYLSFLPLAHIldrmieeyffrkgasvgyyHGDLNA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 57 L------LCP-LWVGATCVM----------LPEFSPkevwehflstdsRSINVFMAvptIYSKLIDY----YESHLAKPg 115
Cdd:PLN02430 304 LrddlmeLKPtLLAGVPRVFerihegiqkaLQELNP------------RRRLIFNA---LYKYKLAWmnrgYSHKKASP- 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 116 IKDF-----VKAMCQQKIRLMVSGSSALPVPTLERWREITGHTLLERYGMTEI--GMALTNPLNGPRVpGSVGNPFPGVG 188
Cdd:PLN02430 368 MADFlafrkVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETlgPTTLGFPDEMCML-GTVGAPAVYNE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 189 VRIaTEIPQKEgssYTvhaegdaagtevfPGFEDREGELQVRGPAVFNEYWNKPQETREAFTpDGWFRTGDTA-VYKDNS 267
Cdd:PLN02430 447 LRL-EEVPEMG---YD-------------PLGEPPRGEICVRGKCLFSGYYKNPELTEEVMK-DGWFHTGDIGeILPNGV 508
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2113536441 268 YWILGRTSvDIIK-SGGYKISALEVERHLLAHPSIADVAVIGapDSTWGQRVSAIV 322
Cdd:PLN02430 509 LKIIDRKK-NLIKlSQGEYVALEYLENVYGQNPIVEDIWVYG--DSFKSMLVAVVV 561
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
5-293 |
1.39e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 68.87 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 5 TSGTTGRPKGVLSTHQNLSAMVTALIDEWSWT-KSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLpefSPKEvwehfl 83
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKV---TPMD------ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 84 stdsrsinvFMAVPTIYSKLIDYYE-SHLAKPGIKD--FVKAMCQQ---------KIRLMVSGSSALPVPTLERWREITG 151
Cdd:PRK07768 231 ---------FLRDPLLWAELISKYRgTMTAAPNFAYalLARRLRRQakpgafdlsSLRFALNGAEPIDPADVEDLLDAGA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 152 ------HTLLERYGMTEIGMALT--NPLNGPR---------------VPGSVGN---------PFPGVGVRIAteipqke 199
Cdd:PRK07768 302 rfglrpEAILPAYGMAEATLAVSfsPCGAGLVvdevdadllaalrraVPATKGNtrrlatlgpPLPGLEVRVV------- 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 200 gssytvhaegDAAGTeVFPgfeDRE-GELQVRGPAVfNEYWNKPQETREAFTPDGWFRTGDTAVYKDNSY-WILGRTSvD 277
Cdd:PRK07768 375 ----------DEDGQ-VLP---PRGvGVIELRGESV-TPGYLTMDGFIPAQDADGWLDTGDLGYLTEEGEvVVCGRVK-D 438
|
330
....*....|....*.
gi 2113536441 278 IIKSGGYKISALEVER 293
Cdd:PRK07768 439 VIIMAGRNIYPTDIER 454
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
1-259 |
4.87e-12 |
|
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: 67.10 E-value: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMvtalidewsWTKSDCI----------LHVLPLHHVHGvVNKLLCPLWVGATCVML 70
Cdd:cd17632 227 LLIYTSGSTGTPKGAMYTERLVATF---------WLKVSSIqdirppasitLNFMPMSHIAG-RISLYGTLARGGTAYFA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 71 PEFSPKEVWEHFLSTdsRSINVFMaVPTIYSKLIDYYESHLAKPGI--------KDFVKAMCQQKI---RLM--VSGSSA 137
Cdd:cd17632 297 AASDMSTLFDDLALV--RPTELFL-VPRVCDMLFQRYQAELDRRSVagadaetlAERVKAELRERVlggRLLaaVCGSAP 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 138 LPvPTLERWREIT-GHTLLERYGMTEIGMALTNplngprvpGSVGNP---------FPGVGVrIATEIPqkegssytvha 207
Cdd:cd17632 374 LS-AEMKAFMESLlDLDLHDGYGSTEAGAVILD--------GVIVRPpvldyklvdVPELGY-FRTDRP----------- 432
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2113536441 208 egdaagtevFPgfedrEGELQVRGPAVFNEYWNKPQETREAFTPDGWFRTGD 259
Cdd:cd17632 433 ---------HP-----RGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGD 470
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
1-335 |
6.45e-12 |
|
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: 66.61 E-value: 6.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMvTALIDEWSWTK-SDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEFSPKEVW 79
Cdd:cd05940 85 LYIYTSGTTGLPKAAIISHRRAWRG-GAFFAGSGGALpSDVLYTCLPLYHSTALIVGWSACLASGATLVIRKKFSASNFW 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 80 EhflstDSRSINVFMaVPTIySKLIDYYESHLAKPGIKDfvkamcqQKIRlMVSGSSALPvptlERWREITGH----TLL 155
Cdd:cd05940 164 D-----DIRKYQATI-FQYI-GELCRYLLNQPPKPTERK-------HKVR-MIFGNGLRP----DIWEEFKERfgvpRIA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 156 ERYGMTEIGMALTNPlngPRVPGSVGNPFPGVGVRIATEIPQKEGSSYTVHAEGDAAGTEVFPGfedREGEL--QVRGPA 233
Cdd:cd05940 225 EFYAATEGNSGFINF---FGKPGAIGRNPSLLRKVAPLALVKYDLESGEPIRDAEGRCIKVPRG---EPGLLisRINPLE 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 234 VFNEYWNkPQET-----REAFTP-DGWFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVAVI 307
Cdd:cd05940 299 PFDGYTD-PAATekkilRDVFKKgDAWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVY 377
|
330 340
....*....|....*....|....*....
gi 2113536441 308 GAP-DSTWGQRVSAIVKLRDGHTLSLKKL 335
Cdd:cd05940 378 GVQvPGTDGRAGMAAIVLQPNEEFDLSAL 406
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
2-366 |
1.45e-11 |
|
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: 65.76 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLsamvtalidewswtksdcILHVLPLHHVHGVV-----------------NKLLCPLWVG 64
Cdd:cd05943 254 ILYSSGTTGLPKCIVHGAGGT------------------LLQHLKEHILHCDLrpgdrlfyyttcgwmmwNWLVSGLAVG 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 65 ATCVML--PEFSPKEVWEHFLSTDSRsINVFMAVPtiysKLIDYYEshlaKPGIKdFVKAMCQQKIRLMVSGSSALPvPT 142
Cdd:cd05943 316 ATIVLYdgSPFYPDTNALWDLADEEG-ITVFGTSA----KYLDALE----KAGLK-PAETHDLSSLRTILSTGSPLK-PE 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 143 LERW--REITGHTLLERY-GMTEI--GMALTNPLNgPRVPGSVGNPFPGVGVRIATEipqkegssytvhaEGDAAGTEVf 217
Cdd:cd05943 385 SFDYvyDHIKPDVLLASIsGGTDIisCFVGGNPLL-PVYRGEIQCRGLGMAVEAFDE-------------EGKPVWGEK- 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 218 pgfedreGELQVRG--PAVFNEYWNKPQETR--EAF--TPDGWFRTGDTA-VYKDNSYWILGRtSVDIIKSGGYKISALE 290
Cdd:cd05943 450 -------GELVCTKpfPSMPVGFWNDPDGSRyrAAYfaKYPGVWAHGDWIeITPRGGVVILGR-SDGTLNPGGVRIGTAE 521
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2113536441 291 VERHLLAHPSIADVAVIGAPDSTWGQRVSAIVKLRDGHTLS---LKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKI 366
Cdd:cd05943 522 IYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDdelRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKK 600
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2-374 |
1.51e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 66.35 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQ-----NLSAMVTALIDEwswtkSDCILHVLPLHHVHGVVNKLLCPLWvGATCVMLPE---F 73
Cdd:PRK05691 3874 VIYTSGSTGLPKGVMVEQRgmlnnQLSKVPYLALSE-----ADVIAQTASQSFDISVWQFLAAPLF-GARVEIVPNaiaH 3947
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 74 SPKEVWEHflsTDSRSINVFMAVPTIYSKLIDyyESHLAKPGIkdfvkamcqqkiRLMVSGSSALPVPTLERWreitght 153
Cdd:PRK05691 3948 DPQGLLAH---VQAQGITVLESVPSLIQGMLA--EDRQALDGL------------RWMLPTGEAMPPELARQW------- 4003
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 154 lLERYgmTEIGmaLTNPLnGP----------RV--PGSVGNPFPgvgvrIATeiPQKEGSSYTVhaegDAAGTEVFPGfe 221
Cdd:PRK05691 4004 -LQRY--PQIG--LVNAY-GPaecsddvaffRVdlASTRGSYLP-----IGS--PTDNNRLYLL----DEALELVPLG-- 4064
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 222 dREGELQVRGPAVFNEYWNKPQETREAFTPDGW-------FRTGDTAVY-KDNSYWILGRtsVD-IIKSGGYKISALEVE 292
Cdd:PRK05691 4065 -AVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRrSDGVLEYVGR--IDhQVKIRGYRIELGEIE 4141
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 293 RHLLAHPSIADVAViGAPDSTWGQRVSAIVKLRDG---HTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKK 369
Cdd:PRK05691 4142 ARLHEQAEVREAAV-AVQEGVNGKHLVGYLVPHQTvlaQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRK 4220
|
....*
gi 2113536441 370 QLLAL 374
Cdd:PRK05691 4221 ALPAL 4225
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
4-273 |
2.53e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 65.14 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVMLPEfspkevweHFL 83
Cdd:PRK07769 187 YTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPA--------AFV 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 84 STDSRSINVFMAVPT----IYSKLIDYYESHLAKPGI-KDFVKAMCQQKIRLMVSGSSALPVPTLERWREITGHTLLER- 157
Cdd:PRK07769 259 RRPGRWIRELARKPGgtggTFSAAPNFAFEHAAARGLpKDGEPPLDLSNVKGLLNGSEPVSPASMRKFNEAFAPYGLPPt 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 158 -----YGMTEIGMAL-TNP--------------LNGPR---VPGSVGNPFPGVGV-RIATeipqkegSSYTVHAEGDAAg 213
Cdd:PRK07769 339 aikpsYGMAEATLFVsTTPmdeeptviyvdrdeLNAGRfveVPADAPNAVAQVSAgKVGV-------SEWAVIVDPETA- 410
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2113536441 214 TEVfPgfEDREGELQVRGPAVFNEYWNKPQETREAF---------------TPDG--WFRTGDTAVYKDNSYWILGR 273
Cdd:PRK07769 411 SEL-P--DGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegAPDDalWVRTGDYGVYFDGELYITGR 484
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
2-330 |
8.77e-11 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 63.43 E-value: 8.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALID--------EWSWTKSDCILHVLPLHHVHGvvnkllcPLWVGATCVM---L 70
Cdd:PRK10524 238 ILYTSGTTGKPKGVQRDTGGYAVALATSMDtifggkagETFFCASDIGWVVGHSYIVYA-------PLLAGMATIMyegL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 71 PEFSPKEVW----EHFlstdsrSINVFMAVPTIYSKLIDYYESHLAKPGIKdfvkamcqqKIRLMVSGSSALPVPTlERW 146
Cdd:PRK10524 311 PTRPDAGIWwrivEKY------KVNRMFSAPTAIRVLKKQDPALLRKHDLS---------SLRALFLAGEPLDEPT-ASW 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 147 -REITGHTLLERYGMTEIGMALTNPLNG----PRVPGSVGNPFPGVGVRIATEipqkegssytvhaegdAAGTEVFPGfe 221
Cdd:PRK10524 375 iSEALGVPVIDNYWQTETGWPILAIARGvedrPTRLGSPGVPMYGYNVKLLNE----------------VTGEPCGPN-- 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 222 dREGELQVRGP-------------AVF-NEYW---NKPQetreaftpdgwFRTGDTAVYKDNSYW-ILGRTSvDIIKSGG 283
Cdd:PRK10524 437 -EKGVLVIEGPlppgcmqtvwgddDRFvKTYWslfGRQV-----------YSTFDWGIRDADGYYfILGRTD-DVINVAG 503
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2113536441 284 YKISALEVERHLLAHPSIADVAVIGAPDSTWGQRVSAIVKLRDGHTL 330
Cdd:PRK10524 504 HRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSL 550
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
1-290 |
2.02e-10 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 62.14 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 1 MIIYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHHVHGVVNKLLCPLWVGATCVmlpeFS-----P 75
Cdd:PRK06334 187 VILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVPVV----FAynplyP 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 76 KEVWEHFlstDSRSINVFMAVPTIYSKLIDyyeshLAKPgikdfvKAMCQQKIRLMVSGSSALPVPTLERWREITGH-TL 154
Cdd:PRK06334 263 KKIVEMI---DEAKVTFLGSTPVFFDYILK-----TAKK------QESCLPSLRFVVIGGDAFKDSLYQEALKTFPHiQL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 155 LERYGMTEIGMALT-NPLNGPRVPGSVGNPFPGVGVRIATE---IPQKEGSSytvhaegdaagtevfpgfedreGELQVR 230
Cdd:PRK06334 329 RQGYGTTECSPVITiNTVNSPKHESCVGMPIRGMDVLIVSEetkVPVSSGET----------------------GLVLTR 386
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2113536441 231 GPAVFNEYW-NKPQETREAFTPDGWFRTGDTA-VYKDNSYWILGRTSvDIIKSGGYKIS--ALE 290
Cdd:PRK06334 387 GTSLFSGYLgEDFGQGFVELGGETWYVTGDLGyVDRHGELFLKGRLS-RFVKIGAEMVSleALE 449
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
5-293 |
4.39e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 60.94 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 5 TSGTTGRPKGVLSTHQNLSAMVTALIDEWSWT-KSDCILHVLPLHHVHGVVNkLLCPLWVGATCVMLPE--FSPKEV-WE 80
Cdd:PRK05851 160 TAGSTGTPRTAILSPGAVLSNLRGLNARVGLDaATDVGCSWLPLYHDMGLAF-LLTAALAGAPLWLAPTtaFSASPFrWL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 81 HFLStDSRSinVFMAVPTIYSKLIDYYESHLAKPGIKdfvkamcqqKIRLMVSGSSALPVPTLERWREITGH------TL 154
Cdd:PRK05851 239 SWLS-DSRA--TLTAAPNFAYNLIGKYARRVSDVDLG---------ALRVALNGGEPVDCDGFERFATAMAPfgfdagAA 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 155 LERYGMTEIGMALTNPLNG---------------PRVPGSVGNPFPGVGVRIAteipqkegssytvhaEGDAAgtevfPG 219
Cdd:PRK05851 307 APSYGLAESTCAVTVPVPGiglrvdevttddgsgARRHAVLGNPIPGMEVRIS---------------PGDGA-----AG 366
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2113536441 220 FEDRE-GELQVRGPAVFNEYWNKPqetreAFTPDGWFRTGDTAVYKDNSYWILGRTSvDIIKSGGYKISALEVER 293
Cdd:PRK05851 367 VAGREiGEIEIRGASMMSGYLGQA-----PIDPDDWFPTGDLGYLVDGGLVVCGRAK-ELITVAGRNIFPTEIER 435
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
2-310 |
1.09e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 60.13 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTA---LIDEWSwtKSDCILHVLPLHHVhgvvnkllcpLWVGATCVMLPE------ 72
Cdd:PLN02387 255 IMYTSGSTGLPKGVMMTHGNIVATVAGvmtVVPKLG--KNDVYLAYLPLAHI----------LELAAESVMAAVgaaigy 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 73 FSPkevweHFLSTDSRSI-------------NVFMAVPTIY------------------SKLID--YYESHLAKPG---- 115
Cdd:PLN02387 323 GSP-----LTLTDTSNKIkkgtkgdasalkpTLMTAVPAILdrvrdgvrkkvdakgglaKKLFDiaYKRRLAAIEGswfg 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 116 -------IKDF-----VKAMCQQKIRLMVSGSSALPVPTlERWREIT-GHTLLERYGMTEI--GMALTNPlNGPRVpGSV 180
Cdd:PLN02387 398 awgleklLWDAlvfkkIRAVLGGRIRFMLSGGAPLSGDT-QRFINIClGAPIGQGYGLTETcaGATFSEW-DDTSV-GRV 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 181 GNPFPGVGVRIateIPQKEGssytvhaeGDAAGTEVFPgfedrEGELQVRGPAVFNEYWNKPQETREAFTPDG----WFR 256
Cdd:PLN02387 475 GPPLPCCYVKL---VSWEEG--------GYLISDKPMP-----RGEIVIGGPSVTLGYFKNQEKTDEVYKVDErgmrWFY 538
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2113536441 257 TGDTA-VYKDNSYWILGRTSvDIIK--SGGYkISALEVERHLLAHPSIADVAVIGAP 310
Cdd:PLN02387 539 TGDIGqFHPDGCLEIIDRKK-DIVKlqHGEY-VSLGKVEAALSVSPYVDNIMVHADP 593
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
4-337 |
1.49e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 59.63 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNLSAMVTALIDE----------WSWtksdcilhvLPLHHVHGVVNKLLCPLwvgaTCVMlpef 73
Cdd:PRK09192 183 YSSGSTRFPRGVIITHRALMANLRAISHDglkvrpgdrcVSW---------LPFYHDMGLVGFLLTPV----ATQL---- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 74 spkevwehflSTDSRSINVFMAVPTIYSKLIDYYESHLA-KPgikDFVKAMCQQKIRlmvsgSSALPVPTLERWR----- 147
Cdd:PRK09192 246 ----------SVDYLPTRDFARRPLQWLDLISRNRGTISySP---PFGYELCARRVN-----SKDLAELDLSCWRvagig 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 148 --EITGHTL-----------------LERYGMTEIGMALTnplngprvpgsvgnpFPGVGVRIATEIPQKEGSSYTVHAE 208
Cdd:PRK09192 308 adMIRPDVLhqfaeafapagfddkafMPSYGLAEATLAVS---------------FSPLGSGIVVEEVDRDRLEYQGKAV 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 209 GDAAGTE----------VFPGFE------------DRE-GELQVRGPAVFNEYWNKpQETREAFTPDGWFRTGDTAVYKD 265
Cdd:PRK09192 373 APGAETRrvrtfvncgkALPGHEieirneagmplpERVvGHICVRGPSLMSGYFRD-EESQDVLAADGWLDTGDLGYLLD 451
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2113536441 266 NSYWILGRTSvDIIKSGGYKISALEVERHLLAHPSI--ADVAVIGAPDSTwGQRVSAIVKLRDGHTLSLKKLKE 337
Cdd:PRK09192 452 GYLYITGRAK-DLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQEN-GEKIVLLVQCRISDEERRGQLIH 523
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
2-274 |
7.52e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 57.42 E-value: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSTHQNLSAMVTALIDeWSWTKS---DCILHVLPLHHVHGVVNKLLCpLWVGATCvmlpefspkEV 78
Cdd:PTZ00342 309 IVYTSGTSGKPKGVMLSNKNLYNTVVPLCK-HSIFKKynpKTHLSYLPISHIYERVIAYLS-FMLGGTI---------NI 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 79 WEHFLSTDSRSI-----NVFMAVPTIYSKLIDYYESHLAK-PGIK--------------------DFVKAMCQ--QKIR- 129
Cdd:PTZ00342 378 WSKDINYFSKDIynskgNILAGVPKVFNRIYTNIMTEINNlPPLKrflvkkilslrksnnnggfsKFLEGITHisSKIKd 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 130 -------LMVSGSSALPvPTLErwREITghTLL-----ERYGMTEIGMALTnplngprVPGSVGNPFPGVGVRIATEIPQ 197
Cdd:PTZ00342 458 kvnpnleVILNGGGKLS-PKIA--EELS--VLLnvnyyQGYGLTETTGPIF-------VQHADDNNTESIGGPISPNTKY 525
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2113536441 198 KEGSSYTVHAegdaagTEVFPgfedrEGELQVRGPAVFNEYWNKPQETREAFTPDGWFRTGDTA-VYKDNSYWILGRT 274
Cdd:PTZ00342 526 KVRTWETYKA------TDTLP-----KGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVqINKNGSLTFLDRS 592
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
4-273 |
9.87e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 56.87 E-value: 9.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQNLSAMVTALIDEW---------------SWtksdcilhvLPLHHVHGVVNKLLCPLWVGATCV 68
Cdd:PRK05850 167 YTSGSTRTPAGVMVSHRNVIANFEQLMSDYfgdtggvpppdttvvSW---------LPFYHDMGLVLGVCAPILGGCPAV 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 69 MLpefSPKEV------WEHFLSTDSRSinvFMAVPTI-----YSKLIDyyeSHLAKPGIKDfvkamcqqkIRLMVSGSSA 137
Cdd:PRK05850 238 LT---SPVAFlqrparWMQLLASNPHA---FSAAPNFafelaVRKTSD---DDMAGLDLGG---------VLGIISGSER 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 138 LPVPTLERWRE------ITGHTLLERYGMTE--IGMALTNPLNGPRV---------PGSVGNPFPGVGVR-IATEIPQke 199
Cdd:PRK05850 300 VHPATLKRFADrfapfnLRETAIRPSYGLAEatVYVATREPGQPPESvrfdyeklsAGHAKRCETGGGTPlVSYGSPR-- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 200 gsSYTVHAEGDAAGTEVFPGfedREGELQVRGPAVFNEYWNKPQETREAF----------TPDG-WFRTGDTAVYKDNSY 268
Cdd:PRK05850 378 --SPTVRIVDPDTCIECPAG---TVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgTPEGpWLRTGDLGFISEGEL 452
|
....*
gi 2113536441 269 WILGR 273
Cdd:PRK05850 453 FIVGR 457
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
2-366 |
1.05e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 57.06 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 2 IIYTSGTTGRPKGVLSThqNLSAMVtALIDEWSWTKSDCILHVLPLHH------VHGVVNKLLCplwVGATCVMLPE--F 73
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRS--NGPHLV-GLKYYWRSIIEKDIPTVVFSHSsigwvsFHGFLYGSLS---LGNTFVMFEGgiI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 74 SPKEVWEHFLST-DSRSINVFMAVPTIYSKLIDYyeshlaKPGIKDFVKAMCQQKIRLMVSGSSALPVPTLERWREITGH 152
Cdd:PTZ00237 333 KNKHIEDDLWNTiEKHKVTHTLTLPKTIRYLIKT------DPEATIIRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 153 TLLERYGMTEIGMALTNPLNGPRVP-GSVGNPFPGVGVRIATEipqkEGSSYTVHAEGDAAGTEVFPgfedregelqvrg 231
Cdd:PTZ00237 407 KSSRGYGQTEIGITYLYCYGHINIPyNATGVPSIFIKPSILSE----DGKELNVNEIGEVAFKLPMP------------- 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 232 PAVFNEYWNKPQETREAFTP-DGWFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSIADVAVIGAP 310
Cdd:PTZ00237 470 PSFATTFYKNDEKFKQLFSKfPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIY 549
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2113536441 311 DSTWGQRVSAIVKLR---DGHTLSLKKLKEWGRAV----MAPYCIPAELIRVEEIPRNQMGKI 366
Cdd:PTZ00237 550 DPDCYNVPIGLLVLKqdqSNQSIDLNKLKNEINNIitqdIESLAVLRKIIIVNQLPKTKTGKI 612
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
4-282 |
1.73e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 53.21 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 4 YTSGTTGRPKGVLSTHQ----NLSAMVTAL------IDEWSWtksdcilhvLPLHHVHGVVNKLLCPLWVGATCVMLP-E 72
Cdd:PRK12476 200 YTSGSTRPPVGVEITHRavgtNLVQMILSIdlldrnTHGVSW---------LPLYHDMGLSMIGFPAVYGGHSTLMSPtA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 73 F--SPKEvWEHFLSTDSRSINVFMAVPTIYSKLIDyyESHLAKPGikdfvkamcqQKIRL----MVSGSSALPVPTLERW 146
Cdd:PRK12476 271 FvrRPQR-WIKALSEGSRTGRVVTAAPNFAYEWAA--QRGLPAEG----------DDIDLsnvvLIIGSEPVSIDAVTTF 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 147 REITGHTLLER------YGMTE--IGMALTNPLNGPRV----PGSVGNpfpGVGVRIATEIP---------QKEGSSYTV 205
Cdd:PRK12476 338 NKAFAPYGLPRtafkpsYGIAEatLFVATIAPDAEPSVvyldREQLGA---GRAVRVAADAPnavahvscgQVARSQWAV 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 206 HAEGDAaGTEVFPGfedREGELQVRGPAVFNEYWNKPQETREAF----------------TPDG--WFRTGDTAVYKDNS 267
Cdd:PRK12476 415 IVDPDT-GAELPDG---EVGEIWLHGDNIGRGYWGRPEETERTFgaklqsrlaegshadgAADDgtWLRTGDLGVYLDGE 490
|
330
....*....|....*
gi 2113536441 268 YWILGRTSVDIIKSG 282
Cdd:PRK12476 491 LYITGRIADLIVIDG 505
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
210-366 |
5.66e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 45.17 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 210 DAAGTEVfpgfEDREGELQVRGPA----VFneYWNKPQETR------EAFtPDGWfRTGDTA-VYKDNSYWILGRtSVDI 278
Cdd:PRK03584 453 DEDGRPV----VGEVGELVCTKPFpsmpLG--FWNDPDGSRyrdayfDTF-PGVW-RHGDWIeITEHGGVVIYGR-SDAT 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 279 IKSGGYKISALEVERHLLAHPSIADVAVIGAPDSTWGQRVSAIVKLRDGHTLS---LKKLKEWGRAVMAPYCIPAELIRV 355
Cdd:PRK03584 524 LNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDdalRARIRTTIRTNLSPRHVPDKIIAV 603
|
170
....*....|.
gi 2113536441 356 EEIPRNQMGKI 366
Cdd:PRK03584 604 PDIPRTLSGKK 614
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
3-371 |
8.52e-05 |
|
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: 44.34 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 3 IYTSGTTGRPKGVLSTHQNLSAMVTALIDEWSWTKSDCILHVLPLHH----VHGVVNKLLcplwVGATCVMLPEFSPKEV 78
Cdd:cd05939 110 IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMRPEDVVYDCLPLYHsaggIMGVGQALL----HGSTVVIRKKFSASNF 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 79 WEhflstDSRSINVfmavpTIYSKLIDYYESHLAKPgikdFVKAMCQQKIRLMVsGSSALPvptlERWREITGH----TL 154
Cdd:cd05939 186 WD-----DCVKYNC-----TIVQYIGEICRYLLAQP----PSEEEQKHNVRLAV-GNGLRP----QIWEQFVRRfgipQI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 155 LERYGMTEIGMALTNPLN-------GPRVPGSVgNPFPGVGVRIATEIPQKEGSSYTVHAEGDAAGTEVfpgfedreGEL 227
Cdd:cd05939 247 GEFYGATEGNSSLVNIDNhvgacgfNSRILPSV-YPIRLIKVDEDTGELIRDSDGLCIPCQPGEPGLLV--------GKI 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2113536441 228 QVRGPAV-FNEYWNKPQET----REAFTP-DGWFRTGDTAVYKDNSYWILGRTSVDIIKSGGYKISALEVERHLLAHPSI 301
Cdd:cd05939 318 IQNDPLRrFDGYVNEGATNkkiaRDVFKKgDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGL 397
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2113536441 302 ADVAVIGA--PDSTWGQRVSAIVKLRDghTLSLKKLKEWGRAVMAPYCIPAELIRVEEIPRNQMGKINKKQL 371
Cdd:cd05939 398 EDVVVYGVevPGVEGRAGMAAIVDPER--KVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
|
|
| |
