|
Name |
Accession |
Description |
Interval |
E-value |
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
8-433 |
0e+00 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 673.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 8 EEIEIMSREKLQFLQLQRLKKTINIA-ANSPYYKEVFSKNGITGDSIQSLDDIRKIPFTTKSDMRANYPFGLVAGDMkRD 86
Cdd:cd05913 1 EEIETMSRDELDALQLARLKWTVRHAyENVPFYRRKFAAAGIDPDDIKSLDDLRKLPFTTKEDLRDNYPFGLFAVPR-EK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 87 GVRIHSSSGTTGNPTVIVHSQHDLDSWANLVARCLYMVGIRKTDVFQNSSGYGMFTGGLGFQYGAERLGCLTVPAAAGNS 166
Cdd:cd05913 80 VVRIHASSGTTGKPTVVGYTKNDLDVWAELVARCLDAAGVTPGDRVQNAYGYGLFTGGLGFHYGAERLGALVIPAGGGNT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 167 KRQIKFISDFKTTALHAIPSYAIRLAEVFQEEGIDPRETTLKTLVIGAEPHTDEQRRKIERMLNVKAYNSFGMTEMNGPG 246
Cdd:cd05913 160 ERQLQLIKDFGPTVLCCTPSYALYLAEEAEEEGIDPRELSLKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGLTEIIGPG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 247 VAFECQEQNGMHFWEDCYLVEIIDPETGEPVPEGEIGELVLTTLDREMMPLIRYRTRDLTRILPGKCPCGRTHLRIDRIK 326
Cdd:cd05913 240 VAFECEEKDGLHIWEDHFIPEIIDPETGEPVPPGEVGELVFTTLTKEAMPLIRYRTRDITRLLPGPCPCGRTHRRIDRIT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 327 GRSDDMFIIKGVNIFPMQVEKILVQFPELGSNYLITLETVNNQDEMIVEVELSDLSTDNYiELEKIRRDIIRQLKDEILV 406
Cdd:cd05913 320 GRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHYQLILTRQEHLDELTIKVEVRPEADDDE-KLEALKQRLERHIKSVLGV 398
|
410 420
....*....|....*....|....*..
gi 2796583109 407 TPKVKLVKKGSLPQSEGKAVRVKDLRD 433
Cdd:cd05913 399 TVEVELVEPGSLPRSEGKAKRVIDKRK 425
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
2-431 |
0e+00 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 659.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 2 STQYWEEeIEIMSREKLQFLQLQRLKKTIN-IAANSPYYKEVFSKNGITGDSIQSLDDIRKIPFTTKSDMRANYPFGLVA 80
Cdd:COG1541 1 SEMYWNP-IETLSREELEALQLERLRATVArAYENSPFYRRKFDEAGVDPDDIKSLEDLAKLPFTTKEDLRDNYPFGLFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 81 GDMkRDGVRIHSSSGTTGNPTVIVHSQHDLDSWANLVARCLYMVGIRKTDVFQNSSGYGMFTGGLGFQYGAERLGCLTVP 160
Cdd:COG1541 80 VPL-EEIVRIHASSGTTGKPTVVGYTRKDLDRWAELFARSLRAAGVRPGDRVQNAFGYGLFTGGLGLHYGAERLGATVIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 161 AAAGNSKRQIKFISDFKTTALHAIPSYAIRLAEVFQEEGIDPRETTLKTLVIGAEPHTDEQRRKIERMLNVKAYNSFGMT 240
Cdd:COG1541 159 AGGGNTERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEEGIDPRDLSLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 241 EMnGPGVAFECQEQNGMHFWEDCYLVEIIDPETGEPVPEGEIGELVLTTLDREMMPLIRYRTRDLTRILPGKCPCGRTHL 320
Cdd:COG1541 239 EV-GPGVAYECEAQDGLHIWEDHFLVEIIDPETGEPVPEGEEGELVVTTLTKEAMPLIRYRTGDLTRLLPEPCPCGRTHP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 321 RIDRIKGRSDDMFIIKGVNIFPMQVEKILVQFPELGSNYLITLETVNNQDEMIVEVELSDlstdnYIELEKIRRDIIRQL 400
Cdd:COG1541 318 RIGRILGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAP-----GASLEALAEAIAAAL 392
|
410 420 430
....*....|....*....|....*....|.
gi 2796583109 401 KDEILVTPKVKLVKKGSLPQSEGKAVRVKDL 431
Cdd:COG1541 393 KAVLGLRAEVELVEPGSLPRSEGKAKRVIDR 423
|
|
| PA_CoA_ligase |
TIGR02155 |
phenylacetate-CoA ligase; Phenylacetate-CoA ligase (PA-CoA ligase) catalyzes the first step in ... |
11-432 |
3.96e-172 |
|
phenylacetate-CoA ligase; Phenylacetate-CoA ligase (PA-CoA ligase) catalyzes the first step in aromatic catabolism of phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Often located in a conserved gene cluster with enzymes involved in phenylacetic acid activation (paaG/H/I/J), phenylacetate-CoA ligase has been found among the proteobacteria as well as in gram positive prokaryotes. In the B-subclass proteobacterium Azoarcus evansii, phenylacetate-CoA ligase has been shown to be induced under aerobic and anaerobic growth conditions. It remains unclear however, whether this induction is due to the same enzyme or to another isoenzyme restricted to specific anaerobic growth conditions. [Energy metabolism, Other]
Pssm-ID: 131210 [Multi-domain] Cd Length: 422 Bit Score: 488.56 E-value: 3.96e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 11 EIMSREKLQFLQLQRLKKTINIA-ANSPYYKEVFSKNGITGDSIQSLDDIRKIPFTTKSDMRANYPFGLVAGDMKRDgVR 89
Cdd:TIGR02155 1 ETASLDELRALQTQRLKWTVKHAyENVPHYRKAFDAAGVHPDDLQSLSDLAKFPFTQKHDLRDNYPFGLFAVPREQV-VR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 90 IHSSSGTTGNPTVIVHSQHDLDSWANLVARCLYMVGIRKTDVFQNSSGYGMFTGGLGFQYGAERLGCLTVPAAAGNSKRQ 169
Cdd:TIGR02155 80 IHASSGTTGKPTVVGYTQNDIDTWSSVVARSIRAAGGRPGDLIHNAYGYGLFTGGLGAHYGAEKLGCTVVPISGGQTEKQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 170 IKFISDFKTTALHAIPSYAIRLAEVFQEEGIDPRETTLKTLVIGAEPHTDEQRRKIERMLNVKAYNSFGMTEMNGPGVAF 249
Cdd:TIGR02155 160 VQLIQDFKPDIIMVTPSYMLNLLEELKRMGIDPAQTSLQVGIFGAEPWTNAMRKEIEARLGMKATDIYGLSEVIGPGVAM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 250 EC-QEQNGMHFWEDCYLVEIIDPETGEPVPEGEIGELVLTTLDREMMPLIRYRTRDLTRILPGkcpCGRTHLRIDRIKGR 328
Cdd:TIGR02155 240 ECvETQDGLHIWEDHFYPEIIDPHTGEVLPDGEEGELVFTTLTKEALPVIRYRTRDLTRLLPG---TARTMRRMDRITGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 329 SDDMFIIKGVNIFPMQVEKILVQFPELGSNYLITLETVNNQDEMIVEVELSDLS--TDNYIELEKIRRDIIRQLKDEILV 406
Cdd:TIGR02155 317 SDDMLIIRGVNVFPTQLEEVILKMDELSPHYQLELTRNGHMDELTLKVELKPESytLRLHEQASLLAGEIQHTIKQEVGV 396
|
410 420
....*....|....*....|....*.
gi 2796583109 407 TPKVKLVKKGSLPQSEGKAVRVKDLR 432
Cdd:TIGR02155 397 SMDVHLVEPGSLPRSEGKARRVVDLR 422
|
|
| AMP-binding_C_2 |
pfam14535 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
337-432 |
1.34e-38 |
|
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: 434024 [Multi-domain] Cd Length: 96 Bit Score: 134.53 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 337 GVNIFPMQVEKILVQFPELGSNYLITLETVNNQDEMIVEVELSDLSTDNYIELEKIRRDIIRQLKDEILVTPKVKLVKKG 416
Cdd:pfam14535 1 GVNVFPSQIEEVLLEIPGVGPEYQIIVTREGGLDELEVKVEVAEGFSDEIKDLEALEKRIAKELKSVLGVSVKVELVEPG 80
|
90
....*....|....*.
gi 2796583109 417 SLPQSEGKAVRVKDLR 432
Cdd:pfam14535 81 TLPRSEGKAKRVIDLR 96
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
86-354 |
2.66e-34 |
|
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: 130.48 E-value: 2.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 86 DGVRIHSSSGTTGNPTVIVHSQHDLDSWANLVARclyMVGIRKTDVFQNSSGYGmFTGGLGFQYGAERLGCLTVPAAAGN 165
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAA---SGGLTEGDVFLSTLPLF-HIGGLFGLLGALLAGGTVVLLPKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 166 SKRQIKFISDFKTTALHAIPSYAIRLAEVFQEEGIDPRetTLKTLVIGAEPHTDEQRRKIERMLNVKAYNSFGMTEMNGP 245
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLS--SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 246 gVAFECQEQNGMHF------WEDCYlVEIIDPETGEpVPEGEIGELVLTT------------LDREMMPLIRYRTRDLTR 307
Cdd:cd04433 155 -VATGPPDDDARKPgsvgrpVPGVE-VRIVDPDGGE-LPPGEIGELVVRGpsvmkgywnnpeATAAVDEDGWYRTGDLGR 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2796583109 308 ILPGKCpcgrthLRIdriKGRSDDMFIIKGVNIFPMQVEKILVQFPE 354
Cdd:cd04433 232 LDEDGY------LYI---VGRLKDMIKSGGENVYPAEVEAVLLGHPG 269
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
93-353 |
9.73e-25 |
|
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: 105.66 E-value: 9.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 93 SSGTTGNPTVIVHSQHDLdsWANlVARCLYMVGIRKTDVFQN----SSGYGMFTGGLGfqygAERLGCLTVPAAAGNSKR 168
Cdd:COG0318 108 TSGTTGRPKGVMLTHRNL--LAN-AAAIAAALGLTPGDVVLValplFHVFGLTVGLLA----PLLAGATLVLLPRFDPER 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 169 QIKFISDFKTTALHAIPSYAIRLAEVFQEEGIDPRetTLKTLVIGAEPHTDEQRRKIERMLNVKAYNSFGMTEMnGPGVA 248
Cdd:COG0318 181 VLELIERERVTVLFGVPTMLARLLRHPEFARYDLS--SLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTET-SPVVT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 249 FECQEQNG---------MHFWEdcylVEIIDPEtGEPVPEGEIGELVlttldremmplIR-------------------- 299
Cdd:COG0318 258 VNPEDPGErrpgsvgrpLPGVE----VRIVDED-GRELPPGEVGEIV-----------VRgpnvmkgywndpeataeafr 321
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796583109 300 ---YRTRDLtrilpGkcpcgrthlRID-----RIKGRSDDMFIIKGVNIFPMQVEKILVQFP 353
Cdd:COG0318 322 dgwLRTGDL-----G---------RLDedgylYIVGRKKDMIISGGENVYPAEVEEVLAAHP 369
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
93-354 |
4.37e-20 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 92.48 E-value: 4.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 93 SSGTTGNPTVIVHSQHDLDSWANLVARclYMVGIRKTDVFQNSSGYGmFTGGLG-FQYGAERLGCLTV--------PAAA 163
Cdd:COG0365 192 TSGTTGKPKGVVHTHGGYLVHAATTAK--YVLDLKPGDVFWCTADIG-WATGHSyIVYGPLLNGATVVlyegrpdfPDPG 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 164 gnskRQIKFISDFKTTALHAIPSyAIRLaevFQEEGIDPRE----TTLKTLVIGAEPHTDEQRRKIERMLNVKAYNSFGM 239
Cdd:COG0365 269 ----RLWELIEKYGVTVFFTAPT-AIRA---LMKAGDEPLKkydlSSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQ 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 240 TEMNG--------------------PGVAfecqeqngmhfwedcylVEIIDpETGEPVPEGEIGELVLtTLDREMMPLiR 299
Cdd:COG0365 341 TETGGifisnlpglpvkpgsmgkpvPGYD-----------------VAVVD-EDGNPVPPGEEGELVI-KGPWPGMFR-G 400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796583109 300 Y-----RTRD--LTRIlPGKCpcgRTH--LRID-----RIKGRSDDMFIIKGVNIFPMQVEKILVQFPE 354
Cdd:COG0365 401 YwndpeRYREtyFGRF-PGWY---RTGdgARRDedgyfWILGRSDDVINVSGHRIGTAEIESALVSHPA 465
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
93-336 |
1.60e-18 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 86.98 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 93 SSGTTGNPTVIVHSQhdldswANLVARCLYMVGIRKTDVFQNSSGYGMFTGGLGFQYGaeRLGCLTVPAAAG-------- 164
Cdd:pfam00501 163 TSGTTGKPKGVMLTH------RNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFG--LSLGLLGPLLAGatvvlppg 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 165 ----NSKRQIKFISDFKTTALHAIPSYAIRLAEVFQEEGIDprETTLKTLVIGAEPHTDEQRRKIERMLNVKAYNSFGMT 240
Cdd:pfam00501 235 fpalDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRAL--LSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLT 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 241 EmNGPGVAFECQEQN--------GMHFWedCYLVEIIDPETGEPVPEGEIGELV---------------LT--TLDREMM 295
Cdd:pfam00501 313 E-TTGVVTTPLPLDEdlrslgsvGRPLP--GTEVKIVDDETGEPVPPGEPGELCvrgpgvmkgylndpeLTaeAFDEDGW 389
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2796583109 296 plirYRTRDLTRILPgkcpcgrthlriD---RIKGRSDDMFIIK 336
Cdd:pfam00501 390 ----YRTGDLGRRDE------------DgylEIVGRKKDQIKLG 417
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
86-353 |
9.87e-17 |
|
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: 81.89 E-value: 9.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 86 DGVRIHSSSGTTGNPTVIVHSQHdldSWANLVARCLYMVGIRKTDVF------QNSSGYGMFTGGlGFQYGAErlgclTV 159
Cdd:cd17631 99 DLALLMYTSGTTGRPKGAMLTHR---NLLWNAVNALAALDLGPDDVLlvvaplFHIGGLGVFTLP-TLLRGGT-----VV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 160 PAAAGNSKRQIKFISDFKTTALHAIPSYAIRLAEVFQEEGIDPreTTLKTLVIGAEPHTDEQRRKIERmLNVKAYNSFGM 239
Cdd:cd17631 170 ILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDL--SSLRAVIYGGAPMPERLLRALQA-RGVKFVQGYGM 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 240 TEMnGPGVAF----ECQEQNGM----HFWEDcylVEIIDPEtGEPVPEGEIGELVLTTLDreMMP-----------LIR- 299
Cdd:cd17631 247 TET-SPGVTFlspeDHRRKLGSagrpVFFVE---VRIVDPD-GREVPPGEVGEIVVRGPH--VMAgywnrpeataaAFRd 319
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2796583109 300 --YRTRDLTRIlpgkcpCGRTHLRI-DRIKgrsdDMFIIKGVNIFPMQVEKILVQFP 353
Cdd:cd17631 320 gwFHTGDLGRL------DEDGYLYIvDRKK----DMIISGGENVYPAEVEDVLYEHP 366
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
90-354 |
5.30e-15 |
|
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: 76.61 E-value: 5.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 90 IHSSSGTTGNPTVIVHS-QHDLDSWANLVarclYMVGIRKTDVFQNSSGYGMFTGGLGFQYGAERLGCLTVPAAAG--NS 166
Cdd:cd05972 86 IYFTSGTTGLPKGVLHThSYPLGHIPTAA----YWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPrfDA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 167 KRQIKFISDFKTTALHAIPSyAIRLaevFQEEGIDPRE-TTLKTLVIGAEPHTDEQRRKIERMLNVKAYNSFGMTEMNGP 245
Cdd:cd05972 162 ERILELLERYGVTSFCGPPT-AYRM---LIKQDLSSYKfSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 246 GVAFECQE--QNGMHFWEDCYLVEIIDPEtGEPVPEGEIGELVLTTLD-----------REMMPLIR---YRTRDLTRil 309
Cdd:cd05972 238 VGNFPDMPvkPGSMGRPTPGYDVAIIDDD-GRELPPGEEGDIAIKLPPpglflgyvgdpEKTEASIRgdyYLTGDRAY-- 314
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2796583109 310 pgKCPCGRThlridRIKGRSDDMFIIKGVNIFPMQVEKILVQFPE 354
Cdd:cd05972 315 --RDEDGYF-----WFVGRADDIIKSSGYRIGPFEVESALLEHPA 352
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
93-353 |
7.05e-13 |
|
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: 70.01 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 93 SSGTTGNPTVIVHSQHDLDSWANLVARCLymvGIRKTDVFQ--------NSSGYGMftgglgfqYGAERLGCLTVPAAAG 164
Cdd:cd05934 89 TSGTTGPPKGVVITHANLTFAGYYSARRF---GLGEDDVYLtvlplfhiNAQAVSV--------LAALSVGATLVLLPRF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 165 NSKRQIKFISDFKTTALHAIPSYAIRLAEvfQEEGIDPRETTLKtlVIGAEPHTDEQRRKIERMLNVKAYNSFGMTEmNG 244
Cdd:cd05934 158 SASRFWSDVRRYGATVTNYLGAMLSYLLA--QPPSPDDRAHRLR--AAYGAPNPPELHEEFEERFGVRLLEGYGMTE-TI 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 245 PGVAFECQEQNG-MHFWE--DCYLVEIIDPEtGEPVPEGEIGELVLTTLD---------------REMMPLIRYRTRDLT 306
Cdd:cd05934 233 VGVIGPRDEPRRpGSIGRpaPGYEVRIVDDD-GQELPAGEPGELVIRGLRgwgffkgyynmpeatAEAMRNGWFHTGDLG 311
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2796583109 307 RILPGkcpcGRTHLrIDRIKgrsdDMFIIKGVNIFPMQVEKILVQFP 353
Cdd:cd05934 312 YRDAD----GFFYF-VDRKK----DMIRRRGENISSAEVERAILRHP 349
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
94-355 |
1.14e-12 |
|
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: 69.48 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 94 SGTTGNPTVIVHSQHdldSWANLVARCLYMVGIRKTDVF-QNSSG---------YGMFTGGlgfqygaerlGCLTV--PA 161
Cdd:cd05930 102 SGSTGKPKGVMVEHR---GLVNLLLWMQEAYPLTPGDRVlQFTSFsfdvsvweiFGALLAG----------ATLVVlpEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 162 AAGNSKRQIKFISDFKTTALHAIPSYAIRLAEvfqeEGIDPRETTLKTLVIGAEPHTDEQRRKIERML-NVKAYNSFGMT 240
Cdd:cd05930 169 VRKDPEALADLLAEEGITVLHLTPSLLRLLLQ----ELELAALPSLRLVLVGGEALPPDLVRRWRELLpGARLVNLYGPT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 241 EMNGPGVAFECQEQNGmhFWE--------DCYLVEIIDPEtGEPVPEGEIGELVLTT-------LDRE-----------M 294
Cdd:cd05930 245 EATVDATYYRVPPDDE--EDGrvpigrpiPNTRVYVLDEN-LRPVPPGVPGELYIGGaglargyLNRPeltaerfvpnpF 321
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2796583109 295 MPLIR-YRTRDLTRILP-GkcpcgrthlRIDRIkGRSDDMFIIKGVNIFPMQVEKILVQFPEL 355
Cdd:cd05930 322 GPGERmYRTGDLVRWLPdG---------NLEFL-GRIDDQVKIRGYRIELGEIEAALLAHPGV 374
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
86-354 |
5.26e-12 |
|
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: 66.92 E-value: 5.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 86 DGVRIHSSSGTTGNPTVIVHSQHDLDSWANLVARCLymvGIRKTDV-------FQnssGYGMFTGGLG-FQYGAErlgcL 157
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERL---GLTEQDRlcipvplFH---CFGSVLGVLAcLTHGAT----M 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 158 TVPAAAGNSKRQIKFISDFKTTALHAIPSYAIRLAEVFQEEGIDPreTTLKTLVIGAEPHTDEQRRKIERMLNVKAYNS- 236
Cdd:cd05917 73 VFPSPSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDL--SSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIa 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 237 FGMTE------MNGPGVAFEcQEQNGMHFWEDCYLVEIIDPETGEPVPEGEIGELVLT-----------------TLDRE 293
Cdd:cd05917 151 YGMTEtspvstQTRTDDSIE-KRVNTVGRIMPHTEAKIVDPEGGIVPPVGVPGELCIRgysvmkgywndpektaeAIDGD 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796583109 294 MMplirYRTRDLTRILP-GKCpcgrthlridRIKGRSDDMFIIKGVNIFPMQVEKILVQFPE 354
Cdd:cd05917 230 GW----LHTGDLAVMDEdGYC----------RIVGRIKDMIIRGGENIYPREIEEFLHTHPK 277
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
93-353 |
1.90e-11 |
|
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: 65.85 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 93 SSGTTGNPTVIVHSQHDLDSWANLVARclYMVGIRKTDVFQNSSgygmftgGLGFQYGaerLG-CLTVPAAAGNS----- 166
Cdd:cd05959 171 SSGSTGRPKGVVHLHADIYWTAELYAR--NVLGIREDDVCFSAA-------KLFFAYG---LGnSLTFPLSVGATtvlmp 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 167 -----KRQIKFISDFKTTALHAIPS-YAIRLA-EVFQEEGidprETTLKTLVIGAEPHTDEQRRKIERMLNVKAYNSFGM 239
Cdd:cd05959 239 erptpAAVFKRIRRYRPTVFFGVPTlYAAMLAaPNLPSRD----LSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGS 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 240 TEM------NGPGvafecQEQNGMHFWE-DCYLVEIIDpETGEPVPEGEIGELVLTTLDREMMPLIRYrtrDLTR--ILP 310
Cdd:cd05959 315 TEMlhiflsNRPG-----RVRYGTTGKPvPGYEVELRD-EDGGDVADGEPGELYVRGPSSATMYWNNR---DKTRdtFQG 385
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2796583109 311 GKCPCGRTHLRIDR----IKGRSDDMFIIKGVNIFPMQVEKILVQFP 353
Cdd:cd05959 386 EWTRTGDKYVRDDDgfytYAGRADDMLKVSGIWVSPFEVESALVQHP 432
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
93-353 |
9.61e-11 |
|
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: 63.27 E-value: 9.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 93 SSGTTGNPTVIVHSQHDLDSWANLVARclYMVGIRKTDVFQNSSGYgMFTGGLG------FQYGAerlGCLTVPAAAgnS 166
Cdd:cd05958 105 TSGTTGAPKATMHFHRDPLASADRYAV--NVLRLREDDRFVGSPPL-AFTFGLGgvllfpFGVGA---SGVLLEEAT--P 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 167 KRQIKFISDFKTTALHAIP-SYAIRLAEVFQEEgidPRETTLKTLVIGAEPHTDEQRRKIERMLNVKAYNSFGMTEM--- 242
Cdd:cd05958 177 DLLLSAIARYKPTVLFTAPtAYRAMLAHPDAAG---PDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMfhi 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 243 ---NGPGVAFECQEQNGMhfweDCYLVEIIDPEtGEPVPEGEIGELVLTTldremmPLI-RY--RTRDLTRILPGKCPCG 316
Cdd:cd05958 254 fisARPGDARPGATGKPV----PGYEAKVVDDE-GNPVPDGTIGRLAVRG------PTGcRYlaDKRQRTYVQGGWNITG 322
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2796583109 317 RTHLRID----RIKGRSDDMFIIKGVNIFPMQVEKILVQFP 353
Cdd:cd05958 323 DTYSRDPdgyfRHQGRSDDMIVSGGYNIAPPEVEDVLLQHP 363
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
2-354 |
1.52e-09 |
|
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: 59.53 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 2 STQYWEEEIEIM---SREKLQFLQLQRLKKTINIAANSPYYKEVFskngITGDSIQSLDDIRKIPFTTKSDMRANYPfgL 78
Cdd:cd05911 66 NPIYTADELAHQlkiSKPKVIFTDPDGLEKVKEAAKELGPKDKII----VLDDKPDGVLSIEDLLSPTLGEEDEDLP--P 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 79 VAGDMKRDGVRIHSSSGTTGNP--TVIVHSqhdldswaNLVARCLYMVGIRKTDVFQNSSGYGMftggLGFQYGAerlGC 156
Cdd:cd05911 140 PLKDGKDDTAAILYSSGTTGLPkgVCLSHR--------NLIANLSQVQTFLYGNDGSNDVILGF----LPLYHIY---GL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 157 LTVPAAAGNSKRQI---KF--------ISDFKTTALHAIPSYAIRLAEvfqeegiDPRET-----TLKTLVIGAEPHTDE 220
Cdd:cd05911 205 FTTLASLLNGATVIimpKFdselfldlIEKYKITFLYLVPPIAAALAK-------SPLLDkydlsSLRVILSGGAPLSKE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 221 QRRKIERML-NVKAYNSFGMTEMNGPGvafeCQEQNGMHFWEDC------YLVEIIDPETGEPVPEGEIGELVL------ 287
Cdd:cd05911 278 LQELLAKRFpNATIKQGYGMTETGGIL----TVNPDGDDKPGSVgrllpnVEAKIVDDDGKDSLGPNEPGEICVrgpqvm 353
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796583109 288 -----------TTLDREMMplirYRTRDLTRILPGkcpcGRTHLrIDRIKgrsdDMFIIKGVNIFPMQVEKILVQFPE 354
Cdd:cd05911 354 kgyynnpeatkETFDEDGW----LHTGDIGYFDED----GYLYI-VDRKK----ELIKYKGFQVAPAELEAVLLEHPG 418
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
94-353 |
3.06e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 58.66 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 94 SGTTGNPTVIVHSQHDLdsWANLVARCLYMvGIRKTDVFQnsSGYGMF-TGGLGFQYGAERLGCLTVPAAAGNSKRQIKF 172
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNL--FLHSLAVCAWL-KLSRDDVYL--VIVPMFhVHAWGLPYLALMAGAKQVIPRRFDPENLLDL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 173 ISDFKTTALHAIPsyAIrLAEVFQEEGIDPRE-TTLKTLVIGAEP------HTDEQRRKIERmlnVKAYnsfGMTEMnGP 245
Cdd:PRK06187 251 IETERVTFFFAVP--TI-WQMLLKAPRAYFVDfSSLRLVIYGGAAlppallREFKEKFGIDL---VQGY---GMTET-SP 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 246 GVAFECQEQNGMHFWE-------DCYLVE--IIDPEtGEPVP--EGEIGELVLttldRE--MMP-----------LIR-- 299
Cdd:PRK06187 321 VVSVLPPEDQLPGQWTkrrsagrPLPGVEarIVDDD-GDELPpdGGEVGEIIV----RGpwLMQgywnrpeataeTIDgg 395
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2796583109 300 -YRTRDLTRILP-GkcpcgrtHLRI-DRIKgrsdDMFIIKGVNIFPMQVEKILVQFP 353
Cdd:PRK06187 396 wLHTGDVGYIDEdG-------YLYItDRIK----DVIISGGENIYPRELEDALYGHP 441
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
92-353 |
3.72e-09 |
|
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: 58.30 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 92 SSSGTTGNPTVIVHSQHDLDSWanlVARCLYMVGIRKTDVFQNSS----GYGMF---TGGLGfqygaerLGCLTVPAAAG 164
Cdd:cd05973 95 FTSGTTGLPKGVPVPLRALAAF---GAYLRDAVDLRPEDSFWNAAdpgwAYGLYyaiTGPLA-------LGHPTILLEGG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 165 NSKRQI-KFISDFKTTALHAIPSyAIRLAEVFQEEGIDPRETTLKTLVIGAEPHTDEQRRKIERMLNVKAYNSFGMTEM- 242
Cdd:cd05973 165 FSVESTwRVIERLGVTNLAGSPT-AYRLLMAAGAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELg 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 243 ----NGPGVAFECQeQNGMHFWEDCYLVEIIDPETGEPVPeGEIGELvltTLDREMMPLIRYRTRDLtriLPGKCPCGRT 318
Cdd:cd05973 244 mvlaNHHALEHPVH-AGSAGRAMPGWRVAVLDDDGDELGP-GEPGRL---AIDIANSPLMWFRGYQL---PDTPAIDGGY 315
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2796583109 319 HLRIDRIK----------GRSDDMFIIKGVNIFPMQVEKILVQFP 353
Cdd:cd05973 316 YLTGDTVEfdpdgsfsfiGRADDVITMSGYRIGPFDVESALIEHP 360
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
85-353 |
6.30e-09 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 57.86 E-value: 6.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 85 RDGVRIHSSSGTTGNPTVIVHSQHDLDSWANLVARclYMVGIRKTDVFQNSSGYGMFTGGLGFQYGAERLGCLTV--PAA 162
Cdd:cd05928 174 QEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGR--YWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQGACVFvhHLP 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 163 AGNSKRQIKFISDFKTTALHAIPSyAIRLaeVFQEEGIDPRETTLKTLVIGAEPHTDEQRRKIERMLNVKAYNSFGMTEm 242
Cdd:cd05928 252 RFDPLVILKTLSSYPITTFCGAPT-VYRM--LVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTE- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 243 ngpgVAFECQEQNGMHF-------WEDCYLVEIIDpETGEPVPEGEIGELVLTTLDREMMPLIRYRTRDLTRIlpGKCPC 315
Cdd:cd05928 328 ----TGLICANFKGMKIkpgsmgkASPPYDVQIID-DNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKT--AATIR 400
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2796583109 316 GRTHLRIDRIK----------GRSDDMFIIKGVNIFPMQVEKILVQFP 353
Cdd:cd05928 401 GDFYLTGDRGImdedgyfwfmGRADDVINSSGYRIGPFEVESALIEHP 448
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
86-353 |
9.10e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 57.48 E-value: 9.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 86 DGVRIHSSSGTTGNPTVIVHSQHDLDSWANLVARCLymvGIRKTDVFQNS----SGYGMFTGGLG-FQYGAerlgCLTVP 160
Cdd:PRK12583 202 DPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESL---GLTEHDRLCVPvplyHCFGMVLANLGcMTVGA----CLVYP 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 161 AAAGNSKRQIKFISDFKTTALHAIPSYAIrlAEVFQEEGIDPRETTLKTLVIGAEPHTDE-QRRKIERMLNVKAYNSFGM 239
Cdd:PRK12583 275 NEAFDPLATLQAVEEERCTALYGVPTMFI--AELDHPQRGNFDLSSLRTGIMAGAPCPIEvMRRVMDEMHMAEVQIAYGM 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 240 TEMNgPgVAFECQEQNGM------------HFwedcyLVEIIDPEtGEPVPEGEIGELVLttldREMMPLIRYRTRDltr 307
Cdd:PRK12583 353 TETS-P-VSLQTTAADDLerrvetvgrtqpHL-----EVKVVDPD-GATVPRGEIGELCT----RGYSVMKGYWNNP--- 417
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796583109 308 ilpgkcpcGRTHLRID-------------------RIKGRSDDMFIIKGVNIFPMQVEKILVQFP 353
Cdd:PRK12583 418 --------EATAESIDedgwmhtgdlatmdeqgyvRIVGRSKDMIIRGGENIYPREIEEFLFTHP 474
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
93-353 |
1.04e-08 |
|
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: 57.01 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 93 SSGTTGNPTVIVHSQHDLdsWANLVARCLYMvGIRKTDVFQNSSGYGMFTgglGFQYGAER---LGCLTVPAAAGNSKRQ 169
Cdd:cd05903 101 TSGTTGEPKGVMHSHNTL--SASIRQYAERL-GLGPGDVFLVASPMAHQT---GFVYGFTLpllLGAPVVLQDIWDPDKA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 170 IKFISDFKTTALHAIPSYAIRLAEVfqEEGIDPRETTLKTLVIGAEPHTDEQRRKIERMLNVKAYNSFGMTEMngPGVAF 249
Cdd:cd05903 175 LALMREHGVTFMMGATPFLTDLLNA--VEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTEC--PGAVT 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 250 ECQEQNGMHFW-EDCYL---VEI-IDPETGEPVPEGEIGEL-------VLTTLDREMM-----PLIRYRTRDLTRILPGK 312
Cdd:cd05903 251 SITPAPEDRRLyTDGRPlpgVEIkVVDDTGATLAPGVEGELlsrgpsvFLGYLDRPDLtadaaPEGWFRTGDLARLDEDG 330
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2796583109 313 cpcgrtHLridRIKGRSDDMFIIKGVNIFPMQVEKILVQFP 353
Cdd:cd05903 331 ------YL---RITGRSKDIIIRGGENIPVLEVEDLLLGHP 362
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
93-355 |
1.42e-08 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 56.60 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 93 SSGTTGNPTVIVHSQHDLdsWANLVArCLYMVGIRKTDVFQNSSGYGMFTGglgFQYGAE---RLGCLTVPAAAGNSKRQ 169
Cdd:PRK13295 205 TSGTTGEPKGVMHTANTL--MANIVP-YAERLGLGADDVILMASPMAHQTG---FMYGLMmpvMLGATAVLQDIWDPARA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 170 IKFISDFKTTALHAIPSYAIRLAEVFQEEGIDprETTLKT-LVIGAE--PHTDEQRRKIermLNVKAYNSFGMTEmNG-- 244
Cdd:PRK13295 279 AELIRTEGVTFTMASTPFLTDLTRAVKESGRP--VSSLRTfLCAGAPipGALVERARAA---LGAKIVSAWGMTE-NGav 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 245 ----PGVAFE-CQEQNGmhfwedCYL----VEIIDPEtGEPVPEGEIGELVLTT-------LDREMMPLIR----YRTRD 304
Cdd:PRK13295 353 tltkLDDPDErASTTDG------CPLpgveVRVVDAD-GAPLPAGQIGRLQVRGcsnfggyLKRPQLNGTDadgwFDTGD 425
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2796583109 305 LTRILPGKCPcgrthlridRIKGRSDDMFIIKGVNIFPMQVEKILVQFPEL 355
Cdd:PRK13295 426 LARIDADGYI---------RISGRSKDVIIRGGENIPVVEIEALLYRHPAI 467
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
266-424 |
2.86e-08 |
|
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: 55.71 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 266 VEIIDPETGEPVPEGEIGELVLT------------TLDREMMPLIR-------YRTRDLTRILPGkcpcgrtHLRIdriK 326
Cdd:cd05931 366 VRIVDPETGRELPDGEVGEIWVRgpsvasgywgrpEATAETFGALAatdeggwLRTGDLGFLHDG-------ELYI---T 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 327 GRSDDMFIIKGVNIFPMQVEKILVQF-PELGSNYLITLeTVNNQDEMIVEVELSDLSTDNYIELEKIRRDIIRQLKDEIL 405
Cdd:cd05931 436 GRLKDLIIVRGRNHYPQDIEATAEEAhPALRPGCVAAF-SVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHG 514
|
170 180
....*....|....*....|.
gi 2796583109 406 VTP-KVKLVKKGSLPQ-SEGK 424
Cdd:cd05931 515 VAPaDVVLVRPGSIPRtSSGK 535
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
93-353 |
8.66e-08 |
|
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: 54.00 E-value: 8.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 93 SSGTTGNPTVIVHSQHDLDSWANLVARCLymVGIRKTDVFQNSS----GYGMfTGGLGF--QYGAErlgCLTVPAAAgNS 166
Cdd:cd05919 99 SSGTTGPPKGVMHAHRDPLLFADAMAREA--LGLTPGDRVFSSAkmffGYGL-GNSLWFplAVGAS---AVLNPGWP-TA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 167 KRQIKFISDFKTTALHAIPS-YAIRLAEVFQEEGIDpreTTLKTLVIGAEPHTDEQRRKIERMLNVKAYNSFGMTEMngp 245
Cdd:cd05919 172 ERVLATLARFRPTVLYGVPTfYANLLDSCAGSPDAL---RSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEV--- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 246 GVAFECqeqNGMHFWE--------DCYLVEIIDPEtGEPVPEGEIGELVLTtldremMPLIR------------------ 299
Cdd:cd05919 246 GHIFLS---NRPGAWRlgstgrpvPGYEIRLVDEE-GHTIPPGEEGDLLVR------GPSAAvgywnnpeksratfnggw 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2796583109 300 YRTRDLTRILPGKCpcgRTHlridriKGRSDDMFIIKGVNIFPMQVEKILVQFP 353
Cdd:cd05919 316 YRTGDKFCRDADGW---YTH------AGRADDMLKVGGQWVSPVEVESLIIQHP 360
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
93-402 |
2.61e-07 |
|
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: 52.76 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 93 SSGTTGNPTVIVHSQHDLDSWANLVARCLymvGIRKTD-VFQNSSgygmftggLGFQYGAERL-------GCLTVPA--A 162
Cdd:cd17649 102 TSGSTGTPKGVAVSHGPLAAHCQATAERY---GLTPGDrELQFAS--------FNFDGAHEQLlpplicgACVVLRPdeL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 163 AGNSKRQIKFISDFKTTALHAIPSYAIRLAEVFQEEGiDPRETTLKTLVIGAEPHTDEQRRKIeRMLNVKAYNSFGMTEM 242
Cdd:cd17649 171 WASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTG-DGRPPSLRLYIFGGEALSPELLRRW-LKAPVRLFNAYGPTEA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 243 NGPGVAFECQEQNGmHFWEDC--------YLVEIIDPETGePVPEGEIGELVL--------------TTLDR-----EMM 295
Cdd:cd17649 249 TVTPLVWKCEAGAA-RAGASMpigrplggRSAYILDADLN-PVPVGVTGELYIggeglargylgrpeLTAERfvpdpFGA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 296 PLIR-YRTRDLTRilpgkcpcGRTHLRIDRIkGRSDDMFIIKGVNIFPMQVEKILVQFPELGSNyLITLETVNNQDEMIV 374
Cdd:cd17649 327 PGSRlYRTGDLAR--------WRDDGVIEYL-GRVDHQVKIRGFRIELGEIEAALLEHPGVREA-AVVALDGAGGKQLVA 396
|
330 340
....*....|....*....|....*...
gi 2796583109 375 EVELSDLSTDNyIELEKIRRDIIRQLKD 402
Cdd:cd17649 397 YVVLRAAAAQP-ELRAQLRTALRASLPD 423
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
84-353 |
3.58e-07 |
|
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: 52.12 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 84 KRDGVRIHSSSGTTGNPTVIVHSQHDLDSWAnLVARclYMVGIRKTDVFQNSSGYGMFTGGLGFQYGAERLGCLTVPAAA 163
Cdd:cd05969 88 PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYY-FTGK--YVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 164 G-NSKRQIKFISDFKTTALHAIPSyAIRLaevFQEEGIDP----RETTLKTLVIGAEPHTDEQRRKIERMLNVKAYNSFG 238
Cdd:cd05969 165 RfDAESWYGIIERVKVTVWYTAPT-AIRM---LMKEGDELarkyDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWW 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 239 MTEMNGPGVA-FECQEQNGMHFWEDCYLVE--IIDpETGEPVPEGEIGELVLTTLDREMMPLIR--------------YR 301
Cdd:cd05969 241 QTETGSIMIAnYPCMPIKPGSMGKPLPGVKaaVVD-ENGNELPPGTKGILALKPGWPSMFRGIWndeeryknsfidgwYL 319
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2796583109 302 TRDLTRILPGKCPCgrthlridrIKGRSDDMFIIKGVNIFPMQVEKILVQFP 353
Cdd:cd05969 320 TGDLAYRDEDGYFW---------FVGRADDIIKTSGHRVGPFEVESALMEHP 362
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
94-287 |
4.74e-07 |
|
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: 51.77 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 94 SGTTGNP--TVIVHSqhdldswaNLVARCL---YMVGIRKTD-VFQNSSgYG-------MFTGglgFQYGaerlGCLTVP 160
Cdd:cd05918 115 SGSTGKPkgVVIEHR--------ALSTSALahgRALGLTSESrVLQFAS-YTfdvsileIFTT---LAAG----GCLCIP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 161 aaagnSKRQI-----KFISDFKTTALHAIPSYAiRLaevfqeegIDPRE-TTLKTLVIGAEPHTDEQRRK-IERmlnVKA 233
Cdd:cd05918 179 -----SEEDRlndlaGFINRLRVTWAFLTPSVA-RL--------LDPEDvPSLRTLVLGGEALTQSDVDTwADR---VRL 241
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796583109 234 YNSFGMTE------MNGPGVAFECQ---EQNGMHFWedcylveIIDPET-GEPVPEGEIGELVL 287
Cdd:cd05918 242 INAYGPAEctiaatVSPVVPSTDPRnigRPLGATCW-------VVDPDNhDRLVPIGAVGELLI 298
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
93-285 |
1.55e-06 |
|
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: 50.31 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 93 SSGTTGNP--TVIVHsqhdldswANLVArclyMVGIRKTDVFQNSSGYGMFTGGL---------GFQYGAERLGCLTVPA 161
Cdd:cd05904 166 SSGTTGRSkgVMLTH--------RNLIA----MVAQFVAGEGSNSDSEDVFLCVLpmfhiyglsSFALGLLRLGATVVVM 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 162 AAGNSKRQIKFISDFKTTALHAIPSyaIRLAEVFQEEGIDPRETTLKTLVIGAEPHTDE-QRRKIERMLNVKAYNSFGMT 240
Cdd:cd05904 234 PRFDLEELLAAIERYKVTHLPVVPP--IVLALVKSPIVDKYDLSSLRQIMSGAAPLGKElIEAFRAKFPNVDLGQGYGMT 311
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2796583109 241 EMNGPGVAFECQEQNGMHF---------WEdcylVEIIDPETGEPVPEGEIGEL 285
Cdd:cd05904 312 ESTGVVAMCFAPEKDRAKYgsvgrlvpnVE----AKIVDPETGESLPPNQTGEL 361
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
94-354 |
2.62e-06 |
|
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: 48.87 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 94 SGTTGNPTVIVHSQHDL----------------DSWanLVARCLYMVGirktdvfqnssGYGMFTGGLgfqYGAERLGCL 157
Cdd:cd17630 9 SGSTGTPKAVVHTAANLlasaaglhsrlgfgggDSW--LLSLPLYHVG-----------GLAILVRSL---LAGAELVLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 158 TVPAAAGNSkrqikfISDFKTTALHAIPSyaiRLAEVFQEEGIDPRETTLKTLVIGAEP-HTDEQRRKIERMLNVkaYNS 236
Cdd:cd17630 73 ERNQALAED------LAPPGVTHVSLVPT---QLQRLLDSGQGPAALKSLRAVLLGGAPiPPELLERAADRGIPL--YTT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 237 FGMTEMnGPGVAfecqeqngmhfweDCYLVEIIDPETGEPVP--------EGEI---GE-LVLTTLDREMMPLIR----Y 300
Cdd:cd17630 142 YGMTET-ASQVA-------------TKRPDGFGRGGVGVLLPgrelriveDGEIwvgGAsLAMGYLRGQLVPEFNedgwF 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2796583109 301 RTRDLTRILPGkcpcGRTHlridrIKGRSDDMFIIKGVNIFPMQVEKILVQFPE 354
Cdd:cd17630 208 TTKDLGELHAD----GRLT-----VLGRADNMIISGGENIQPEEIEAALAAHPA 252
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
94-357 |
3.43e-06 |
|
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: 49.17 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 94 SGTTGNPTVIVHSQHDLDSWANlVARCLYMVGirKTDVFQNSSGY----GMFTGGLGFQYGaerlGCLTV--PAAAGNSK 167
Cdd:cd05945 106 SGSTGRPKGVQISHDNLVSFTN-WMLSDFPLG--PGDVFLNQAPFsfdlSVMDLYPALASG----ATLVPvpRDATADPK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 168 RQIKFISDFKTTALHAIPSYAirlAEVFQEEGIDPRET-TLKTLVIGAEPHTDEQRRK-IERMLNVKAYNSFGMTEMNGP 245
Cdd:cd05945 179 QLFRFLAEHGITVWVSTPSFA---AMCLLSPTFTPESLpSLRHFLFCGEVLPHKTARAlQQRFPDARIYNTYGPTEATVA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 246 -------------------GVAFECQEqngmhfwedcylVEIIDpETGEPVPEGEIGELVLTT-------LDRE------ 293
Cdd:cd05945 256 vtyievtpevldgydrlpiGYAKPGAK------------LVILD-EDGRPVPPGEKGELVISGpsvskgyLNNPektaaa 322
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796583109 294 --MMPLIR-YRTRDLTRILPGkcpcGRTHLRidrikGRSDDMFIIKGVNIFPMQVEKILVQFPELGS 357
Cdd:cd05945 323 ffPDEGQRaYRTGDLVRLEAD----GLLFYR-----GRLDFQVKLNGYRIELEEIEAALRQVPGVKE 380
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
93-372 |
1.52e-05 |
|
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: 47.08 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 93 SSGTTGNPT-VIVHSQHdldsWANLVA--RCLYMVGIRKTDVFQNSS-GYGMFTGGLgfqygAERL--GCLTVPAAAG-- 164
Cdd:cd17650 101 TSGTTGKPKgVMVEHRN----VAHAAHawRREYELDSFPVRLLQMASfSFDVFAGDF-----ARSLlnGGTLVICPDEvk 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 165 -NSKRQIKFISDFKTTALHAIPSYAIRLAEVFQEEGIDPreTTLKTLVIGAEPHT-----DEQRRKIERMLNVkayNSFG 238
Cdd:cd17650 172 lDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDL--SAMRLLIVGSDGCKaqdfkTLAARFGQGMRII---NSYG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 239 MTEMNGPGVAFEcqeqNGMHFWEDCYLVEIIDP----------ETGEPVPEGEIGELV---------------LTT---L 290
Cdd:cd17650 247 VTEATIDSTYYE----EGRDPLGDSANVPIGRPlpntamyvldERLQPQPVGVAGELYiggagvargylnrpeLTAerfV 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 291 DREMMPLIR-YRTRDLTRILP-GKCPCgrthlridriKGRSDDMFIIKGVNIFPMQVEKILVQFPELGSNYLITLETVNN 368
Cdd:cd17650 323 ENPFAPGERmYRTGDLARWRAdGNVEL----------LGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGG 392
|
....
gi 2796583109 369 QDEM 372
Cdd:cd17650 393 EARL 396
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
78-287 |
2.66e-05 |
|
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: 46.32 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 78 LVAGDMKRDGVRIHSSSGTTGNPTVIVHSQHDLdsWANLVA-RCLYMVgirktdvfqnsSGYGMFTGGLGFQYGAERLGC 156
Cdd:cd05935 77 AVVGSELDDLALIPYTSGTTGLPKGCMHTHFSA--AANALQsAVWTGL-----------TPSDVILACLPLFHVTGFVGS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 157 LTVPAAAGNS---------KRQIKFISDFKTTALHAIPSYAIrlaEVFQEEGIDPRE-TTLKTLVIGAEPHTDEQRRKIE 226
Cdd:cd05935 144 LNTAVYVGGTyvlmarwdrETALELIEKYKVTFWTNIPTMLV---DLLATPEFKTRDlSSLKVLTGGGAPMPPAVAEKLL 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796583109 227 RMLNVKAYNSFGMTE------MNGPGvAFECQEQNGMHFWEDcylVEIIDPETGEPVPEGEIGELVL 287
Cdd:cd05935 221 KLTGLRFVEGYGLTEtmsqthTNPPL-RPKLQCLGIP*FGVD---ARVIDIETGRELPPNEVGEIVV 283
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
93-288 |
4.92e-05 |
|
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: 45.40 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 93 SSGTTGNPTVIVHSQHDLdsWANlVARCLYMVGIRKTDVFQNS----SGYGmFTGGLGF--QYGAErlgcLTVPAAAGNS 166
Cdd:cd05909 155 TSGSEGLPKGVVLSHKNL--LAN-VEQITAIFDPNPEDVVFGAlpffHSFG-LTGCLWLplLSGIK----VVFHPNPLDY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 167 KRQIKFISDFKTTALHAIP---SYAIRLAEVFQEEgidpretTLKTLVIGAEPHTDEQRRKIERMLNVKAYNSFGMTEMN 243
Cdd:cd05909 227 KKIPELIYDKKATILLGTPtflRGYARAAHPEDFS-------SLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECS 299
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2796583109 244 gPGVAFECQEqngMHFWEDCY-------LVEIIDPETGEPVPEGEIGELVLT 288
Cdd:cd05909 300 -PVISVNTPQ---SPNKEGTVgrplpgmEVKIVSVETHEEVPIGEGGLLLVR 347
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
86-355 |
5.99e-05 |
|
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: 45.26 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 86 DGVRIHSSSGTTGNPTVIVHSQHDLDSWANLVARCLYMVGirKTDVFQNSSGYGMFTGGLGFQYGAERLGCLTV------ 159
Cdd:cd17634 233 DPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYG--PGDIYWCTADVGWVTGHSYLLYGPLACGATTLlyegvp 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 160 --PAAAgnskRQIKFISDFKTTALHAIPSyAIRlaeVFQEEGIDPRE----TTLKTLVIGAEPHTDEQRRKIERMLNVK- 232
Cdd:cd17634 311 nwPTPA----RMWQVVDKHGVNILYTAPT-AIR---ALMAAGDDAIEgtdrSSLRILGSVGEPINPEAYEWYWKKIGKEk 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 233 --AYNSFGMTEMNG------PGVAFECQEQNGMHFWEdcYLVEIIDPEtGEPVPEGEIGELVLTTldrEMMPLIRYRTRD 304
Cdd:cd17634 383 cpVVDTWWQTETGGfmitplPGAIELKAGSATRPVFG--VQPAVVDNE-GHPQPGGTEGNLVITD---PWPGQTRTLFGD 456
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796583109 305 LTRILpgkcpcgRTHLR-------------IDR-----IKGRSDDMFIIKGVNIFPMQVEKILVQFPEL 355
Cdd:cd17634 457 HERFE-------QTYFStfkgmyfsgdgarRDEdgyywITGRSDDVINVAGHRLGTAEIESVLVAHPKV 518
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
86-353 |
6.30e-05 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 44.87 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 86 DGVRIHSSSGTTGNPTVIVHSQHdldSWANLVARCLYMVGIRKTDVFQNSSGYGmftgglgfqYGAERLGCLTVPAAAG- 164
Cdd:cd05974 86 DPMLLYFTSGTTSKPKLVEHTHR---SYPVGHLSTMYWIGLKPGDVHWNISSPG---------WAKHAWSCFFAPWNAGa 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 165 ----------NSKRQIKFISDFKTTALHAIPSyairLAEVFQEEGIDPRETTLKTLVIGAEPHTDEQRRKIERMLNVKAY 234
Cdd:cd05974 154 tvflfnyarfDAKRVLAALVRYGVTTLCAPPT----VWRMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 235 NSFGMTEM-----NGPGvafECQEQNGMHFWEDCYLVEIIDPETGePVPEGEIGeLVLTTLD---------------REM 294
Cdd:cd05974 230 DGYGQTETtalvgNSPG---QPVKAGSMGRPLPGYRVALLDPDGA-PATEGEVA-LDLGDTRpvglmkgyagdpdktAHA 304
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2796583109 295 MPLIRYRTRDLTRilpgkcpcgRTHLRIDRIKGRSDDMFIIKGVNIFPMQVEKILVQFP 353
Cdd:cd05974 305 MRGGYYRTGDIAM---------RDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHP 354
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
93-353 |
1.13e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 44.95 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 93 SSGTTGNP--TVIVHSqhdldswaNLVARCLYMvgirkTDVFQNSSGYGM-------FTGGLGFQYGAERLGCLTVPAAA 163
Cdd:PRK12316 663 TSGSTGKPkgAGNRHR--------ALSNRLCWM-----QQAYGLGVGDTVlqktpfsFDVSVWEFFWPLMSGARLVVAAP 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 164 G---NSKRQIKFISDFKTTALHAIPSyairLAEVFQEEGIDPRETTLKTLVIGAEP-HTDEQRRKIERMLNVKAYNSFGM 239
Cdd:PRK12316 730 GdhrDPAKLVELINREGVDTLHFVPS----MLQAFLQDEDVASCTSLRRIVCSGEAlPADAQEQVFAKLPQAGLYNLYGP 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 240 TEMNGPGVAFECQEQNGMHfwedcylVEIIDPETG----------EPVPEGEIGELVLTT-------LDREMM------- 295
Cdd:PRK12316 806 TEAAIDVTHWTCVEEGGDS-------VPIGRPIANlacyildanlEPVPVGVLGELYLAGrglargyHGRPGLtaerfvp 878
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2796583109 296 -PLI----RYRTRDLTRIlpgkcpcgRTHLRIDRIkGRSDDMFIIKGVNIFPMQVEKILVQFP 353
Cdd:PRK12316 879 sPFVagerMYRTGDLARY--------RADGVIEYA-GRIDHQVKLRGLRIELGEIEARLLEHP 932
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
266-353 |
3.63e-04 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 42.88 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 266 VEIIDPETGEPVPEGEIGELV-------------------------------LTTLDREmmpliryrtrdltrilpGKCp 314
Cdd:PRK08315 382 VKIVDPETGETVPRGEQGELCtrgysvmkgywndpektaeaidadgwmhtgdLAVMDEE-----------------GYV- 443
|
90 100 110
....*....|....*....|....*....|....*....
gi 2796583109 315 cgrthlridRIKGRSDDMFIIKGVNIFPMQVEKILVQFP 353
Cdd:PRK08315 444 ---------NIVGRIKDMIIRGGENIYPREIEEFLYTHP 473
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
93-384 |
1.23e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 41.48 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 93 SSGTTGNPTVIVHSQHDLDSWANLVARCLYMVGIRKTDVFQNSSgygmFTGGLGFQYGAERLGCLTVPAAAGNSKRQIKF 172
Cdd:PRK12316 3204 TSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFS----FDVFVEELFWPLMSGARVVLAGPEDWRDPALL 3279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 173 ISDFKTTALHAIPSYAIRLAEVFQEEGIDpRETTLKTLVIGAEPHTDEQRRKIERMLNVkaYNSFGMTEMNGPGVAFECQ 252
Cdd:PRK12316 3280 VELINSEGVDVLHAYPSMLQAFLEEEDAH-RCTSLKRIVCGGEALPADLQQQVFAGLPL--YNLYGPTEATITVTHWQCV 3356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 253 EQNGMHFW-------EDCYLVEIidpeTGEPVPEGEIGELVL--------------TTLDREM----MPLIR-YRTRDLT 306
Cdd:PRK12316 3357 EEGKDAVPigrpianRACYILDG----SLEPVPVGALGELYLggeglargyhnrpgLTAERFVpdpfVPGERlYRTGDLA 3432
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796583109 307 RIlpgkcpcgRTHLRIDRIkGRSDDMFIIKGVNIFPMQVEKILVQFPELGSNYLITLetvnNQDEMIVEVELSDLSTD 384
Cdd:PRK12316 3433 RY--------RADGVIEYI-GRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAV----DGRQLVAYVVPEDEAGD 3497
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
325-355 |
1.53e-03 |
|
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: 40.47 E-value: 1.53e-03
10 20 30
....*....|....*....|....*....|.
gi 2796583109 325 IKGRSDDMFIIKGVNIFPMQVEKILVQFPEL 355
Cdd:cd17633 226 LVGRESDMIIIGGINIFPTEIESVLKAIPGI 256
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
266-353 |
3.36e-03 |
|
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: 39.61 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 266 VEIIDpETGEPVPEGEIGELVLTT-------LDREMM------------PLIRYRTRDLTRILP-GkcpcgrthlRIDRI 325
Cdd:cd12115 279 AYVLD-RALQPVPLGVPGELYIGGagvargyLGRPGLtaerflpdpfgpGARLYRTGDLVRWRPdG---------LLEFL 348
|
90 100
....*....|....*....|....*...
gi 2796583109 326 kGRSDDMFIIKGVNIFPMQVEKILVQFP 353
Cdd:cd12115 349 -GRADNQVKVRGFRIELGEIEAALRSIP 375
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
325-355 |
5.00e-03 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 38.97 E-value: 5.00e-03
10 20 30
....*....|....*....|....*....|.
gi 2796583109 325 IKGRSDDMFIIKGVNIFPMQVEKILVQFPEL 355
Cdd:PRK13382 434 VVGRDDEMIVSGGENVYPIEVEKTLATHPDV 464
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
325-354 |
7.03e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 38.61 E-value: 7.03e-03
10 20 30
....*....|....*....|....*....|
gi 2796583109 325 IKGRSDDMFIIKGVNIFPMQVEKILVQFPE 354
Cdd:PRK07638 379 IVGREKNMILFGGINIFPEEIESVLHEHPA 408
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
268-286 |
8.01e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 38.40 E-value: 8.01e-03
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
325-356 |
8.09e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 38.48 E-value: 8.09e-03
10 20 30
....*....|....*....|....*....|..
gi 2796583109 325 IKGRSDDMFIIKGVNIFPMQVEKILVQFPELG 356
Cdd:PRK07470 412 ITGRASDMYISGGSNVYPREIEEKLLTHPAVS 443
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
90-287 |
8.10e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 38.57 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 90 IHSSSGTTGNPTVIVHSQHdldswANLVARCLYMVGIRKTD----VFQNSS-GYGMFTGGLgfqYGAERLGCLTVPAAAG 164
Cdd:PTZ00237 259 ILYTSGTTGNSKAVVRSNG-----PHLVGLKYYWRSIIEKDiptvVFSHSSiGWVSFHGFL---YGSLSLGNTFVMFEGG 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796583109 165 NSKrQIKFISDF-KTTALHAIpSYAIRLAEVFQEE-GIDPRET---------TLKTLVIGAEPHTDEQRRKIERMLNVKA 233
Cdd:PTZ00237 331 IIK-NKHIEDDLwNTIEKHKV-THTLTLPKTIRYLiKTDPEATiirskydlsNLKEIWCGGEVIEESIPEYIENKLKIKS 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2796583109 234 YNSFGMTEMnGPGVAFECQEQNGMH---FWEDCYLVEIIDPETGEPVPEGEIGELVL 287
Cdd:PTZ00237 409 SRGYGQTEI-GITYLYCYGHINIPYnatGVPSIFIKPSILSEDGKELNVNEIGEVAF 464
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
324-353 |
8.86e-03 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 38.31 E-value: 8.86e-03
10 20 30
....*....|....*....|....*....|
gi 2796583109 324 RIKGRSDDMFIIKGVNIFPMQVEKILVQFP 353
Cdd:PRK09029 348 TILGRLDNLFFSGGEGIQPEEIERVINQHP 377
|
|
| |
