|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
6-317 |
0e+00 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 624.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 6 KHDIPANIADRCLISPEQYQEKYQQSVSSPDAFWGEQGHILDWIKPYqkvkNTSFAPGNVSIKWYEDGTLNLAANCLDRH 85
Cdd:PRK00174 1 VFPPPAEFAANALIDMEQYKALYQESVEDPEGFWAEQAKRLDWFKPF----DTVLDWNAPFIKWFEDGELNVSYNCLDRH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 86 LAERGNETAIIWEGDDASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGG 165
Cdd:PRK00174 77 LKTRGDKVAIIWEGDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 166 FSPEAVAGRIVDSNSKLVITADEGVRAGRGIPLKKNVDEALKNPNvkSINNVIVLKRTGGKIDWHEGRDLWWSDLIENAS 245
Cdd:PRK00174 157 FSAEALADRIIDAGAKLVITADEGVRGGKPIPLKANVDEALANCP--SVEKVIVVRRTGGDVDWVEGRDLWWHELVAGAS 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 823296640 246 DQHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLL 317
Cdd:PRK00174 235 DECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVGWVTGHSYIV 306
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
18-317 |
0e+00 |
|
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: 553.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 18 LISPEQYQEKYQQSVSSPDAFWGEQGH-ILDWIKPYQKVKNTSFAPgnvSIKWYEDGTLNLAANCLDRHLAERGNETAII 96
Cdd:TIGR02188 1 IANLEQYKELYEESIEDPDKFWAKLAReLLDWFKPFTKVLDWSFPP---FYKWFVGGELNVSYNCVDRHLEARPDKVAII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 97 WEGDDASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIV 176
Cdd:TIGR02188 78 WEGDEPGEVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALADRIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 177 DSNSKLVITADEGVRAGRGIPLKKNVDEALKNPNVkSINNVIVLKRTGGKID-WHEGRDLWWSDLIENASDQHQPEEMNA 255
Cdd:TIGR02188 158 DAGAKLVITADEGLRGGKVIPLKAIVDEALEKCPV-SVEHVLVVRRTGNPVVpWVEGRDVWWHDLMAKASAYCEPEPMDS 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 823296640 256 EDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLL 317
Cdd:TIGR02188 237 EDPLFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGHSYIV 298
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
22-317 |
0e+00 |
|
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: 547.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 22 EQYQEKYQQSVSSPDAFWGEQGHILDWIKPYQKVKNTSFapGNVSIKWYEDGTLNLAANCLDRHLAERGNETAIIWEGDD 101
Cdd:cd05966 1 EQYKELYKQSIEDPEEFWGEIAKELDWFKPWDKVLDWSK--GPPFIKWFEGGKLNISYNCLDRHLKERGDKVAIIWEGDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 102 ASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSK 181
Cdd:cd05966 79 PDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 182 LVITADEGVRAGRGIPLKKNVDEALKnpNVKSINNVIVLKRTGGKIDWHEGRDLWWSDLIENASDQHQPEEMNAEDPLFI 261
Cdd:cd05966 159 LVITADGGYRGGKVIPLKEIVDEALE--KCPSVEKVLVVKRTGGEVPMTEGRDLWWHDLMAKQSPECEPEWMDSEDPLFI 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 823296640 262 LYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLL 317
Cdd:cd05966 237 LYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIGWITGHSYIV 292
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
24-317 |
1.00e-180 |
|
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: 511.74 E-value: 1.00e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 24 YQEKYQQSVSSPDAFWGEQGHILDWIKPYQKVKNTSFAPGNVSIKWYEDGTLNLAANCLDRHLAERGNETAIIWEGDDAS 103
Cdd:cd17634 1 YETKYRQSINDPDTFWGEAGKILDWITPYQKVKNTSFAPGAPSIKWFEDATLNLAANALDRHLRENGDRTAIIYEGDDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 104 QSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLV 183
Cdd:cd17634 81 QSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 184 ITADEGVRAGRGIPLKKNVDEALkNPNVKSINNVIVLKRTGGKIDWHEGRDLWWSDLIENASDQHQPEEMNAEDPLFILY 263
Cdd:cd17634 161 ITADGGVRAGRSVPLKKNVDDAL-NPNVTSVEHVIVLKRTGSDIDWQEGRDLWWRDLIAKASPEHQPEAMNAEDPLFILY 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 823296640 264 TSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLL 317
Cdd:cd17634 240 TSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVTGHSYLL 293
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
68-317 |
3.77e-143 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 415.28 E-value: 3.77e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 68 KWYEDGTLNLAANCLDRHLAERGNETAIIWEGDDaSQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAV 147
Cdd:COG0365 1 RWFVGGRLNIAYNCLDRHAEGRGDKVALIWEGED-GEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 148 AMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITADEGVRAGRGIPLKKNVDEALKnpNVKSINNVIVLKRTGGKI 227
Cdd:COG0365 80 AMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLRGGKVIDLKEKVDEALE--ELPSLEHVIVVGRTGADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 228 DWHEgrDLWWSDLIENASDQHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADV 307
Cdd:COG0365 158 PMEG--DLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADI 235
|
250
....*....|
gi 823296640 308 GWVTGHSYLL 317
Cdd:COG0365 236 GWATGHSYIV 245
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
24-315 |
2.99e-115 |
|
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: 345.84 E-value: 2.99e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 24 YQEKYQQSVSSPDAFWGEQGHILDWIKPYQKVKNTSFAPgnvSIKWYEDGTLNLAANCLDRH-LAERGNETAIIWEGDDA 102
Cdd:cd05967 1 YEEVYARSIAEPEAFWAEQARLIDWFKPPEKILDNSNPP---FTRWFVGGRLNTCYNALDRHvEAGRGDQIALIYDSPVT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 103 SQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKL 182
Cdd:cd05967 78 GTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 183 VITADEGVRAGRGIPLKKNVDEALKNPNVKSiNNVIVLKRTGGKID-WHEGRDLWWSDLIENASdQHQPEEMNAEDPLFI 261
Cdd:cd05967 158 IVTASCGIEPGKVVPYKPLLDKALELSGHKP-HHVLVLNRPQVPADlTKPGRDLDWSELLAKAE-PVDCVPVAATDPLYI 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 823296640 262 LYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSY 315
Cdd:cd05967 236 LYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASDVGWVVGHSY 289
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
20-316 |
5.46e-115 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 346.50 E-value: 5.46e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 20 SPEQYQEKYQQSVSSPDAFWGEQGHILDWIKPY--QKV--KNTSFAPGNVSIKWYEDGTLNLAANCLDRHL-AERGNETA 94
Cdd:PLN02654 28 SPQQYMEMYKRSVDDPAGFWSDIASQFYWKQKWegDEVcsENLDVRKGPISIEWFKGGKTNICYNCLDRNVeAGNGDKIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 95 IIWEGDDASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGR 174
Cdd:PLN02654 108 IYWEGNEPGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 175 IVDSNSKLVITADEGVRAGRGIPLKKNVDEALKNPNVKSIN--------NVIVLKRTGGKidWHEGRDLWWSDLIENASD 246
Cdd:PLN02654 188 IVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNGVSvgicltyeNQLAMKREDTK--WQEGRDVWWQDVVPNYPT 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 247 QHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYL 316
Cdd:PLN02654 266 KCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYV 335
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
22-315 |
1.55e-114 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 344.24 E-value: 1.55e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 22 EQYQEKYQQSVSSPDAFWGEQGHILDWIKPYQKVKNTS---FApgnvsiKWYEDGTLNLAANCLDRHLAERGNETAIIWE 98
Cdd:PRK10524 2 MSYSEFYQRSIDDPEAFWAEQARRIDWQTPFTQVLDYSnppFA------RWFVGGRTNLCHNAVDRHLAKRPEQLALIAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 99 GDDASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDS 178
Cdd:PRK10524 76 STETDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGGFASHSLAARIDDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 179 NSKLVITADEGVRAGRGIPLKKNVDEALKNPNVKSiNNVIVLKRTGGKIDWHEGRDLWWSDLIENASDQHQPEE-MNAED 257
Cdd:PRK10524 156 KPVLIVSADAGSRGGKVVPYKPLLDEAIALAQHKP-RHVLLVDRGLAPMARVAGRDVDYATLRAQHLGARVPVEwLESNE 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 823296640 258 PLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSY 315
Cdd:PRK10524 235 PSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASDIGWVVGHSY 292
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
22-312 |
3.59e-82 |
|
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: 260.11 E-value: 3.59e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 22 EQYQEKYQQSVSSPDAFWGEQGHILD--WIKPYQKVKNTSfaPGNVSIKWYEDGTLNLAANCLDRHLAERGNETAIIWEG 99
Cdd:cd05968 7 PDLEAFLERSAEDNAWFWGEFVKDVGieWYEPPYQTLDLS--GGKPWAAWFVGGRMNIVEQLLDKWLADTRTRPALRWEG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 100 DDASqSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSN 179
Cdd:cd05968 85 EDGT-SRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 180 SKLVITADEGVRAGRGIPLKKNVDEALKnpNVKSINNVIVLKRTGGKIDWHEGRDLWWSDLIENASDqhQPEEMNAEDPL 259
Cdd:cd05968 164 AKALITADGFTRRGREVNLKEEADKACA--QCPTVEKVVVVRHLGNDFTPAKGRDLSYDEEKETAGD--GAERTESEDPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 823296640 260 FILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGD-IYWCTaDVGWVTG 312
Cdd:cd05968 240 MIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDlLTWFT-DLGWMMG 292
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
69-315 |
2.74e-65 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 215.14 E-value: 2.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 69 WYEDGTLNLAANCLDRHLA-ERGNETAIIWEGDDASQSkhISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAV 147
Cdd:PRK04319 36 WLETGKVNIAYEAIDRHADgGRKDKVALRYLDASRKEK--YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 148 AMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITADEGVRagrgiplKKNVDEAlknPNVKSInnVIV---LKRTG 224
Cdd:PRK04319 114 ALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLE-------RKPADDL---PSLKHV--LLVgedVEEGP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 225 GKIDWHEgrdlwwsdLIENASDQHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTfKYVFDYHPGDIYWCT 304
Cdd:PRK04319 182 GTLDFNA--------LMEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTG-KYVLDLHEDDVYWCT 252
|
250
....*....|.
gi 823296640 305 ADVGWVTGHSY 315
Cdd:PRK04319 253 ADPGWVTGTSY 263
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
82-317 |
1.66e-54 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 182.90 E-value: 1.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 82 LDRHLAERGNETAiiWEGDDasqSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:pfam00501 1 LERQAARTPDKTA--LEVGE---GRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 162 IFGGFSPEAVAGRIVDSNSKLVITADEgvragrgiPLKKNVDEALKNPNVKSInnVIVLKRTggkiDWHEGRDLWWSDLI 241
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDA--------LKLEELLEALGKLEVVKL--VLVLDRD----PVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 242 EnASDQHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTgGYLVYAATTFKYV----FDYHPGDIYWCTADVGWVTGHSYLL 317
Cdd:pfam00501 142 A-DVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH-RNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSLGL 219
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
13-309 |
1.90e-47 |
|
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: 168.60 E-value: 1.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 13 IADRCLISPEQYQEKYQQSVSSPDAFWGEqghILDWI-----KPYQKV-KNTSFAPGNvsiKWYEDGTLNLAANCLDRHl 86
Cdd:cd05943 8 VNARHGLSLADYAALHRWSVDDPGAFWAA---VWDFSgvrgsKPYDVVvVSGRIMPGA---RWFPGARLNYAENLLRHA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 87 aeRGNETAIIWEGDDASqSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGF 166
Cdd:cd05943 81 --DADDPAAIYAAEDGE-RTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 167 SPEAVAGRIVDSNSKLVITADEGVRAGRGIPLKKNVDEALKnpNVKSINNVIVLKRTG--GKIDW-HEGRDLWWSDLIEN 243
Cdd:cd05943 158 GVPGVLDRFGQIEPKVLFAVDAYTYNGKRHDVREKVAELVK--GLPSLLAVVVVPYTVaaGQPDLsKIAKALTLEDFLAT 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 823296640 244 ASD-QHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGW 309
Cdd:cd05943 236 GAAgELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKEHILHCDLRPGDRLFYYTTCGW 302
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
13-310 |
8.47e-45 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 161.50 E-value: 8.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 13 IADRCLISPEQYQEKYQQSVSSPDAFWGE-------QGHildwiKPYQKVKNTSFAPGNvsiKWYEDGTLNLAANCLdRH 85
Cdd:PRK03584 25 LAARRGLSFDDYAALWRWSVEDLEAFWQSvwdffgvIGS-----TPYTVVLAGRRMPGA---RWFPGARLNYAENLL-RH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 86 laERGNETAIIWEGDDASQSKhISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGG 165
Cdd:PRK03584 96 --RRDDRPAIIFRGEDGPRRE-LSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 166 FSPEAVAGRIVDSNSKLVITADeGVRAGrGiplkKNVDEALKNPNV----KSINNVIVLKRTGGKIDW-HEGRDLWWSDL 240
Cdd:PRK03584 173 FGVQGVLDRFGQIEPKVLIAVD-GYRYG-G----KAFDRRAKVAELraalPSLEHVVVVPYLGPAAAAaALPGALLWEDF 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 823296640 241 IENASDQH-QPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGD-IYWCTAdVGWV 310
Cdd:PRK03584 247 LAPAEAAElEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDrFFWYTT-CGWM 317
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
109-315 |
5.24e-40 |
|
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: 145.34 E-value: 5.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 109 SYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITADE 188
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 189 gvragrgiplkknvdealknpnvksinnvivLKrtggkidwhegrdlwwsdlienasdqhqpEEMNAEDPLFILYTSGST 268
Cdd:cd05969 82 -------------------------------LY-----------------------------ERTDPEDPTLLHYTSGTT 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 823296640 269 GKPKGVLHTTGGYLVYAATTfKYVFDYHPGDIYWCTADVGWVTGHSY 315
Cdd:cd05969 102 GTPKGVLHVHDAMIFYYFTG-KYVLDLHPDDIYWCTADPGWVTGTVY 147
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
18-316 |
2.54e-39 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 146.04 E-value: 2.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 18 LISPEQYQEKYQQSVSSPDAFWGEQG-HILDWIKPYQKVkntsFAPGNVSIKWYEDGTLNLAANCLDRHL--AERGNETA 94
Cdd:PTZ00237 4 LSDPFDYENDSNYANSNPESFWDEVAkKYVHWDKMYDKV----YSGDEIYPDWFKGGELNTCYNVLDIHVknPLKRDQDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 95 IIWEGDDASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGR 174
Cdd:PTZ00237 80 LIYECPYLKKTIKLTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 175 IVDSNSKLVITADEGVRAGRGIPLKKNVDEALKNPNVKSiNNVIVLKRTggkiDWHEGRD-------------LWWSDLI 241
Cdd:PTZ00237 160 IETITPKLIITTNYGILNDEIITFTPNLKEAIELSTFKP-SNVITLFRN----DITSESDlkkietiptipntLSWYDEI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 242 ENASDQHQ-------PEEMNaeDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHS 314
Cdd:PTZ00237 235 KKIKENNQspfyeyvPVESS--HPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHG 312
|
..
gi 823296640 315 YL 316
Cdd:PTZ00237 313 FL 314
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
22-313 |
1.73e-38 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 144.45 E-value: 1.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 22 EQYQEKYQQSVSSPDAFWG---EQGHILDWIKPYQKVKNTSFA-PGNvsiKWYEDGTLNLAANCLDRHLAERGNETAIIW 97
Cdd:PLN03052 120 SSFSEFQRFSVENPEVYWSivlDELSLVFSVPPRCILDTSDESnPGG---QWLPGAVLNVAECCLTPKPSKTDDSIAIIW 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 98 --EGDDASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRI 175
Cdd:PLN03052 197 rdEGSDDLPVNRMTLSELRSQVSRVANALDALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRL 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 176 VDSNSKLVITADEGVRAGRGIPLKKNVDEAlKNPnvksinNVIVLKRTGGKIDWH-EGRDLWWSDLIENASDQHQPEE-- 252
Cdd:PLN03052 277 KISKAKAIFTQDVIVRGGKSIPLYSRVVEA-KAP------KAIVLPADGKSVRVKlREGDMSWDDFLARANGLRRPDEyk 349
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 823296640 253 ---MNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVfDYHPGDIY-WCTaDVGWVTGH 313
Cdd:PLN03052 350 aveQPVEAFTNILFSSGTTGEPKAIPWTQLTPLRAAADAWAHL-DIRKGDIVcWPT-NLGWMMGP 412
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
109-315 |
6.23e-31 |
|
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: 120.52 E-value: 6.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 109 SYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITade 188
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 189 gvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdlienasdqhqpeemNAEDPLFILYTSGST 268
Cdd:cd05972 79 -----------------------------------------------------------------DAEDPALIYFTSGTT 93
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 823296640 269 GKPKGVLHTTgGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSY 315
Cdd:cd05972 94 GLPKGVLHTH-SYPLGHIPTAAYWLGLRPDDIHWNIADPGWAKGAWS 139
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
82-312 |
1.74e-30 |
|
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: 119.53 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 82 LDRHLAERGNETAIIWEGddasqsKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:COG0318 5 LRRAAARHPDRPALVFGG------RRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 162 IFGGFSPEAVAGRIVDSNSKLVITAdegvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdli 241
Cdd:COG0318 79 LNPRLTAEELAYILEDSGARALVTA------------------------------------------------------- 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 823296640 242 enasdqhqpeemnaedplFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTA----DVGWVTG 312
Cdd:COG0318 104 ------------------LILYTSGTTGRPKGVMLTHRN-LLANAAAIAAALGLTPGDVVLVALplfhVFGLTVG 159
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
82-301 |
6.17e-30 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 119.43 E-value: 6.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 82 LDRHLAERGNETAIIWEGDDASQSkhISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:COG1022 17 LRRRAARFPDRVALREKEDGIWQS--LTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 162 IFGGFSPEAVAGRIVDSNSKLVITADEGVragrgipLKKnVDEALKN-PNVKsinNVIVLKRTGGKIDwheGRDLWWSDL 240
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVEDQEQ-------LDK-LLEVRDElPSLR---HIVVLDPRGLRDD---PRLLSLDEL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 823296640 241 IENASDQHQPEEMNA-------EDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIY 301
Cdd:COG1022 161 LALGREVADPAELEArraavkpDDLATIIYTSGTTGRPKGVMLTHRN-LLSNARALLERLPLGPGDRT 227
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
72-277 |
1.41e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 109.12 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 72 DGTLNLAaNCLDRHLAERGNETAIIWEGddasqsKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLA 151
Cdd:PRK06187 3 DYPLTIG-RILRHGARKHPDKEAVYFDG------RRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 152 CARIGAI-HSV-IFggFSPEAVAGRIVDSNSKLVITADEGVragrgiPLKKNVDEALknPNVKSinnVIVL---KRTGGK 226
Cdd:PRK06187 76 VPKIGAVlHPInIR--LKPEEIAYILNDAEDRVVLVDSEFV------PLLAAILPQL--PTVRT---VIVEgdgPAAPLA 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 823296640 227 IDWHEgrdlwWSDLIENASDQHQPEEMNAEDPLFILYTSGSTGKPKGVLHT 277
Cdd:PRK06187 143 PEVGE-----YEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLS 188
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
108-315 |
2.43e-25 |
|
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: 104.91 E-value: 2.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 108 ISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITad 187
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 188 egvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdlieNASDQHQPeemnAEDPLFILYTSGS 267
Cdd:cd05973 79 -------------------------------------------------------DAANRHKL----DSDPFVMMFTSGT 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 823296640 268 TGKPKGVLHTTGGYLVYAAtTFKYVFDYHPGDIYWCTADVGWVTGHSY 315
Cdd:cd05973 100 TGLPKGVPVPLRALAAFGA-YLRDAVDLRPEDSFWNAADPGWAYGLYY 146
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
101-274 |
1.36e-24 |
|
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: 103.45 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 101 DASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNS 180
Cdd:cd05911 4 DADTGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 181 KLVITADEGVragrgiplkKNVDEALKnpNVKSINNVIVLkrtGGKIDWHEGR-DLWWSDLIENASDQHQPEEMNAEDPL 259
Cdd:cd05911 84 KVIFTDPDGL---------EKVKEAAK--ELGPKDKIIVL---DDKPDGVLSIeDLLSPTLGEEDEDLPPPLKDGKDDTA 149
|
170
....*....|....*
gi 823296640 260 FILYTSGSTGKPKGV 274
Cdd:cd05911 150 AILYSSGTTGLPKGV 164
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
76-310 |
1.90e-22 |
|
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: 97.54 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 76 NLAANCLD-----RHLAERGNETAIIWEGDDASQSKHiSYKELHRDVCRFANVLL-AQGIKKGDVVAIYMPMVPEAAVAM 149
Cdd:cd05928 6 NFASDVLDqwadkEKAGKRPPNPALWWVNGKGDEVKW-SFRELGSLSRKAANVLSgACGLQRGDRVAVILPRVPEWWLVN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 150 LACARIGAIhsVIFGGFSPEA--VAGRIVDSNSKLVITADEgvragrgipLKKNVDE-ALKNPNVKSinNVIVLkrtggk 226
Cdd:cd05928 85 VACIRTGLV--FIPGTIQLTAkdILYRLQASKAKCIVTSDE---------LAPEVDSvASECPSLKT--KLLVS------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 227 idwHEGRDLWWS--DLIENASDQHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCT 304
Cdd:cd05928 146 ---EKSRDGWLNfkELLNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNT 222
|
....*.
gi 823296640 305 ADVGWV 310
Cdd:cd05928 223 SDTGWI 228
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
93-277 |
4.48e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 96.16 E-value: 4.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 93 TAIIWEGddasqsKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVA 172
Cdd:PRK08316 28 TALVFGD------RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 173 GRIVDSNSKLVITADEgvragrgipLKKNVDEALKNPNVKSinnVIVLKRTGGkiDWHEGRDLWWSDLIENASDQHQPEE 252
Cdd:PRK08316 102 YILDHSGARAFLVDPA---------LAPTAEAALALLPVDT---LILSLVLGG--REAPGGWLDFADWAEAGSVAEPDVE 167
|
170 180
....*....|....*....|....*
gi 823296640 253 MNAEDPLFILYTSGSTGKPKGVLHT 277
Cdd:PRK08316 168 LADDDLAQILYTSGTESLPKGAMLT 192
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
104-299 |
7.40e-22 |
|
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: 95.62 E-value: 7.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 104 QSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLV 183
Cdd:TIGR03098 22 HDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 184 ITADEgvragrgiPLKKNVDEALKNPNVKSInnVIVLKRTGGKIDWHEGRDLWWSDLiENASDQHQPEEMNAEDPLFILY 263
Cdd:TIGR03098 102 VTSSE--------RLDLLHPALPGCHDLRTL--IIVGDPAHASEGHPGEEPASWPKL-LALGDADPPHPVIDSDMAAILY 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 823296640 264 TSGSTGKPKGVL--HTTggyLVYAATTFKYVFDYHPGD 299
Cdd:TIGR03098 171 TSGSTGRPKGVVlsHRN---LVAGAQSVATYLENRPDD 205
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
64-309 |
1.51e-21 |
|
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: 94.87 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 64 NVSIKWYEdgTLNLAANCLDRHLAERGNETAIIWeGDDASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVP 143
Cdd:cd05970 7 NFSINVPE--NFNFAYDVVDAMAKEYPDKLALVW-CDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 144 EAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITADEGvragrGIPlkKNVDEALknpnvKSINNVIVLKRT 223
Cdd:cd05970 84 EFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAED-----NIP--EEIEKAA-----PECPSKPKLVWV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 224 GGKIdwhegRDLW--WSDLIENASDQHQPEEMNA----EDPLFILYTSGSTGKPKGVLHTTG---GYLVyaatTFKYVFD 294
Cdd:cd05970 152 GDPV-----PEGWidFRKLIKNASPDFERPTANSypcgEDILLVYFSSGTTGMPKMVEHDFTyplGHIV----TAKYWQN 222
|
250
....*....|....*
gi 823296640 295 YHPGDIYWCTADVGW 309
Cdd:cd05970 223 VREGGLHLTVADTGW 237
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
105-312 |
1.63e-21 |
|
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: 94.04 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 105 SKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVI 184
Cdd:cd05971 4 PEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 185 TaDEgvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdlienasdqhqpeemnAEDPLFILYT 264
Cdd:cd05971 84 T-DG------------------------------------------------------------------SDDPALIIYT 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 823296640 265 SGSTGKPKGVLHTTgGYLVYAATTFKYVFDYHP--GDIYWCTADVGWVTG 312
Cdd:cd05971 97 SGTTGPPKGALHAH-RVLLGHLPGVQFPFNLFPrdGDLYWTPADWAWIGG 145
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
82-304 |
3.77e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 93.43 E-value: 3.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 82 LDRHLAERGNETAIIWEGDDasqskhISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:PRK07656 11 LARAARRFGDKEAYVFGDQR------LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 162 IFGGFSPEAVAGRIVDSNSKLVITADEGvragrgIPLKKNVDEALknPNVKSInnVIVlkrTGGKIDWHEGRDLWWSDLI 241
Cdd:PRK07656 85 LNTRYTADEAAYILARGDAKALFVLGLF------LGVDYSATTRL--PALEHV--VIC---ETEEDDPHTEKMKTFTDFL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823296640 242 ENASDQHQPEEMNAEDPLFILYTSGSTGKPKGVLhTTGGYLVYAATTFKYVFDYHPGDIYWCT 304
Cdd:PRK07656 152 AAGDPAERAPEVDPDDVADILFTSGTTGRPKGAM-LTHRQLLSNAADWAEYLGLTEGDRYLAA 213
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
78-277 |
7.81e-21 |
|
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: 92.43 E-value: 7.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 78 AANCLDRHLAE-RGNETAIIwegDDASqskHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIG 156
Cdd:cd05959 5 AATLVDLNLNEgRGDKTAFI---DDAG---SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 157 AIHSVIFGGFSPEAVAGRIVDSNSKLVITADEgvragrgipLKKNVDEALKnpnvKSINNVIVLKRTGGKIDwhEGRDLW 236
Cdd:cd05959 79 IVPVPVNTLLTPDDYAYYLEDSRARVVVVSGE---------LAPVLAAALT----KSEHTLVVLIVSGGAGP--EAGALL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 823296640 237 WSDLIENASDQHQPEEMNAEDPLFILYTSGSTGKPKGVLHT 277
Cdd:cd05959 144 LAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHL 184
|
|
| ACAS_N |
pfam16177 |
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many ... |
24-81 |
1.06e-20 |
|
Acetyl-coenzyme A synthetase N-terminus; This domain is found at the N-terminus of many acetyl-coenzyme A synthetase enzymes.
Pssm-ID: 465043 [Multi-domain] Cd Length: 55 Bit Score: 83.68 E-value: 1.06e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 823296640 24 YQEKYQQSVSSPDAFWGEQGHILDWIKPYQKVKNTSFAPGnvsIKWYEDGTLNLAANC 81
Cdd:pfam16177 1 YEALYRRSIEDPEGFWGEVAKELDWFKPFDKVLDGSNGPF---AKWFVGGKLNVCYNC 55
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
82-305 |
1.22e-20 |
|
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: 91.52 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 82 LDRHLAERGNETAIIWEGddasqsKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:cd17631 1 LRRRARRHPDRTALVFGG------RSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 162 IFGGFSPEAVAGRIVDSNSKLVItadegvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdli 241
Cdd:cd17631 75 LNFRLTPPEVAYILADSGAKVLF--------------------------------------------------------- 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823296640 242 enasdqhqpeemnaEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTA 305
Cdd:cd17631 98 --------------DDLALLMYTSGTTGRPKGAMLTHRN-LLWNAVNALAALDLGPDDVLLVVA 146
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
82-272 |
1.96e-20 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 91.47 E-value: 1.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 82 LDRHLAERGNETAIIWEGddasqsKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:PRK08279 43 FEEAAARHPDRPALLFED------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 162 IFGGFSPEAVAGRIVDSNSKLVITADEgvragrgipLKKNVDEALKNPNVksinnvivlkrtGGKIDWHEGRDLWWSDLI 241
Cdd:PRK08279 117 LNTQQRGAVLAHSLNLVDAKHLIVGEE---------LVEAFEEARADLAR------------PPRLWVAGGDTLDDPEGY 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 823296640 242 EN------ASDQHQPEE---MNAEDPLFILYTSGSTGKPK 272
Cdd:PRK08279 176 EDlaaaaaGAPTTNPASrsgVTAKDTAFYIYTSGTTGLPK 215
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
75-304 |
2.31e-20 |
|
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: 91.14 E-value: 2.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 75 LNLAANCLDRHLAERGNeTAIIwegdDASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACAR 154
Cdd:cd05904 5 LPLDSVSFLFASAHPSR-PALI----DAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 155 IGAIHSVIFGGFSPEAVAGRIVDSNSKLVITADEGVragrgiplkknvdealknPNVKSINNVIVLKRtggkiDWHEGRD 234
Cdd:cd05904 80 LGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELA------------------EKLASLALPVVLLD-----SAEFDSL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 823296640 235 LWWSDLIENASDQHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFD--YHPGDIYWCT 304
Cdd:cd05904 137 SFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRN-LIAMVAQFVAGEGsnSDSEDVFLCV 207
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
109-277 |
1.55e-19 |
|
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: 88.09 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 109 SYKELHRDVCRFANVLLAQ-GIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITAD 187
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 188 EGVRAGRGIPLKknvdealknpnvksinnVIVLkrtggkidwhegRDLWWSDLIENASDQHQPEEMNAEDPLFILYTSGS 267
Cdd:TIGR01733 81 ALASRLAGLVLP-----------------VILL------------DPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGS 131
|
170
....*....|
gi 823296640 268 TGKPKGVLHT 277
Cdd:TIGR01733 132 TGRPKGVVVT 141
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
82-277 |
1.87e-19 |
|
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: 88.39 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 82 LDRHLAERGNETAIIWEGddasqsKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAI--- 158
Cdd:cd05936 5 LEEAARRFPDKTALIFMG------RKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVvvp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 159 HSVIFGgfsPEAVAGRIVDSNSKLVITadegvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrDLWWS 238
Cdd:cd05936 79 LNPLYT---PRELEHILNDSGAKALIV------------------------------------------------AVSFT 107
|
170 180 190
....*....|....*....|....*....|....*....
gi 823296640 239 DLIENASDQHQPEEMNAEDPLFILYTSGSTGKPKGVLHT 277
Cdd:cd05936 108 DLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLT 146
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
108-277 |
5.02e-19 |
|
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: 87.37 E-value: 5.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 108 ISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITAD 187
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 188 EGvrAGRGIPLKKNVDEALKNPNVksinnvivlkRTGGKIDWHEGRDLwwSDLIENASDQHQPEEMNAEDPLFILYTSGS 267
Cdd:cd05926 95 GE--LGPASRAASKLGLAILELAL----------DVGVLIRAPSAESL--SNLLADKKNAKSEGVPLPDDLALILHTSGT 160
|
170
....*....|
gi 823296640 268 TGKPKGVLHT 277
Cdd:cd05926 161 TGRPKGVPLT 170
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
82-275 |
9.03e-19 |
|
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: 87.22 E-value: 9.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 82 LDRHLAERGNETAIIWEGDdasqskHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGA---- 157
Cdd:COG1020 482 FEAQAARTPDAVAVVFGDQ------SLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAayvp 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 158 IhsvifggfSPEAVAGRIV----DSNSKLVITADEgvragrgiplkknVDEALKNPNVKSINnvivlkrtggkIDwhegr 233
Cdd:COG1020 556 L--------DPAYPAERLAymleDAGARLVLTQSA-------------LAARLPELGVPVLA-----------LD----- 598
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 823296640 234 dlwwSDLIENASDQHQPEEMNAEDPLFILYTSGSTGKPKGVL 275
Cdd:COG1020 599 ----ALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVM 636
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
79-311 |
2.30e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 85.21 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 79 ANCLDRHLAERGNETAIIWEGDDasqskhISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAI 158
Cdd:PRK07786 20 VNQLARHALMQPDAPALRFLGNT------TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 159 HSVIFGGFSPEAVAGRIVDSNSKLVITadEGVRAgrgiPLKKNVDEAlknpnVKSINNVIVLkrtGGKIDwheGRDLWWS 238
Cdd:PRK07786 94 AVPVNFRLTPPEIAFLVSDCGAHVVVT--EAALA----PVATAVRDI-----VPLLSTVVVA---GGSSD---DSVLGYE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 823296640 239 DLIENASDQHQPEEMNAEDPLFILYTSGSTGKPKG-VL-HTTggyLVYAATTFKYVFDYHPGDiywctaDVGWVT 311
Cdd:PRK07786 157 DLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGaVLtHAN---LTGQAMTCLRTNGADINS------DVGFVG 222
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
91-301 |
1.03e-17 |
|
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: 82.96 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 91 NETAIIWEGddasqsKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIfggfSPEA 170
Cdd:cd05930 2 DAVAVVDGD------QSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPL----DPSY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 171 VAGRIV----DSNSKLVITadegvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdlienasd 246
Cdd:cd05930 72 PAERLAyileDSGAKLVLT------------------------------------------------------------- 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 823296640 247 qhqpeemNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIY 301
Cdd:cd05930 91 -------DPDDLAYVIYTSGSTGKPKGVMVEHRG-LVNLLLWMQEAYPLTPGDRV 137
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
82-280 |
2.19e-17 |
|
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: 82.32 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 82 LDRHLAERGNETAIIWEGddasqsKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:cd17646 4 VAEQAARTPDAPAVVDEG------RTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 162 IFGGFSPEAVAGRIVDSNSKLVIT-ADEGVRAGRGIPLKKNVDEALKNPnvksinnvivlkrtggkidwhegrdlwwsdl 240
Cdd:cd17646 78 LDPGYPADRLAYMLADAGPAVVLTtADLAARLPAGGDVALLGDEALAAP------------------------------- 126
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 823296640 241 ienASDQHQPEEmNAEDPLFILYTSGSTGKPKGVLHTTGG 280
Cdd:cd17646 127 ---PATPPLVPP-RPDNLAYVIYTSGSTGRPKGVMVTHAG 162
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
82-303 |
2.42e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 82.31 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 82 LDRHLAERGNETAIIW--EGDDASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGaIH 159
Cdd:PRK07529 31 LSRAAARHPDAPALSFllDADPLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG-IA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 160 SVIFGGFSPEAVAGRIVDSNSKLVITAdeGVRAGRGIPLKknVDEALKN-PNVKSINNVIVLKRTGGKIDW--------H 230
Cdd:PRK07529 110 NPINPLLEPEQIAELLRAAGAKVLVTL--GPFPGTDIWQK--VAEVLAAlPELRTVVEVDLARYLPGPKRLavplirrkA 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 823296640 231 EGRDLWWSDLIENASDQH--QPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWC 303
Cdd:PRK07529 186 HARILDFDAELARQPGDRlfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGN-EVANAWLGALLLGLGPGDTVFC 259
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
79-317 |
2.63e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 82.10 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 79 ANCLDRHLAERGNETAIIWEGddasqsKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAI 158
Cdd:PRK06164 13 ASLLDAHARARPDAVALIDED------RPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 159 HSVIFGGFSPEAVAGRIVDSNSKLVITADegvrAGRGIPLKKNVDEALKNpNVKSINNVIVLKRTGGKIDWH-EGRDLWW 237
Cdd:PRK06164 87 VIAVNTRYRSHEVAHILGRGRARWLVVWP----GFKGIDFAAILAAVPPD-ALPPLRAIAVVDDAADATPAPaPGARVQL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 238 SDLIENASDQHQPEEMNAEDPLFILY-TSGSTGKPKGVLHTTGGYLVYAATTFKyVFDYHPGDIYWCTADVGWVTGHSYL 316
Cdd:PRK06164 162 FALPDPAPPAAAGERAADPDAGALLFtTSGTTSGPKLVLHRQATLLRHARAIAR-AYGYDPGAVLLAALPFCGVFGFSTL 240
|
.
gi 823296640 317 L 317
Cdd:PRK06164 241 L 241
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
84-299 |
5.21e-17 |
|
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: 81.24 E-value: 5.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 84 RHLAERGNETAIIWEGDdasqskHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIF 163
Cdd:cd17651 3 RQAARTPDAPALVAEGR------RLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 164 GGFSPEAVAGRIVDSNSKLVITADE-----GVRAGRGIPLkknvdealknpnvksinnvivlkrtggkiDWHEGRDLwws 238
Cdd:cd17651 77 PAYPAERLAFMLADAGPVLVLTHPAlagelAVELVAVTLL-----------------------------DQPGAAAG--- 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823296640 239 dlienASDQHQPeEMNAEDPLFILYTSGSTGKPKGVL--HTTGGYLVYAATTfkyVFDYHPGD 299
Cdd:cd17651 125 -----ADAEPDP-ALDADDLAYVIYTSGSTGRPKGVVmpHRSLANLVAWQAR---ASSLGPGA 178
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
75-277 |
1.59e-16 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 80.02 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 75 LNLAANCLDRhLAERGNETAIIwegdDASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACAR 154
Cdd:PLN02246 23 LPLHDYCFER-LSEFSDRPCLI----DGATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 155 IGAIHSVIFGGFSPEAVAGRIVDSNSKLVITadegvragrgipLKKNVDealKNPNVKSINNVIVLkrtggKIDWHEGRD 234
Cdd:PLN02246 98 RGAVTTTANPFYTPAEIAKQAKASGAKLIIT------------QSCYVD---KLKGLAEDDGVTVV-----TIDDPPEGC 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 823296640 235 LWWSDLIENASDQHQPEEMNAEDPLFILYTSGSTGKPKGVLHT 277
Cdd:PLN02246 158 LHFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLT 200
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
82-286 |
1.87e-16 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 79.71 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 82 LDRHLAERGNETAIIWEGDDASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:PRK13295 30 LDACVASCPDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 162 IFGGFSPEAVAGRIVDSNSKLVITAdegvRAGRGIPLKKNVdEALKnPNVKSINNVIVLkrtGGkidwhEGRDLWWSDLI 241
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLVVP----KTFRGFDHAAMA-RRLR-PELPALRHVVVV---GG-----DGADSFEALLI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 823296640 242 ----ENASDQHQPEEMNAEDP---LFILYTSGSTGKPKGVLHTT----GGYLVYAA 286
Cdd:PRK13295 176 tpawEQEPDAPAILARLRPGPddvTQLIYTSGTTGEPKGVMHTAntlmANIVPYAE 231
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
139-312 |
2.64e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 79.09 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 139 MPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITADEGVRAGRGIPLKKNVDEAlkNPNVksinnVI 218
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLRGGRALPLYSKVVEA--APAK-----AI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 219 VLKRTGGK--IDWHEGrDLWWSDLIENASDQH-------QPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTF 289
Cdd:PLN03051 74 VLPAAGEPvaVPLREQ-DLSWCDFLGVAAAQGsvggneySPVYAPVESVTNILFSSGTTGEPKAIPWTHLSPLRCASDGW 152
|
170 180
....*....|....*....|...
gi 823296640 290 KYVfDYHPGDIYWCTADVGWVTG 312
Cdd:PLN03051 153 AHM-DIQPGDVVCWPTNLGWMMG 174
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
90-277 |
1.14e-15 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 77.42 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 90 GNETAIIWEgDDASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPE 169
Cdd:PRK08008 21 GHKTALIFE-SSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 170 AVAGRIVDSNSKLVITADEGVRAGRgiPLKKNVDEALKNpnvksinnvIVLKRTGgkidwhegrdlwwSDLIENASD--- 246
Cdd:PRK08008 100 ESAWILQNSQASLLVTSAQFYPMYR--QIQQEDATPLRH---------ICLTRVA-------------LPADDGVSSftq 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 823296640 247 --QHQPEEMN------AEDPLFILYTSGSTGKPKGVLHT 277
Cdd:PRK08008 156 lkAQQPATLCyapplsTDDTAEILFTSGTTSRPKGVVIT 194
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
70-277 |
1.74e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 76.96 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 70 YEDGTLnlaANCLDRHLAERGNETAIIWEGddasqsKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAM 149
Cdd:PRK05605 29 YGDTTL---VDLYDNAVARFGDRPALDFFG------ATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 150 LACARIGAI---HSVIfggFSPEAVAGRIVDSNSKLVITAD------EGVRagRGIPLKKNVdealknpNVKSINNVIVL 220
Cdd:PRK05605 100 YAVLRLGAVvveHNPL---YTAHELEHPFEDHGARVAIVWDkvaptvERLR--RTTPLETIV-------SVNMIAAMPLL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823296640 221 KRTGGKI---DWHEGRD---------LWWSDLIENA----SDQHQPEEMNAEDPLFILYTSGSTGKPKGVLHT 277
Cdd:PRK05605 168 QRLALRLpipALRKARAaltgpapgtVPWETLVDAAiggdGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLT 240
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
108-292 |
1.78e-15 |
|
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: 76.48 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 108 ISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAgRIV-DSNSKLVITA 186
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIA-YILnDSEAKALFVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 187 DegvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdlienasdqhqpeemnAEDPLFILYTSG 266
Cdd:cd05907 85 D-------------------------------------------------------------------PDDLATIIYTSG 97
|
170 180
....*....|....*....|....*.
gi 823296640 267 STGKPKGVLHTTGGYLVYAATTFKYV 292
Cdd:cd05907 98 TTGRPKGVMLSHRNILSNALALAERL 123
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
109-274 |
2.31e-15 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 76.39 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 109 SYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITADe 188
Cdd:PRK08315 45 TYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAAD- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 189 gvrAGRG----------IP-LKKNVDEALKNPNVKSINNVIVL--KRTGGKIDwhegrdlwWSDLIENASDQHQPE---- 251
Cdd:PRK08315 124 ---GFKDsdyvamlyelAPeLATCEPGQLQSARLPELRRVIFLgdEKHPGMLN--------FDELLALGRAVDDAElaar 192
|
170 180
....*....|....*....|....*
gi 823296640 252 --EMNAEDPLFILYTSGSTGKPKGV 274
Cdd:PRK08315 193 qaTLDPDDPINIQYTSGTTGFPKGA 217
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
84-289 |
2.50e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 76.23 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 84 RHLAERGNET-AIIWEGDDasqskhISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVI 162
Cdd:PRK06178 40 RAWARERPQRpAIIFYGHV------ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 163 FGGFSPEAVAGRIVDSNSKLVITAD------EGVRAGRgiplkknvdeALKNPNVKSINNVIVLKRTGGKIDWHEGRDLW 236
Cdd:PRK06178 114 SPLFREHELSYELNDAGAEVLLALDqlapvvEQVRAET----------SLRHVIVTSLADVLPAEPTLPLPDSLRAPRLA 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 823296640 237 ---WSDLIENASDQHQP---EEMNAEDPLFILYTSGSTGKPKGVLHTTgGYLVYAATTF 289
Cdd:PRK06178 184 aagAIDLLPALRACTAPvplPPPALDALAALNYTGGTTGMPKGCEHTQ-RDMVYTAAAA 241
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
90-275 |
4.24e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 75.69 E-value: 4.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 90 GNETAIIWeGDDAsqskhISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPE 169
Cdd:PRK07798 17 PDRVALVC-GDRR-----LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVED 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 170 AVAGRIVDSNSKLVITADEgvRAGRgiplkknVDEAL-KNPNVKsinnVIVLKRTGGKIDWHEGrDLWWSDLIENASDQH 248
Cdd:PRK07798 91 ELRYLLDDSDAVALVYERE--FAPR-------VAEVLpRLPKLR----TLVVVEDGSGNDLLPG-AVDYEDALAAGSPER 156
|
170 180
....*....|....*....|....*..
gi 823296640 249 QPEEMNAEDpLFILYTSGSTGKPKGVL 275
Cdd:PRK07798 157 DFGERSPDD-LYLLYTGGTTGMPKGVM 182
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
104-274 |
4.56e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 75.58 E-value: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 104 QSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLV 183
Cdd:PRK12583 42 QALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 184 ITADeGVRA-------GRGIP-LKKNVDEALKNPNVKSINNVIVL--KRTGGKIDWHEgrdlwwsdlIENASDQHQPEEM 253
Cdd:PRK12583 122 ICAD-AFKTsdyhamlQELLPgLAEGQPGALACERLPELRGVVSLapAPPPGFLAWHE---------LQARGETVSREAL 191
|
170 180
....*....|....*....|....*...
gi 823296640 254 NA-------EDPLFILYTSGSTGKPKGV 274
Cdd:PRK12583 192 AErqasldrDDPINIQYTSGTTGFPKGA 219
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
87-277 |
6.25e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 75.00 E-value: 6.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 87 AER-GNETAIIWEGddasqsKHISYKELHRDVCRFANVLLAQ-GIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFG 164
Cdd:PRK08314 20 ARRyPDKTAIVFYG------RAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 165 GFSPEAVAGRIVDSNSKLVITADEgvRAGRGIPLKKnvDEALKnpnvksinNVIVLKRTG-----GKI---DW------- 229
Cdd:PRK08314 94 MNREEELAHYVTDSGARVAIVGSE--LAPKVAPAVG--NLRLR--------HVIVAQYSDylpaePEIavpAWlraeppl 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 823296640 230 ---HEGRDLWWSDLIENasdQHQPEEMNA--EDPLFILYTSGSTGKPKGVLHT 277
Cdd:PRK08314 162 qalAPGGVVAWKEALAA---GLAPPPHTAgpDDLAVLPYTSGTTGVPKGCMHT 211
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
83-275 |
6.90e-15 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 74.93 E-value: 6.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 83 DRHLAERGNETAIIWEGDDasqskhISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVI 162
Cdd:cd12117 4 EEQAARTPDAVAVVYGDRS------LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 163 FGGFSPEAVAGRIVDSNSKLVITADEGVRAGRGIPLKKNVDEALknpnvksinnvivlkRTGGKIDWHEGRDlwwsdlie 242
Cdd:cd12117 78 DPELPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEAL---------------DAGPAGNPAVPVS-------- 134
|
170 180 190
....*....|....*....|....*....|...
gi 823296640 243 nasdqhqpeemnAEDPLFILYTSGSTGKPKGVL 275
Cdd:cd12117 135 ------------PDDLAYVMYTSGSTGRPKGVA 155
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
108-314 |
7.07e-15 |
|
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: 74.81 E-value: 7.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 108 ISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITad 187
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 188 egvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdlienasdqhqpeemNAEDPLFILYTSGS 267
Cdd:cd05919 89 ------------------------------------------------------------------SADDIAYLLYSSGT 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 823296640 268 TGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIYWCTADV--GWVTGHS 314
Cdd:cd05919 103 TGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKMffGYGLGNS 151
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
84-275 |
5.20e-14 |
|
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: 72.27 E-value: 5.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 84 RHLAERGNETAIIWEGDDASQSKHISYKELHRDVCRFANVLLAQGiKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIF 163
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 164 GGFSPEA---VAGRIVDSNSKLVITaDEGVRAGrgiplkknvdealknpnvksinnvivLKRTGGKIDWHEGRDLWWSDL 240
Cdd:cd05931 80 PPTPGRHaerLAAILADAGPRVVLT-TAAALAA--------------------------VRAFAASRPAAGTPRLLVVDL 132
|
170 180 190
....*....|....*....|....*....|....*.
gi 823296640 241 IE-NASDQHQPEEMNAEDPLFILYTSGSTGKPKGVL 275
Cdd:cd05931 133 LPdTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVV 168
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
257-317 |
5.38e-14 |
|
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: 71.55 E-value: 5.38e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 823296640 257 DPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPGDIYWCTADVGWVTGHSYLL 317
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAAS-GGLTEGDVFLSTLPLFHIGGLFGLL 60
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
93-315 |
7.57e-14 |
|
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: 71.57 E-value: 7.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 93 TAIIWEGDdasqskHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVA 172
Cdd:cd17643 4 VAVVDEDR------RLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 173 GRIVDSNSKLVITadegvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdlienasdqhqpee 252
Cdd:cd17643 78 FILADSGPSLLLT------------------------------------------------------------------- 90
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823296640 253 mNAEDPLFILYTSGSTGKPKGVLHTTGGYL-VYAATTfkYVFDYHPGDIywctadvgWVTGHSY 315
Cdd:cd17643 91 -DPDDLAYVIYTSGSTGRPKGVVVSHANVLaLFAATQ--RWFGFNEDDV--------WTLFHSY 143
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
107-274 |
1.56e-13 |
|
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: 70.76 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 107 HISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIfggfSPEAVAGRI----VDSNSKL 182
Cdd:cd12114 12 TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPV----DIDQPAARReailADAGARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 183 VITADEGVragrgiplkKNVDEALknpnvksinnvivlkrtggkidwhegRDLWWSDLIENASDQHQPEEMNAEDPLFIL 262
Cdd:cd12114 88 VLTDGPDA---------QLDVAVF--------------------------DVLILDLDALAAPAPPPPVDVAPDDLAYVI 132
|
170
....*....|..
gi 823296640 263 YTSGSTGKPKGV 274
Cdd:cd12114 133 FTSGSTGTPKGV 144
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
82-282 |
2.64e-13 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 70.17 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 82 LDRHLAERGNETAIIwEGDdasqsKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAI--- 158
Cdd:COG1021 31 LRRRAERHPDRIAVV-DGE-----RRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIpvf 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 159 ------HSVI--FGGFSpEAVAgrivdsnskLVITADEGVRAGRGIplkknVDEALKnpNVKSINNVIVLKRTGGKIDwh 230
Cdd:COG1021 105 alpahrRAEIshFAEQS-EAVA---------YIIPDRHRGFDYRAL-----ARELQA--EVPSLRHVLVVGDAGEFTS-- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 823296640 231 egrdlwWSDLIENASDQHQPeEMNAEDPLFILYTSGSTGKPKGVLHTTGGYL 282
Cdd:COG1021 166 ------LDALLAAPADLSEP-RPDPDDVAFFQLSGGTTGLPKLIPRTHDDYL 210
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
109-317 |
3.20e-13 |
|
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: 69.72 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 109 SYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITADE 188
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 189 gvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwWSdlienasdQHQPEEMNAeDPLFILYTSGST 268
Cdd:cd05903 83 ------------------------------------------------FR--------QFDPAAMPD-AVALLLFTSGTT 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 823296640 269 GKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLL 317
Cdd:cd05903 106 GEPKGVMHSHNT-LSASIRQYAERLGLGPGDVFLVASPMAHQTGFVYGF 153
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
102-275 |
3.22e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 69.93 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 102 ASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSK 181
Cdd:PRK08276 6 APSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 182 LVITADEGVRAGRGIPlkknvdEALKNPnvksinnVIVLKRTGGKIDWHEGrdlwWSDLIENASDQHQPEEMNAEDplfI 261
Cdd:PRK08276 86 VLIVSAALADTAAELA------AELPAG-------VPLLLVVAGPVPGFRS----YEEALAAQPDTPIADETAGAD---M 145
|
170
....*....|....
gi 823296640 262 LYTSGSTGKPKGVL 275
Cdd:PRK08276 146 LYSSGTTGRPKGIK 159
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
109-274 |
5.30e-13 |
|
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: 69.24 E-value: 5.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 109 SYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITADE 188
Cdd:cd12116 14 SYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTDDA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 189 GV-RAGRGIPLKKNVDEALKNPnvksinnvivlkrtggkidwHEGRdlwwsdlienasdqhqPEEMNAEDPLFILYTSGS 267
Cdd:cd12116 94 LPdRLPAGLPVLLLALAAAAAA--------------------PAAP----------------RTPVSPDDLAYVIYTSGS 137
|
....*..
gi 823296640 268 TGKPKGV 274
Cdd:cd12116 138 TGRPKGV 144
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
91-279 |
6.08e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 68.84 E-value: 6.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 91 NETAIIWEGddasqsKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEA 170
Cdd:PRK03640 17 DRTAIEFEE------KKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 171 VAGRIVDSNSKLVITADEGVRagrgiplkknvdealknpnvksinnvivlKRTGGKidwhegrDLWWSDLIE-NASDQHQ 249
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFEA-----------------------------KLIPGI-------SVKFAELMNgPKEEAEI 134
|
170 180 190
....*....|....*....|....*....|
gi 823296640 250 PEEMNAEDPLFILYTSGSTGKPKGVLHTTG 279
Cdd:PRK03640 135 QEEFDLDEVATIMYTSGTTGKPKGVIQTYG 164
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
107-301 |
8.60e-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: 68.47 E-value: 8.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 107 HISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITa 186
Cdd:cd05934 3 RWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 187 degvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdlienasdqhqpeemnaeDPLFILYTSG 266
Cdd:cd05934 82 ----------------------------------------------------------------------DPASILYTSG 91
|
170 180 190
....*....|....*....|....*....|....*
gi 823296640 267 STGKPKGVLhTTGGYLVYAATTFKYVFDYHPGDIY 301
Cdd:cd05934 92 TTGPPKGVV-ITHANLTFAGYYSARRFGLGEDDVY 125
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
75-283 |
1.47e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 67.76 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 75 LNLAaNCLDRHLAERGNETAIIWeGDdasqsKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACAR 154
Cdd:PRK07470 7 MNLA-HFLRQAARRFPDRIALVW-GD-----RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 155 IGAIHSVIFGGFSPEAVAGRIVDSNSKLVITAD---EGVRAGRGIPLkknvdealknpnvkSINNVIVLKRTGGKIDwhe 231
Cdd:PRK07470 80 LGAVWVPTNFRQTPDEVAYLAEASGARAMICHAdfpEHAAAVRAASP--------------DLTHVVAIGGARAGLD--- 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 823296640 232 grdlwWSDLI-ENASDQHQPEEMNAEDPLFILYTSGSTGKPK-GVL-HTTGGYLV 283
Cdd:PRK07470 143 -----YEALVaRHLGARVANAAVDHDDPCWFFFTSGTTGRPKaAVLtHGQMAFVI 192
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
108-287 |
1.87e-12 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 67.59 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 108 ISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVI--- 184
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVcdp 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 185 TADEGVRAgrgiplkknVDEALKNPNVKSINnvivLKRTGGkidwhegrdlwWSDLIENASDQHQPEEMNAEDPLFILYT 264
Cdd:PRK07514 109 ANFAWLSK---------IAAAAGAPHVETLD----ADGTGS-----------LLEAAAAAPDDFETVPRGADDLAAILYT 164
|
170 180
....*....|....*....|...
gi 823296640 265 SGSTGKPKGVLHTTGGYLVYAAT 287
Cdd:PRK07514 165 SGTTGRSKGAMLSHGNLLSNALT 187
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
84-275 |
4.90e-12 |
|
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: 66.41 E-value: 4.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 84 RHLAERGNETAI-IWEGDdasqskhISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIhSVI 162
Cdd:cd05918 7 ERARSQPDAPAVcAWDGS-------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGA-FVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 163 FGGFSPEAVAGRIV-DSNSKLVITadegvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdli 241
Cdd:cd05918 79 LDPSHPLQRLQEILqDTGAKVVLT-------------------------------------------------------- 102
|
170 180 190
....*....|....*....|....*....|....
gi 823296640 242 enasdqHQPeemnaEDPLFILYTSGSTGKPKGVL 275
Cdd:cd05918 103 ------SSP-----SDAAYVIFTSGSTGKPKGVV 125
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
108-274 |
8.99e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 66.13 E-value: 8.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 108 ISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITAD 187
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQS 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 188 egvRAGRGIPLKKNVDealknpnvksinnVIVLKRTGgkidwhegrdLWWSDLIENASDQHqpeeMNAEDPLFILYTSGS 267
Cdd:PRK12316 617 ---HLGRKLPLAAGVQ-------------VLDLDRPA----------AWLEGYSEENPGTE----LNPENLAYVIYTSGS 666
|
....*..
gi 823296640 268 TGKPKGV 274
Cdd:PRK12316 667 TGKPKGA 673
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
101-277 |
1.48e-11 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 65.00 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 101 DASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAihsvIFGGFSPEAVAGRIVD--- 177
Cdd:PLN02330 49 EAVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGG----VFSGANPTALESEIKKqae 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 178 -SNSKLVITADE--GVRAGRGIPlkknvdealknpnvksinnVIVLKRT--GGKIDWHEgrdlwWSDLIENASDQHQPEE 252
Cdd:PLN02330 125 aAGAKLIVTNDTnyGKVKGLGLP-------------------VIVLGEEkiEGAVNWKE-----LLEAADRAGDTSDNEE 180
|
170 180
....*....|....*....|....*
gi 823296640 253 MNAEDPLFILYTSGSTGKPKGVLHT 277
Cdd:PLN02330 181 ILQTDLCALPFSSGTTGISKGVMLT 205
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
76-275 |
2.05e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 64.64 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 76 NLAANCLDRHL--AERGNETAIIWEGDDASQskhISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACA 153
Cdd:PRK05857 11 QLPSTVLDRVFeqARQQPEAIALRRCDGTSA---LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 154 RIGAIhSVIFGGFSPEAVAGRIVDSNSKLVITADEGVRagrgiplkknVDEALKNPNVKSINNVIVLKRTGGKIDWHEGr 233
Cdd:PRK05857 88 KLGAI-AVMADGNLPIAAIERFCQITDPAAALVAPGSK----------MASSAVPEALHSIPVIAVDIAAVTRESEHSL- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 823296640 234 dlwwsdliENASDQHQPEeMNAEDPLFILYTSGSTGKPKGVL 275
Cdd:PRK05857 156 --------DAASLAGNAD-QGSEDPLAMIFTSGTTGEPKAVL 188
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
108-310 |
2.17e-11 |
|
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: 64.37 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 108 ISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITAD 187
Cdd:cd17641 12 FTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAED 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 188 EgvragrgiplkKNVDEALK-NPNVKSINNVIVLKRTGGKiDWHEGRDLWWSDLIE--NASDQHQPEEMNA-------ED 257
Cdd:cd17641 92 E-----------EQVDKLLEiADRIPSVRYVIYCDPRGMR-KYDDPRLISFEDVVAlgRALDRRDPGLYERevaagkgED 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 823296640 258 PLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKyvFDY-HPGDIYWCTADVGWV 310
Cdd:cd17641 160 VAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLA--ADPlGPGDEYVSVLPLPWI 211
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
93-306 |
2.45e-11 |
|
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: 64.19 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 93 TAIIWEGDDasqskhISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVA 172
Cdd:cd05945 8 PAVVEGGRT------LTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 173 gRIVDSNSKLVITADEGvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdlienasdqhqpee 252
Cdd:cd05945 82 -EILDAAKPALLIADGD--------------------------------------------------------------- 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 823296640 253 mnaeDPLFILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPGDIYWCTAD 306
Cdd:cd05945 98 ----DNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSD-FPLGPGDVFLNQAP 146
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
104-274 |
2.76e-11 |
|
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: 64.03 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 104 QSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLV 183
Cdd:cd17656 10 ENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 184 ITADEgvragrgiplkknvdealkNPNVKSINNVIVLkrtggkIDWhegrdlwwsDLIENASDQHQPEEMNAEDPLFILY 263
Cdd:cd17656 90 LTQRH-------------------LKSKLSFNKSTIL------LED---------PSISQEDTSNIDYINNSDDLLYIIY 135
|
170
....*....|.
gi 823296640 264 TSGSTGKPKGV 274
Cdd:cd17656 136 TSGTTGKPKGV 146
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
109-275 |
2.82e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 64.06 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 109 SYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLvITADE 188
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRL-LLGDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 189 GVRAGRGIPLkknvdealknpnvksinnvivlkrtggkidwhegrDLwwSDLIENAsDQHQPEE---MNAEDPLFILYTS 265
Cdd:PRK09088 103 AVAAGRTDVE-----------------------------------DL--AAFIASA-DALEPADtpsIPPERVSLILFTS 144
|
170
....*....|
gi 823296640 266 GSTGKPKGVL 275
Cdd:PRK09088 145 GTSGQPKGVM 154
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
73-277 |
2.95e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 63.85 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 73 GTLNLAAncldrhLAERGNETAIIWegDDASqskhISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEA----AVA 148
Cdd:PRK06188 15 GHLLVSA------LKRYPDRPALVL--GDTR----LTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVlmaiGAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 149 MLACARIGAIHSVIfggfSPEAVAGRIVDSNSKLVItADEGVRAGRGIPLKKNVDealknpnvkSINNVIVLKRTGGkid 228
Cdd:PRK06188 83 QLAGLRRTALHPLG----SLDDHAYVLEDAGISTLI-VDPAPFVERALALLARVP---------SLKHVLTLGPVPD--- 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 823296640 229 wheGRDLWwsdlieNASDQHQPEEMNAE----DPLFILYTSGSTGKPKGVLHT 277
Cdd:PRK06188 146 ---GVDLL------AAAAKFGPAPLVAAalppDIAGLAYTGGTTGKPKGVMGT 189
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
107-275 |
2.99e-11 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 64.30 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 107 HISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITA 186
Cdd:PRK10252 483 QFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITT 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 187 DEgvRAGR--GIPlkknvDEALKNPNVksinnvivlkrtggkidwhegrdlWWsdlienASDQHQPEEMNA-EDPLFILY 263
Cdd:PRK10252 563 AD--QLPRfaDVP-----DLTSLCYNA------------------------PL------APQGAAPLQLSQpHHTAYIIF 605
|
170
....*....|..
gi 823296640 264 TSGSTGKPKGVL 275
Cdd:PRK10252 606 TSGSTGRPKGVM 617
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
106-274 |
3.11e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.59 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 106 KHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVIT 185
Cdd:PRK12316 2027 QHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT 2106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 186 aDEGVRAGRGIPlkknvdealknpnvksiNNVIVLKRTggkidwhegRDLWWSDlienaSDQHQPEEMNAEDPL-FILYT 264
Cdd:PRK12316 2107 -QRHLLERLPLP-----------------AGVARLPLD---------RDAEWAD-----YPDTAPAVQLAGENLaYVIYT 2154
|
170
....*....|
gi 823296640 265 SGSTGKPKGV 274
Cdd:PRK12316 2155 SGSTGLPKGV 2164
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
87-277 |
3.14e-11 |
|
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: 63.80 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 87 AERGNETAIIWEGDDASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGF 166
Cdd:cd12119 5 AARLHGDREIVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 167 SPEAVAGRIVDSNSKLVITADEGVragrgiPLKKNVDEALKNpnvksINNVIVLKRTGGKIDWHEGRDLWWSDLIENASD 246
Cdd:cd12119 85 FPEQIAYIINHAEDRVVFVDRDFL------PLLEAIAPRLPT-----VEHVVVMTDDAAMPEPAGVGVLAYEELLAAESP 153
|
170 180 190
....*....|....*....|....*....|.
gi 823296640 247 QHQPEEMNAEDPLFILYTSGSTGKPKGVLHT 277
Cdd:cd12119 154 EYDWPDFDENTAAAICYTSGTTGNPKGVVYS 184
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
106-302 |
3.25e-11 |
|
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: 63.60 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 106 KHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVIT 185
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 186 adegvragrgiplkkNVDEALKNPNVKSINNVIVLkrtggkidwhegrdlwwsdlienasdqhqpeemNAEDPLFILYTS 265
Cdd:cd05939 82 ---------------NLLDPLLTQSSTEPPSQDDV---------------------------------NFRDKLFYIYTS 113
|
170 180 190
....*....|....*....|....*....|....*..
gi 823296640 266 GSTGKPKGVLHTTGGYLVYAATTFkYVFDYHPGDIYW 302
Cdd:cd05939 114 GTTGLPKAAVIVHSRYYRIAAGAY-YAFGMRPEDVVY 149
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
101-274 |
3.45e-11 |
|
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: 63.68 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 101 DASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNS 180
Cdd:cd05923 22 DPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 181 KLVITAD--EGVRAGRGIPLKknvdealknpnvksINNVIVLKRTGgkidwhegrdlwwsdLIENASDQHQPEEMNAEDP 258
Cdd:cd05923 102 TAAVIAVdaQVMDAIFQSGVR--------------VLALSDLVGLG---------------EPESAGPLIEDPPREPEQP 152
|
170
....*....|....*.
gi 823296640 259 LFILYTSGSTGKPKGV 274
Cdd:cd05923 153 AFVFYTSGTTGLPKGA 168
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
108-309 |
4.99e-11 |
|
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: 62.97 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 108 ISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIhsvifggfspeavagriVDSNSKLVITAD 187
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAV-----------------VIPATTLLTPDD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 188 EGVRAGRGIPLKKNVDEAlknpnvksinnvivlkrtggkidwhegrdlwwsdlienasdqhqpeeMNAEDPLFILYTSGS 267
Cdd:cd05974 64 LRDRVDRGGAVYAAVDEN-----------------------------------------------THADDPMLLYFTSGT 96
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 823296640 268 TGKPKGVLHTTGGYLVYAATTFkYVFDYHPGDIYWCTADVGW 309
Cdd:cd05974 97 TSKPKLVEHTHRSYPVGHLSTM-YWIGLKPGDVHWNISSPGW 137
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
109-312 |
7.55e-11 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 62.84 E-value: 7.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 109 SYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITade 188
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 189 gvragrgiPLKKN----VDEALKNPN-VKSINNVIVLKRTGGKIDwhegrDLWWSDLIENASDQHQPEEMNAEDPLFILY 263
Cdd:PRK06087 128 --------PTLFKqtrpVDLILPLQNqLPQLQQIVGVDKLAPATS-----SLSLSQIIADYEPLTTAITTHGDELAAVLF 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 823296640 264 TSGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWCTADVGWVTG 312
Cdd:PRK06087 195 TSGTEGLPKGVMLTHNN-ILASERAYCARLNLTWQDVFMMPAPLGHATG 242
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
81-274 |
1.10e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 62.67 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 81 CLDRHLAERGNET----AIIWEGddasqsKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIG 156
Cdd:PRK12316 4552 CVHQLVAERARMTpdavAVVFDE------EKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAG 4625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 157 AIHSVIFGGFSPEAVAGRIVDSNSKLVITADegvRAGRGIPLKKNVDEalknpnvksinnvIVLKRTGgkiDWhEGRdlw 236
Cdd:PRK12316 4626 GAYVPLDPEYPRERLAYMMEDSGAALLLTQS---HLLQRLPIPDGLAS-------------LALDRDE---DW-EGF--- 4682
|
170 180 190
....*....|....*....|....*....|....*....
gi 823296640 237 wsdlienasDQHQPE-EMNAEDPLFILYTSGSTGKPKGV 274
Cdd:PRK12316 4683 ---------PAHDPAvRLHPDNLAYVIYTSGSTGRPKGV 4712
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
84-278 |
1.23e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 62.25 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 84 RHLAERG-NETAIIwegDDASQskhISYKELHRDVCRFANVLLAQGIKKGDVVAI----YMPMVpeaaVAMLACARIGAI 158
Cdd:PRK07788 56 AHAARRApDRAALI---DERGT---LTYAELDEQSNALARGLLALGVRAGDGVAVlarnHRGFV----LALYAAGKVGAR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 159 HSVIFGGFSPEAVAGRIVDSNSKLVITADEGVRAGRGIPlkknvdealknPNVKSInNVIVLKRTGGKIDWHEGRDLwwS 238
Cdd:PRK07788 126 IILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALP-----------PDLGRL-RAWGGNPDDDEPSGSTDETL--D 191
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 823296640 239 DLIENASDQHQPEemnAEDP-LFILYTSGSTGKPKGVLHTT 278
Cdd:PRK07788 192 DLIAGSSTAPLPK---PPKPgGIVILTSGTTGTPKGAPRPE 229
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
108-301 |
1.34e-10 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 62.06 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 108 ISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITAD 187
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 188 EgvragrgiPLKKNVDEALKnpnVKSINNVIVLKRTGGKIDWHEGRDLWW-----SDLIENASDQHQPEEM-NAEDPLFI 261
Cdd:PLN02387 187 K--------QLKKLIDISSQ---LETVKRVIYMDDEGVDSDSSLSGSSNWtvssfSEVEKLGKENPVDPDLpSPNDIAVI 255
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 823296640 262 LYTSGSTGKPKGVLHTTGGYLVYAATTFKYVFDYHPGDIY 301
Cdd:PLN02387 256 MYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVY 295
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
103-274 |
1.58e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 61.64 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 103 SQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSK- 181
Cdd:PRK12406 7 SGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 182 LVITAD--EGVRAgrGIPLKKNVDEALKNPNVKSINNVIVLKRT--GGKIDWHEgrdlWWSdlienasdQHQP-EEMNAE 256
Cdd:PRK12406 87 LIAHADllHGLAS--ALPAGVTVLSVPTPPEIAAAYRISPALLTppAGAIDWEG----WLA--------QQEPyDGPPVP 152
|
170
....*....|....*...
gi 823296640 257 DPLFILYTSGSTGKPKGV 274
Cdd:PRK12406 153 QPQSMIYTSGTTGHPKGV 170
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
107-299 |
1.66e-10 |
|
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: 61.50 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 107 HISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITa 186
Cdd:cd17652 12 TLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLT- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 187 degvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdlienasdqhqpeemNAEDPLFILYTSG 266
Cdd:cd17652 91 -------------------------------------------------------------------TPDNLAYVIYTSG 103
|
170 180 190
....*....|....*....|....*....|....*
gi 823296640 267 STGKPKGVL--HTTGGYLVYAATTFkyvFDYHPGD 299
Cdd:cd17652 104 STGRPKGVVvtHRGLANLAAAQIAA---FDVGPGS 135
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
93-279 |
2.72e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 61.06 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 93 TAIIWEGDDasqskhISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVA 172
Cdd:PRK06145 19 AALVYRDQE------ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 173 GRIVDSNSKLVITaDEGVRAGRGIPLKKNVDEALKNPNVKsinnviVLKRTGGKIdwhegrdlwwsdlienasdqhQPEE 252
Cdd:PRK06145 93 YILGDAGAKLLLV-DEEFDAIVALETPKIVIDAAAQADSR------RLAQGGLEI---------------------PPQA 144
|
170 180
....*....|....*....|....*...
gi 823296640 253 MNAEDPLF-ILYTSGSTGKPKGVLHTTG 279
Cdd:PRK06145 145 AVAPTDLVrLMYTSGTTDRPKGVMHSYG 172
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
102-289 |
3.34e-10 |
|
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: 60.41 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 102 ASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSK 181
Cdd:cd12115 19 VCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQAR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 182 LVITadegvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdlienasdqhqpeemNAEDPLFI 261
Cdd:cd12115 99 LVLT--------------------------------------------------------------------DPDDLAYV 110
|
170 180 190
....*....|....*....|....*....|.
gi 823296640 262 LYTSGSTGKPKGVL---HTTGGYLVYAATTF 289
Cdd:cd12115 111 IYTSGSTGRPKGVAiehRNAAAFLQWAAAAF 141
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
84-300 |
4.02e-10 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 60.68 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 84 RHL----AERGNETAII----WEGDDASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARI 155
Cdd:PRK09274 10 RHLpraaQERPDQLAVAvpggRGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 156 GAIHSVIFGGFSPEAVAGRIVDSNSKLVItadegvragrGIPlKKNVDEALKNPNVKSINNVIVlkrTGGKIDWhEGRDL 235
Cdd:PRK09274 90 GAVPVLVDPGMGIKNLKQCLAEAQPDAFI----------GIP-KAHLARRLFGWGKPSVRRLVT---VGGRLLW-GGTTL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 823296640 236 wwsDLIENASDQHQPE--EMNAEDPLFILYTSGSTGKPKGVLHTTGGYL--VYAAttfKYVFDYHPGDI 300
Cdd:PRK09274 155 ---ATLLRDGAAAPFPmaDLAPDDMAAILFTSGSTGTPKGVVYTHGMFEaqIEAL---REDYGIEPGEI 217
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
87-280 |
4.64e-10 |
|
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: 60.42 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 87 AERG-NETAIIWEGDdasqskHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIfgg 165
Cdd:cd17655 7 AEKTpDHTAVVFEDQ------TLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 166 fSPEAVAGRIV----DSNSKLVITADegvragrgiPLKKNVDEAlknpnvksinnvivlkrtgGKIDWHEGRDlwwsdlI 241
Cdd:cd17655 78 -DPDYPEERIQyileDSGADILLTQS---------HLQPPIAFI-------------------GLIDLLDEDT------I 122
|
170 180 190
....*....|....*....|....*....|....*....
gi 823296640 242 ENASDQHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGG 280
Cdd:cd17655 123 YHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRG 161
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
106-277 |
2.63e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 58.12 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 106 KHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVIT 185
Cdd:PRK06710 48 KDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 186 AD---------------EGV---RAGRGIPLKKNvdeaLKNPNV-KSINNVIVlkrtggKIDWHEGRDLWWSdlIENASD 246
Cdd:PRK06710 128 LDlvfprvtnvqsatkiEHVivtRIADFLPFPKN----LLYPFVqKKQSNLVV------KVSESETIHLWNS--VEKEVN 195
|
170 180 190
....*....|....*....|....*....|..
gi 823296640 247 QHQPEEMNAEDPLFIL-YTSGSTGKPKGVLHT 277
Cdd:PRK06710 196 TGVEVPCDPENDLALLqYTGGTTGFPKGVMLT 227
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
70-282 |
3.13e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 57.65 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 70 YEDGTLNLAANC--------LDRHLAERGNETAIIWEGddasqsKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPM 141
Cdd:PRK08162 4 YEQGLDRNAANYvpltplsfLERAAEVYPDRPAVIHGD------RRRTWAETYARCRRLASALARRGIGRGDTVAVLLPN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 142 VPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITADEGVragrgiPLKKNVDEALKNPNVKSINnvIVLK 221
Cdd:PRK08162 78 IPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFA------EVAREALALLPGPKPLVID--VDDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823296640 222 RTGGKidwHEGRDLWWSDLIENASDQHQPEEMNAE-DPLFILYTSGSTGKPKGVL-HTTGGYL 282
Cdd:PRK08162 150 EYPGG---RFIGALDYEAFLASGDPDFAWTLPADEwDAIALNYTSGTTGNPKGVVyHHRGAYL 209
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
106-279 |
3.85e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 57.68 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 106 KHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVIT 185
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 186 ADEGVragrgiplkKNVDEALKNPNVKSINnVIVLKRTGGKIDWHEGRDLWWSDLIEN---ASDQHQ---PEemNAEDPL 259
Cdd:PTZ00216 200 NGKNV---------PNLLRLMKSGGMPNTT-IIYLDSLPASVDTEGCRLVAWTDVVAKghsAGSHHPlniPE--NNDDLA 267
|
170 180
....*....|....*....|
gi 823296640 260 FILYTSGSTGKPKGVLHTTG 279
Cdd:PTZ00216 268 LIMYTSGTTGDPKGVMHTHG 287
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
117-317 |
5.30e-09 |
|
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: 57.06 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 117 VCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEavagrIVDSNSKLVItADEGVRAGrgI 196
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPT-----LKESVLRYLV-ADAGGRIV--L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 197 PLKKNVDEALKNPNVKSINNVIVlkrtggkidwheGRDLWWSDliENASDQHQPEEmnaEDPLFILYTSGSTGKPKGVL- 275
Cdd:cd05922 75 ADAGAADRLRDALPASPDPGTVL------------DADGIRAA--RASAPAHEVSH---EDLALLLYTSGSTGSPKLVRl 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 823296640 276 -HTTggyLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYLL 317
Cdd:cd05922 138 sHQN---LLANARSIAEYLGITADDRALTVLPLSYDYGLSVLN 177
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
102-307 |
5.61e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 102 ASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPeAVAGRIV-DSNS 180
Cdd:PRK13390 19 AETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA-PEADYIVgDSGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 181 KLVI--TADEGVRAGRGIPLKKNVDealknpnvksinnvivlkrTGGKIDwhegrdlWWSDLiENASDQHQPEEmnAEDP 258
Cdd:PRK13390 98 RVLVasAALDGLAAKVGADLPLRLS-------------------FGGEID-------GFGSF-EAALAGAGPRL--TEQP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 823296640 259 L--FILYTSGSTGKPKGV--------LHTTGGYLVYAATTFkyvFDYHPGDIYWCTADV 307
Cdd:PRK13390 149 CgaVMLYSSGTTGFPKGIqpdlpgrdVDAPGDPIVAIARAF---YDISESDIYYSSAPI 204
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
87-277 |
7.20e-09 |
|
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: 56.52 E-value: 7.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 87 AERGNETAIIWEGDDASQSKhISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACarigaihsvIFGGF 166
Cdd:cd05906 20 AERGPTKGITYIDADGSEEF-QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAC---------VLAGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 167 SPeavagrivdsnsklvitadegvragrgIPLKKNVDEALKNPNVKSINNV-------IVLKRTGG--------KIDWHE 231
Cdd:cd05906 90 VP---------------------------APLTVPPTYDEPNARLRKLRHIwqllgspVVLTDAELvaefagleTLSGLP 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 823296640 232 GRDLwwsDLIENASDQ------HQPEemnAEDPLFILYTSGSTGKPKGVLHT 277
Cdd:cd05906 143 GIRV---LSIEELLDTaadhdlPQSR---PDDLALLMLTSGSTGFPKAVPLT 188
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
109-277 |
7.84e-09 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 56.75 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 109 SYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITADE 188
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 189 GVRagrgiplkknvdeALKNPNVKSINNV--IVLKRTGGKIDWHEGRDLW-----WSDLIENAsdQHQPEEMNAEDPL-- 259
Cdd:PLN02430 158 KIK-------------ELLEPDCKSAKRLkaIVSFTSVTEEESDKASQIGvktysWIDFLHMG--KENPSETNPPKPLdi 222
|
170
....*....|....*....
gi 823296640 260 -FILYTSGSTGKPKGVLHT 277
Cdd:PLN02430 223 cTIMYTSGTSGDPKGVVLT 241
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
102-291 |
8.65e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 57.09 E-value: 8.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 102 ASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSK 181
Cdd:PRK12467 532 VFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVR 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 182 LVITADEGVRAgrgIPLKKNVdealknpnvksinNVIVLKRTGgkidwhegrdlwwsDLIENASDQHQPEEMNAEDPLFI 261
Cdd:PRK12467 612 LLLTQSHLLAQ---LPVPAGL-------------RSLCLDEPA--------------DLLCGYSGHNPEVALDPDNLAYV 661
|
170 180 190
....*....|....*....|....*....|
gi 823296640 262 LYTSGSTGKPKGVLHTTGGYLVYAATTFKY 291
Cdd:PRK12467 662 IYTSGSTGQPKGVAISHGALANYVCVIAER 691
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
108-277 |
1.01e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 56.02 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 108 ISYKELHRDVCRFANVLLAQ-GIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITA 186
Cdd:PRK06839 28 MTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 187 DEGVRAgrgiplkknvdealknpnVKSINNVIVLKRTggkidwhegrdLWWSDLIEnaSDQHQP---EEMNAEDPLFILY 263
Cdd:PRK06839 108 KTFQNM------------------ALSMQKVSYVQRV-----------ISITSLKE--IEDRKIdnfVEKNESASFIICY 156
|
170
....*....|....
gi 823296640 264 TSGSTGKPKGVLHT 277
Cdd:PRK06839 157 TSGTTGKPKGAVLT 170
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
108-184 |
1.35e-08 |
|
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: 55.82 E-value: 1.35e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 823296640 108 ISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVI 184
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
106-303 |
1.38e-08 |
|
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: 55.83 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 106 KHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIhSVIFGGFSPEAVAGRIV-DSNSKLVI 184
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAV-DVVRGSDSSVEELLYILnHSESVALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 185 tadegvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdlIENASDqhqpeemnaeDPLFILYT 264
Cdd:cd17640 83 --------------------------------------------------------VENDSD----------DLATIIYT 96
|
170 180 190
....*....|....*....|....*....|....*....
gi 823296640 265 SGSTGKPKGVLHTTGGyLVYAATTFKYVFDYHPGDIYWC 303
Cdd:cd17640 97 SGTTGNPKGVMLTHAN-LLHQIRSLSDIVPPQPGDRFLS 134
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
72-282 |
1.75e-08 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 55.62 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 72 DGTLNLAANCLDRHlaERGNETAIIwegdDASQSKHISYKELHRDVCRFANVLLAQ-GIKKGDVVAIYMPMVPEAAVAML 150
Cdd:PLN02574 37 DPNLDAVSFIFSHH--NHNGDTALI----DSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 151 ACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITADEGVraGRGIPLKKNVDEALKNPNVKSINNvivlkrtggkidwh 230
Cdd:PLN02574 111 AVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTSPENV--EKLSPLGVPVIGVPENYDFDSKRI-------------- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 823296640 231 EGRDLWWsdLIENASDQHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYL 282
Cdd:PLN02574 175 EFPKFYE--LIKEDFDFVPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLI 224
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
93-299 |
1.86e-08 |
|
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: 55.07 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 93 TAIIWEGddasqsKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVA 172
Cdd:cd17649 4 VALVFGD------QSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 173 GRIVDSNSKLVITadegvragrgiplkknvdealknpnvksinnvivlkrtggkidwHEGRDLWWsdlienasdqhqpee 252
Cdd:cd17649 78 YMLEDSGAGLLLT--------------------------------------------HHPRQLAY--------------- 98
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 823296640 253 mnaedplfILYTSGSTGKPKGVLHTTGGYLVYAATTFKYvFDYHPGD 299
Cdd:cd17649 99 --------VIYTSGSTGTPKGVAVSHGPLAAHCQATAER-YGLTPGD 136
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
108-277 |
3.29e-08 |
|
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: 54.41 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 108 ISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITAD 187
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 188 EgvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdlienasdqhqpeemnAEDPLFILYTSGS 267
Cdd:cd05935 82 E------------------------------------------------------------------LDDLALIPYTSGT 95
|
170
....*....|
gi 823296640 268 TGKPKGVLHT 277
Cdd:cd05935 96 TGLPKGCMHT 105
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
100-288 |
3.82e-08 |
|
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: 54.24 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 100 DDASQSkhISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGfSPEAVAGRIVD-S 178
Cdd:cd17653 17 ESLGGS--LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK-LPSARIQAILRtS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 179 NSKLVITADegvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdlienasdqhqpeemNAEDP 258
Cdd:cd17653 94 GATLLLTTD------------------------------------------------------------------SPDDL 107
|
170 180 190
....*....|....*....|....*....|
gi 823296640 259 LFILYTSGSTGKPKGVLHTTGGYLVYAATT 288
Cdd:cd17653 108 AYIIFTSGSTGIPKGVMVPHRGVLNYVSQP 137
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
103-277 |
7.09e-08 |
|
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: 53.37 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 103 SQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKL 182
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 183 VITadegvragrgiplkknvdealkNPNvksinnvivlkrtggkidwhegrdlwwsdlienasdqhqpeemnAEDPLFIL 262
Cdd:cd17639 81 IFT----------------------DGK--------------------------------------------PDDLACIM 94
|
170
....*....|....*
gi 823296640 263 YTSGSTGKPKGVLHT 277
Cdd:cd17639 95 YTSGSTGNPKGVMLT 109
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
82-309 |
1.24e-07 |
|
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: 52.69 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 82 LDRHLAERGNETAIIWEgddasqSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:cd12118 10 LERAAAVYPDRTSIVYG------DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 162 IFGGFSPEAVAGRIVDSNSKLVItadegvragrgiplkknVDEALKnpnvksinnvivlkrtggkidwhegrdlwWSDLI 241
Cdd:cd12118 84 LNTRLDAEEIAFILRHSEAKVLF-----------------VDREFE-----------------------------YEDLL 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823296640 242 ENASDQHQPEEMNAE-DPLFILYTSGSTGKPKGVLHT-TGGYLvyAATTFKYVFDYHPGDIYWCTADV----GW 309
Cdd:cd12118 118 AEGDPDFEWIPPADEwDPIALNYTSGTTGRPKGVVYHhRGAYL--NALANILEWEMKQHPVYLWTLPMfhcnGW 189
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
22-274 |
1.58e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 52.86 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 22 EQYQEKYQQSVSSPDAFWGE----QGHILDWIKPYQKVKNTSFAPGNVSIKWYEDgtlnlaancldrHLAERGNETAIIW 97
Cdd:PRK12467 3049 ESFDRLLQAMLNNPAARLGElptlAAHERRQVLHAWNATAAAYPSERLVHQLIEA------------QVARTPEAPALVF 3116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 98 EGddasqsKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVD 177
Cdd:PRK12467 3117 GD------QQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIED 3190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 178 SNSKLVITadegvragrgiplKKNVDEALKNPNVksiNNVIVLKRtggkidwhegrDLWWSDLIENASDQHQPEEMnaed 257
Cdd:PRK12467 3191 SGVKLLLT-------------QAHLLEQLPAPAG---DTALTLDR-----------LDLNGYSENNPSTRVMGENL---- 3239
|
250
....*....|....*..
gi 823296640 258 pLFILYTSGSTGKPKGV 274
Cdd:PRK12467 3240 -AYVIYTSGSTGKPKGV 3255
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
91-277 |
2.17e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 52.09 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 91 NETAIIWEgddasqSKHISYKELHRDVCRFANVLLAQGiKKGDVVAIYMPMVPE-----AAVAMLACARIGaihsvIFGG 165
Cdd:PRK07638 16 NKIAIKEN------DRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEflqlfAGAAMAGWTCVP-----LDIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 166 FSPEAVAGRIVDSNSKLVITadegvragrgiplkknvDEALKNPnvksINNVivlkrTGGKIDWHEgrdlwWSDLIENAS 245
Cdd:PRK07638 84 WKQDELKERLAISNADMIVT-----------------ERYKLND----LPDE-----EGRVIEIDE-----WKRMIEKYL 132
|
170 180 190
....*....|....*....|....*....|..
gi 823296640 246 DQHQPEEMNAEDPLFILYTSGSTGKPKGVLHT 277
Cdd:PRK07638 133 PTYAPIENVQNAPFYMGFTSGSTGKPKAFLRA 164
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
108-277 |
3.40e-07 |
|
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: 51.45 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 108 ISYKELHRDVCRFANVLLAQGIK--KGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAgRIVDsNSKL-VI 184
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIE-YILN-HAEIsIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 185 TADEGVRagrgiplkknvdealknpnvksinnvIVLkrtggkidwhegrdlwWSDLIE-NASDQHQPEEMNAEDPLFILY 263
Cdd:cd05927 84 FCDAGVK--------------------------VYS----------------LEEFEKlGKKNKVPPPPPKPEDLATICY 121
|
170
....*....|....
gi 823296640 264 TSGSTGKPKGVLHT 277
Cdd:cd05927 122 TSGTTGNPKGVMLT 135
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
107-275 |
3.90e-07 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 51.30 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 107 HISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITA 186
Cdd:PRK06155 46 RWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 187 DEGVRAGRGIPlkknvdealknPNVKSINNVIVLkrtGGKIDWHEgrDLWWSDLIENASDQHQP-EEMNAEDPLFILYTS 265
Cdd:PRK06155 126 AALLAALEAAD-----------PGDLPLPAVWLL---DAPASVSV--PAGWSTAPLPPLDAPAPaAAVQPGDTAAILYTS 189
|
170
....*....|
gi 823296640 266 GSTGKPKGVL 275
Cdd:PRK06155 190 GTTGPSKGVC 199
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
108-275 |
6.35e-07 |
|
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: 50.54 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 108 ISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITad 187
Cdd:cd17650 13 LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLT-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 188 egvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdlienasdqhQPeemnaEDPLFILYTSGS 267
Cdd:cd17650 91 -------------------------------------------------------------QP-----EDLAYVIYTSGT 104
|
....*...
gi 823296640 268 TGKPKGVL 275
Cdd:cd17650 105 TGKPKGVM 112
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
115-316 |
6.39e-07 |
|
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: 50.51 E-value: 6.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 115 RDVC-RFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITADEGVR-A 192
Cdd:cd05915 31 YQRArRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLPlV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 193 GRGIPLKKNVDEalkNPNVKSinnvivlkrtggKIDWHEgrdlwwsDLIENASDQHQP-EEMNAEDPLFILYTSGSTGKP 271
Cdd:cd05915 111 EAIRGELKTVQH---FVVMDE------------KAPEGY-------LAYEEALGEEADpVRVPERAACGMAYTTGTTGLP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 823296640 272 KGVLHT-TGGYLVYAATTFKYVFDYHPGDIYWCTADVGWVTGHSYL 316
Cdd:cd05915 169 KGVVYShRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLP 214
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
104-192 |
1.23e-06 |
|
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: 49.74 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 104 QSKHISYKELHRDVCRFANVLL-AQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKL 182
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRF 81
|
90
....*....|
gi 823296640 183 VITADEGVRA 192
Cdd:cd05937 82 VIVDPDDPAI 91
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
93-277 |
1.55e-06 |
|
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: 49.21 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 93 TAIIwegddASQSKHiSYKELHRDVCRFANVLLAQG-IKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAV 171
Cdd:cd05941 3 IAIV-----DDGDSI-TYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 172 AGRIVDSNSKLVItadegvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdlienasdqhqpe 251
Cdd:cd05941 77 EYVITDSEPSLVL------------------------------------------------------------------- 89
|
170 180
....*....|....*....|....*.
gi 823296640 252 emnaeDPLFILYTSGSTGKPKGVLHT 277
Cdd:cd05941 90 -----DPALILYTSGTTGRPKGVVLT 110
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
100-275 |
1.59e-06 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 49.68 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 100 DDASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEavagR--IVD 177
Cdd:TIGR03443 263 DPSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPA----RqtIYL 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 178 SNSK---LVITADegvrAGRGIPL-----KKNVDEALKNPNVKSINNVIVlkrTGGKIDwhegrdlwwsdliENASDQHQ 249
Cdd:TIGR03443 339 SVAKpraLIVIEK----AGTLDQLvrdyiDKELELRTEIPALALQDDGSL---VGGSLE-------------GGETDVLA 398
|
170 180 190
....*....|....*....|....*....|....*.
gi 823296640 250 PEEMNAEDPLFIL----------YTSGSTGKPKGVL 275
Cdd:TIGR03443 399 PYQALKDTPTGVVvgpdsnptlsFTSGSEGIPKGVL 434
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
54-277 |
2.78e-06 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 48.72 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 54 KVKNTSFAPGNVSIKWYEDGTLNLAAN------------CLDRHLAERGNETAIIwEGDDASQSKHISYKELHRDVCRFA 121
Cdd:PRK08180 5 RYRPVAFAPPAVEVERRADGTIYLRSAeplgdyprrltdRLVHWAQEAPDRVFLA-ERGADGGWRRLTYAEALERVRAIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 122 NVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIfggfSPeAVAGRIVDSnSKL----------VITADEGVR 191
Cdd:PRK08180 84 QALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPV----SP-AYSLVSQDF-GKLrhvlelltpgLVFADDGAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 192 AGRGIplkknvdEALKNPNVKsinnVIVLKRTGGkidwhEGRDLWWSDLIENASDQHQPEEMNAEDPLFI---LYTSGST 268
Cdd:PRK08180 158 FARAL-------AAVVPADVE----VVAVRGAVP-----GRAATPFAALLATPPTAAVDAAHAAVGPDTIakfLFTSGST 221
|
....*....
gi 823296640 269 GKPKGVLHT 277
Cdd:PRK08180 222 GLPKAVINT 230
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
108-272 |
5.96e-06 |
|
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: 47.67 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 108 ISYKELHRDVCRFANVLLAQ-GIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITA 186
Cdd:cd05938 6 YTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 187 DEgvragrgipLKKNVDEALknPNVKSiNNVIVLKRTGGKIdwHEG-RDLwwSDLIENASDQHQPEEMNAE----DPLFI 261
Cdd:cd05938 86 PE---------LQEAVEEVL--PALRA-DGVSVWYLSHTSN--TEGvISL--LDKVDAASDEPVPASLRAHvtikSPALY 149
|
170
....*....|.
gi 823296640 262 LYTSGSTGKPK 272
Cdd:cd05938 150 IYTSGTTGLPK 160
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
79-274 |
8.99e-06 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 47.19 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 79 ANCLDRHLAERGNETAIIWegddASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAI 158
Cdd:PRK05852 19 ADLVEVAATRLPEAPALVV----TADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 159 HSVIFGGFSPEAVAGRIVDSNSKLVITADEGV-----RAGRGIPLKKNVDEalknpnvksinnviVLKRTGGKIDWHEGr 233
Cdd:PRK05852 95 VVPLDPALPIAEQRVRSQAAGARVVLIDADGPhdraePTTRWWPLTVNVGG--------------DSGPSGGTLSVHLD- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 823296640 234 dlwwsDLIENASDQHQPEEMNAEDPLfILYTSGSTGKPKGV 274
Cdd:PRK05852 160 -----AATEPTPATSTPEGLRPDDAM-IMFTGGTTGLPKMV 194
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
108-274 |
9.61e-06 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 46.81 E-value: 9.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 108 ISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGaiHSVIfggfsPEAV---AGRIVD----SNS 180
Cdd:PRK04813 28 LTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAG--HAYI-----PVDVsspAERIEMiievAKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 181 KLVITADEgvragrgIPLkknvdEALKNPnVKSINNVivlkrtggkidwhegRDLWWSDLIENASDQhqpeeMNAEDPLF 260
Cdd:PRK04813 101 SLIIATEE-------LPL-----EILGIP-VITLDEL---------------KDIFATGNPYDFDHA-----VKGDDNYY 147
|
170
....*....|....
gi 823296640 261 ILYTSGSTGKPKGV 274
Cdd:PRK04813 148 IIFTSGTTGKPKGV 161
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
82-272 |
1.02e-05 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 46.91 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 82 LDRHLAerGNETAIIwegddaSQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIhsV 161
Cdd:PRK10946 31 LTRHAA--SDAIAVI------CGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--P 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 162 IFGGFSPE-----AVAGRIvdsNSKLVItadegvrAGRGIPLKKNVD--EALKNpNVKSINNVIVLKRTGgkidwheGRD 234
Cdd:PRK10946 101 VNALFSHQrselnAYASQI---EPALLI-------ADRQHALFSDDDflNTLVA-EHSSLRVVLLLNDDG-------EHS 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 823296640 235 LwwSDLIENASDQHQPEEMNAEDPLFILYTSGSTGKPK 272
Cdd:PRK10946 163 L--DDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPK 198
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
91-275 |
1.14e-05 |
|
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: 46.78 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 91 NETAIIWEGddasQSkhISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEA 170
Cdd:cd17645 13 DHVAVVDRG----QS--LTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 171 VAGRIVDSNSKLVITadegvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdlienasdqhqp 250
Cdd:cd17645 87 IAYMLADSSAKILLT----------------------------------------------------------------- 101
|
170 180
....*....|....*....|....*
gi 823296640 251 eemNAEDPLFILYTSGSTGKPKGVL 275
Cdd:cd17645 102 ---NPDDLAYVIYTSGSTGLPKGVM 123
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
108-300 |
1.22e-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: 46.56 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 108 ISYKELhrdvcRFANVLLAQGIKK----GDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLV 183
Cdd:cd05909 8 LTYRKL-----LTGAIALARKLAKmtkeGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 184 ITADEGVRAGrGIPLKKNVDEALKnpnvksinnVIVLKRTGGKIDWHEG---------RDLWWSDLIENASDQhqpeemn 254
Cdd:cd05909 83 LTSKQFIEKL-KLHHLFDVEYDAR---------IVYLEDLRAKISKADKckaflagkfPPKWLLRIFGVAPVQ------- 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 823296640 255 AEDPLFILYTSGSTGKPKGVLHTTGGYL--VYAATTfkyVFDYHPGDI 300
Cdd:cd05909 146 PDDPAVILFTSGSEGLPKGVVLSHKNLLanVEQITA---IFDPNPEDV 190
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
91-282 |
1.30e-05 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 46.55 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 91 NETAIIWegddasQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEA 170
Cdd:PLN03102 29 NRTSIIY------GKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 171 VAGRIVDSNSKLVITADEGVRAGRGIPLKKNVDEALKNPNVKSINNVIVLKRTGGKidwhegrDLWWSDLIENAsdQHQP 250
Cdd:PLN03102 103 IAAILRHAKPKILFVDRSFEPLAREVLHLLSSEDSNLNLPVIFIHEIDFPKRPSSE-------ELDYECLIQRG--EPTP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 823296640 251 EEM-------NAEDPLFILYTSGSTGKPKGVLHT-TGGYL 282
Cdd:PLN03102 174 SLVarmfriqDEHDPISLNYTSGTTADPKGVVIShRGAYL 213
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
106-277 |
1.69e-05 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 46.41 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 106 KHISYKELHRDVCRFANVLLAQ-GIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVI 184
Cdd:PRK08751 49 KTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 185 TAD------EGVRAGrgIPLKKNV-----------DEALKNPNVKSINNVIVLKRTGGKIDWHEGrdlwwsdLIENASDQ 247
Cdd:PRK08751 129 VIDnfgttvQQVIAD--TPVKQVIttglgdmlgfpKAALVNFVVKYVKKLVPEYRINGAIRFREA-------LALGRKHS 199
|
170 180 190
....*....|....*....|....*....|
gi 823296640 248 HQPEEMNAEDPLFILYTSGSTGKPKGVLHT 277
Cdd:PRK08751 200 MPTLQIEPDDIAFLQYTGGTTGVAKGAMLT 229
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
101-277 |
2.09e-05 |
|
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: 45.98 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 101 DASQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNS 180
Cdd:cd17642 38 DAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 181 KLVITADEGvragrgipLKKNVDEALKNPNVKSInnvIVLKrtgGKIDWHEGRDLwwsdliENASDQHQPEEMNA----- 255
Cdd:cd17642 118 TIVFCSKKG--------LQKVLNVQKKLKIIKTI---IILD---SKEDYKGYQCL------YTFITQNLPPGFNEydfkp 177
|
170 180
....*....|....*....|....*...
gi 823296640 256 ------EDPLFILYTSGSTGKPKGVLHT 277
Cdd:cd17642 178 psfdrdEQVALIMNSSGSTGLPKGVQLT 205
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
121-300 |
2.09e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 46.11 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 121 ANVL---LAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIfgGFSpeAVAGRIVDS----NSKLVITADEGVRAG 193
Cdd:PRK06814 668 AFVLgrkLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMI--NFS--AGIANILSAckaaQVKTVLTSRAFIEKA 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 194 RGIPLKKNVDEALKnpnvksinnVIVLK------RTGGKIDwhegrdlwwsDLIENASDQHQPEEMNAEDPLFILYTSGS 267
Cdd:PRK06814 744 RLGPLIEALEFGIR---------IIYLEdvraqiGLADKIK----------GLLAGRFPLVYFCNRDPDDPAVILFTSGS 804
|
170 180 190
....*....|....*....|....*....|...
gi 823296640 268 TGKPKGVLHTTGGYLVYAATTFKYVfDYHPGDI 300
Cdd:PRK06814 805 EGTPKGVVLSHRNLLANRAQVAARI-DFSPEDK 836
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
109-281 |
2.11e-05 |
|
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: 45.92 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 109 SYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITAde 188
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVG-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 189 gvragrgiplKKNVDEALKNPNVKSINNVIVLKRTGGKIDWHegrdlwWSDLIEnasdQHQPEE----MNAEDPLFILYT 264
Cdd:cd05932 86 ----------KLDDWKAMAPGVPEGLISISLPPPSAANCQYQ------WDDLIA----QHPPLEerptRFPEQLATLIYT 145
|
170
....*....|....*..
gi 823296640 265 SGSTGKPKGVLHTTGGY 281
Cdd:cd05932 146 SGTTGQPKGVMLTFGSF 162
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
108-293 |
2.79e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 45.60 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 108 ISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLVITAD 187
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 188 EGVRAGRGIpLKKNvdealkNPNVKSINNVIVLKRTGGKIDWHEGRDLW-WSDLIENASDQHQPEEMNAEDPLFILYTSG 266
Cdd:PLN02861 158 SKISSILSC-LPKC------SSNLKTIVSFGDVSSEQKEEAEELGVSCFsWEEFSLMGSLDCELPPKQKTDICTIMYTSG 230
|
170 180
....*....|....*....|....*..
gi 823296640 267 STGKPKGVLHTTGGYLVYAATTFKYVF 293
Cdd:PLN02861 231 TTGEPKGVILTNRAIIAEVLSTDHLLK 257
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
237-303 |
3.45e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 45.40 E-value: 3.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 823296640 237 WSDLIENASDQHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTGGYLVYA-ATTFKYvfDYHPGDIYWC 303
Cdd:PRK13388 131 YAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGrALTERF--GLTRDDVCYV 196
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
233-282 |
4.09e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.54 E-value: 4.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 823296640 233 RDLWWSDLIENASDQHQPEEMNAEDPL-FILYTSGSTGKPKGVLHTTGGYL 282
Cdd:PRK05691 3845 RLLVWEEVQAGEVASHNPGIYSGPDNLaYVIYTSGSTGLPKGVMVEQRGML 3895
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
82-279 |
4.83e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.16 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 82 LDRHLAERGNETAIIWEGDDasqskhISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSV 161
Cdd:PRK05691 1137 LNEQARQTPERIALVWDGGS------LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVP 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 162 IFGGFSPEAVAGRIVDSNSKLVITadegvragrgiplKKNVDEALKNPNVKSINNVIVLKrtggkidwhegrdlwwsdlI 241
Cdd:PRK05691 1211 LDPDYPAERLAYMLADSGVELLLT-------------QSHLLERLPQAEGVSAIALDSLH-------------------L 1258
|
170 180 190
....*....|....*....|....*....|....*...
gi 823296640 242 ENASDQHQPEEMNAEDPLFILYTSGSTGKPKGVLHTTG 279
Cdd:PRK05691 1259 DSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHA 1296
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
84-286 |
6.32e-05 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 44.48 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 84 RHLAE-RGNETAIIwegddaSQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAihsvi 162
Cdd:PRK09029 10 RHWAQvRPQAIALR------LNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGA----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 163 fggfspeavagRIVDSNSKLvitadegvragrgiPlkknvdEALKNPNVKSINNVIVLKRTGgkidwhegrDLWWSDLie 242
Cdd:PRK09029 79 -----------RVLPLNPQL--------------P------QPLLEELLPSLTLDFALVLEG---------ENTFSAL-- 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 823296640 243 nasDQHQPEEMNAEDPLF--------ILYTSGSTGKPKGVLHTTGGYLVYAA 286
Cdd:PRK09029 117 ---TSLHLQLVEGAHAVAwqpqrlatMTLTSGSTGLPKAAVHTAQAHLASAE 165
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
248-275 |
8.49e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 43.83 E-value: 8.49e-05
10 20
....*....|....*....|....*...
gi 823296640 248 HQPEEMNAEDPLFILYTSGSTGKPKGVL 275
Cdd:PRK07787 120 HRYPEPDPDAPALIVYTSGTTGPPKGVV 147
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
108-279 |
1.29e-04 |
|
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: 43.10 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 108 ISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVAGRIVDSNSKLvitad 187
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 188 egvragrgiplkknvdealknpnvksinnvivlkrtggkidwhegrdlwwsdlienasdqhqpeemnaEDPLFILYTSGS 267
Cdd:cd05912 77 --------------------------------------------------------------------DDIATIMYTSGT 88
|
170
....*....|..
gi 823296640 268 TGKPKGVLHTTG 279
Cdd:cd05912 89 TGKPKGVQQTFG 100
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
103-193 |
1.86e-04 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 42.89 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 103 SQSKHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPE------------- 169
Cdd:cd17647 16 SKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPArqniylgvakprg 95
|
90 100 110
....*....|....*....|....*....|.
gi 823296640 170 ----AVAGRIV--DSNSKLVITA-DEGVRAG 193
Cdd:cd17647 96 liviRAAGVVVgpDSNPTLSFTSgSEGIPKG 126
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
78-286 |
2.09e-04 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 42.82 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 78 AANCLDRhlaergneTAIIwegDDASQskhISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGA 157
Cdd:PRK13382 53 AQRCPDR--------PGLI---DELGT---LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 158 iHSVIFG-GFSPEAVAGRIVDSNSKLVITADEGvragrgIPLkknVDEALKN-PNVKSInnvivlkrtggkIDWHEGRDL 235
Cdd:PRK13382 119 -DILLLNtSFAGPALAEVVTREGVDTVIYDEEF------SAT---VDRALADcPQATRI------------VAWTDEDHD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 823296640 236 WWSDLIENASDQHQPEEMNAEDPLfILYTSGSTGKPKGVLHT-TGGYLVYAA 286
Cdd:PRK13382 177 LTVEVLIAAHAGQRPEPTGRKGRV-ILLTSGTTGTPKGARRSgPGGIGTLKA 227
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
106-156 |
2.19e-04 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 42.70 E-value: 2.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 823296640 106 KHISYKELHRDVCRFANVLLAQGIKKGDVVAIYMPMVPEAAVAMLACARIG 156
Cdd:PRK07059 47 KAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAG 97
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
249-317 |
4.13e-04 |
|
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: 41.65 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 249 QPEEMnaedpLFILYTSGSTGKPKGVL--------HTTGGYLVYAATTFKYV-------FDYHPGDIYwctadVGWVTGH 313
Cdd:cd17644 104 QPENL-----AYVIYTSGSTGKPKGVMiehqslvnLSHGLIKEYGITSSDRVlqfasiaFDVAAEEIY-----VTLLSGA 173
|
....
gi 823296640 314 SYLL 317
Cdd:cd17644 174 TLVL 177
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
124-301 |
4.52e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 41.62 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 124 LLAQGIKKGDVVAIYMPMVPEAAVAMLACARIGAIHSVIFGGFSPEAVagrivdsnsKLVITADEgVRAGRGIPLKKNVD 203
Cdd:PLN02736 95 LVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAV---------KFIVNHAE-VAAIFCVPQTLNTL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823296640 204 EALKN--PNVKSInnVIVL----------KRTGGKIdwhegrdLWWSDLI-ENASDQHQPEEMNAEDPLFILYTSGSTGK 270
Cdd:PLN02736 165 LSCLSeiPSVRLI--VVVGgadeplpslpSGTGVEI-------VTYSKLLaQGRSSPQPFRPPKPEDVATICYTSGTTGT 235
|
170 180 190
....*....|....*....|....*....|.
gi 823296640 271 PKGVLHTTGGyLVYAATTFKYVFDYHPGDIY 301
Cdd:PLN02736 236 PKGVVLTHGN-LIANVAGSSLSTKFYPSDVH 265
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
255-279 |
9.34e-04 |
|
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: 40.52 E-value: 9.34e-04
10 20
....*....|....*....|....*
gi 823296640 255 AEDPLFILYTSGSTGKPKGVLHTTG 279
Cdd:cd05910 84 ADEPAAILFTSGSTGTPKGVVYRHG 108
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
256-275 |
2.14e-03 |
|
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: 39.29 E-value: 2.14e-03
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
257-277 |
5.68e-03 |
|
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: 38.08 E-value: 5.68e-03
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
255-277 |
9.11e-03 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 37.77 E-value: 9.11e-03
|
| |
