|
Name |
Accession |
Description |
Interval |
E-value |
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
26-392 |
1.06e-143 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 415.32 E-value: 1.06e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 26 QIARA-QGLAGYAGSLD--DVEAALITSMSALADLPVLRKSELGKAQaadaPFGgFTTKPAQGFSHVFQSPGPIYEP--- 99
Cdd:COG1541 27 TVARAyENSPFYRRKFDeaGVDPDDIKSLEDLAKLPFTTKEDLRDNY----PFG-LFAVPLEEIVRIHASSGTTGKPtvv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 100 --SSTDPDWW--RMGRFLHGMGIGTGDIVHNCFGYHLTPAGMIFESGARAVGATVLPAGTGQTELQVIAARDVGSTAYAG 175
Cdd:COG1541 102 gyTRKDLDRWaeLFARSLRAAGVRPGDRVQNAFGYGLFTGGLGLHYGAERLGATVIPAGGGNTERQLRLMQDFGPTVLVG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 176 TPDYLKIILEKADEMGV---TLKITRAAVGGGALFPSLREWYSAR-GITCLQCYATADLG-NIAYESPSMEGMIVDEG-V 249
Cdd:COG1541 182 TPSYLLYLAEVAEEEGIdprDLSLKKGIFGGEPWSEEMRKEIEERwGIKAYDIYGLTEVGpGVAYECEAQDGLHIWEDhF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 250 IVEIVTPGTGNPVPEGEVGEVVVTTLNPD-YPLIRFATGDLSAVMAGPSPCGRTNMRIKGWMGRADQTTKIKGMFVRPEQ 328
Cdd:COG1541 262 LVEIIDPETGEPVPEGEEGELVVTTLTKEaMPLIRYRTGDLTRLLPEPCPCGRTHPRIGRILGRADDMLIIRGVNVFPSQ 341
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 329 VAQLVSHHSEIS-RARVVATREGEQDVMTVRIE-SETHDAEAYGRSVAELLK----LKGRIEVVAPGSLP 392
Cdd:COG1541 342 IEEVLLRIPEVGpEYQIVVDREGGLDELTVRVElAPGASLEALAEAIAAALKavlgLRAEVELVEPGSLP 411
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
48-403 |
2.96e-88 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 273.73 E-value: 2.96e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 48 ITSMSALADLPVLRKSELgkaqAADAPFGGFTTKPAQG-----FSHVFQSPGPIYEPSStDPDWW--RMGRFLHGMGIGT 120
Cdd:cd05913 47 IKSLDDLRKLPFTTKEDL----RDNYPFGLFAVPREKVvrihaSSGTTGKPTVVGYTKN-DLDVWaeLVARCLDAAGVTP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 121 GDIVHNCFGYHLTPAGMIFESGARAVGATVLPAGTGQTELQVIAARDVGSTAYAGTPDYLKIILEKADEMGV---TLKIT 197
Cdd:cd05913 122 GDRVQNAYGYGLFTGGLGFHYGAERLGALVIPAGGGNTERQLQLIKDFGPTVLCCTPSYALYLAEEAEEEGIdprELSLK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 198 RAAVGGGALFPSLREWYSAR-GITCLQCYATADLG--NIAYESPSMEGM-IVDEGVIVEIVTPGTGNPVPEGEVGEVVVT 273
Cdd:cd05913 202 VGIFGAEPWTEEMRKRIERRlGIKAYDIYGLTEIIgpGVAFECEEKDGLhIWEDHFIPEIIDPETGEPVPPGEVGELVFT 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 274 TLNPDY-PLIRFATGDLSAVMAGPSPCGRTNMRIKGWMGRADQTTKIKGMFVRPEQVAQLVSHHSE-ISRARVVATREGE 351
Cdd:cd05913 282 TLTKEAmPLIRYRTRDITRLLPGPCPCGRTHRRIDRITGRSDDMLIIRGVNVFPSQIEDVLLKIPGlGPHYQLILTRQEH 361
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640636305 352 QDVMTVRIE-SETHDAEAYGRSVAELLK--------LKGRIEVVAPGSLPK---DGLVIEDQRT 403
Cdd:cd05913 362 LDELTIKVEvRPEADDDEKLEALKQRLErhiksvlgVTVEVELVEPGSLPRsegKAKRVIDKRK 425
|
|
| AMP-binding_C_2 |
pfam14535 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
326-392 |
5.07e-06 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 434024 [Multi-domain] Cd Length: 96 Bit Score: 44.77 E-value: 5.07e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640636305 326 PEQVAQLVSHHSEISRA-RVVATREGEQDVMTVRIE------SETHDAEAYGRSVAELLK----LKGRIEVVAPGSLP 392
Cdd:pfam14535 6 PSQIEEVLLEIPGVGPEyQIIVTREGGLDELEVKVEvaegfsDEIKDLEALEKRIAKELKsvlgVSVKVELVEPGTLP 83
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
248-368 |
9.00e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 41.57 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 248 GVIVEIVTPGTGNPVPEGEVGEVVVTTL--------NPDY--PLIR---FATGDLSAVmagpSPCGRTNmrikgWMGRAD 314
Cdd:PRK06178 395 GTEFKICDFETGELLPLGAEGEIVVRTPsllkgywnKPEAtaEALRdgwLHTGDIGKI----DEQGFLH-----YLGRRK 465
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 640636305 315 QTTKIKGMFVRPEQVAQLVSHHSEISRARVVA---TREGEQDVMTVRIESE-THDAEA 368
Cdd:PRK06178 466 EMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGrpdPDKGQVPVAFVQLKPGaDLTAAA 523
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
26-392 |
1.06e-143 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 415.32 E-value: 1.06e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 26 QIARA-QGLAGYAGSLD--DVEAALITSMSALADLPVLRKSELGKAQaadaPFGgFTTKPAQGFSHVFQSPGPIYEP--- 99
Cdd:COG1541 27 TVARAyENSPFYRRKFDeaGVDPDDIKSLEDLAKLPFTTKEDLRDNY----PFG-LFAVPLEEIVRIHASSGTTGKPtvv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 100 --SSTDPDWW--RMGRFLHGMGIGTGDIVHNCFGYHLTPAGMIFESGARAVGATVLPAGTGQTELQVIAARDVGSTAYAG 175
Cdd:COG1541 102 gyTRKDLDRWaeLFARSLRAAGVRPGDRVQNAFGYGLFTGGLGLHYGAERLGATVIPAGGGNTERQLRLMQDFGPTVLVG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 176 TPDYLKIILEKADEMGV---TLKITRAAVGGGALFPSLREWYSAR-GITCLQCYATADLG-NIAYESPSMEGMIVDEG-V 249
Cdd:COG1541 182 TPSYLLYLAEVAEEEGIdprDLSLKKGIFGGEPWSEEMRKEIEERwGIKAYDIYGLTEVGpGVAYECEAQDGLHIWEDhF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 250 IVEIVTPGTGNPVPEGEVGEVVVTTLNPD-YPLIRFATGDLSAVMAGPSPCGRTNMRIKGWMGRADQTTKIKGMFVRPEQ 328
Cdd:COG1541 262 LVEIIDPETGEPVPEGEEGELVVTTLTKEaMPLIRYRTGDLTRLLPEPCPCGRTHPRIGRILGRADDMLIIRGVNVFPSQ 341
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 329 VAQLVSHHSEIS-RARVVATREGEQDVMTVRIE-SETHDAEAYGRSVAELLK----LKGRIEVVAPGSLP 392
Cdd:COG1541 342 IEEVLLRIPEVGpEYQIVVDREGGLDELTVRVElAPGASLEALAEAIAAALKavlgLRAEVELVEPGSLP 411
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
48-403 |
2.96e-88 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 273.73 E-value: 2.96e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 48 ITSMSALADLPVLRKSELgkaqAADAPFGGFTTKPAQG-----FSHVFQSPGPIYEPSStDPDWW--RMGRFLHGMGIGT 120
Cdd:cd05913 47 IKSLDDLRKLPFTTKEDL----RDNYPFGLFAVPREKVvrihaSSGTTGKPTVVGYTKN-DLDVWaeLVARCLDAAGVTP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 121 GDIVHNCFGYHLTPAGMIFESGARAVGATVLPAGTGQTELQVIAARDVGSTAYAGTPDYLKIILEKADEMGV---TLKIT 197
Cdd:cd05913 122 GDRVQNAYGYGLFTGGLGFHYGAERLGALVIPAGGGNTERQLQLIKDFGPTVLCCTPSYALYLAEEAEEEGIdprELSLK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 198 RAAVGGGALFPSLREWYSAR-GITCLQCYATADLG--NIAYESPSMEGM-IVDEGVIVEIVTPGTGNPVPEGEVGEVVVT 273
Cdd:cd05913 202 VGIFGAEPWTEEMRKRIERRlGIKAYDIYGLTEIIgpGVAFECEEKDGLhIWEDHFIPEIIDPETGEPVPPGEVGELVFT 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 274 TLNPDY-PLIRFATGDLSAVMAGPSPCGRTNMRIKGWMGRADQTTKIKGMFVRPEQVAQLVSHHSE-ISRARVVATREGE 351
Cdd:cd05913 282 TLTKEAmPLIRYRTRDITRLLPGPCPCGRTHRRIDRITGRSDDMLIIRGVNVFPSQIEDVLLKIPGlGPHYQLILTRQEH 361
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640636305 352 QDVMTVRIE-SETHDAEAYGRSVAELLK--------LKGRIEVVAPGSLPK---DGLVIEDQRT 403
Cdd:cd05913 362 LDELTIKVEvRPEADDDEKLEALKQRLErhiksvlgVTVEVELVEPGSLPRsegKAKRVIDKRK 425
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
116-393 |
3.43e-11 |
|
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: 63.84 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 116 MGIGTGDIVHNCFG-YHLTPAGMIFesGARAVGATVLPAGTGQTELQVIAARDVGSTAYAGTPDYLKIILEKADEMGVTL 194
Cdd:cd04433 36 GGLTEGDVFLSTLPlFHIGGLFGLL--GALLAGGTVVLLPKFDPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 195 -KITRAAVGGGALFPSLREWYSAR-GITCLQCY-ATADLGNIAYESPSME-------GMIVdEGVIVEIVTPGTGnPVPE 264
Cdd:cd04433 114 sSLRALVSGGAPLPPELLERFEEApGIKLVNGYgLTETGGTVATGPPDDDarkpgsvGRPV-PGVEVRIVDPDGG-ELPP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 265 GEVGEVVVTTLNPD--YPLIR-----------FATGDLsavmagpspcGRtnMRIKGWM---GRADQTTKIKGMFVRPEQ 328
Cdd:cd04433 192 GEIGELVVRGPSVMkgYWNNPeataavdedgwYRTGDL----------GR--LDEDGYLyivGRLKDMIKSGGENVYPAE 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640636305 329 VAQLVSHHSEISRARVVA---TREGEQDVMTV-RIESETHDAE---AYGRSVAELLKLKGRIEVVAPgsLPK 393
Cdd:cd04433 260 VEAVLLGHPGVAEAAVVGvpdPEWGERVVAVVvLRPGADLDAEelrAHVRERLAPYKVPRRVVFVDA--LPR 329
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
106-393 |
1.59e-06 |
|
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: 49.81 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 106 WWRMGRFLHGMGIGTGDIV-------HnCFGYHLTPAGMIFeSGARAVgatVLPAGTGQTELQVIAARDVgsTAYAGTPD 178
Cdd:COG0318 126 LANAAAIAAALGLTPGDVVlvalplfH-VFGLTVGLLAPLL-AGATLV---LLPRFDPERVLELIERERV--TVLFGVPT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 179 YLKIILEKADEMGVTLKITRAAVGGGALFPS--LREWYSARGITCLQCY--------ATADLGNIAYESPSMEGMIVDeG 248
Cdd:COG0318 199 MLARLLRHPEFARYDLSSLRLVVSGGAPLPPelLERFEERFGVRIVEGYgltetspvVTVNPEDPGERRPGSVGRPLP-G 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 249 VIVEIVTPgTGNPVPEGEVGEVVV-----------------TTLNPDYplirFATGDLsAVMAgpsPCGRtnMRIKgwmG 311
Cdd:COG0318 278 VEVRIVDE-DGRELPPGEVGEIVVrgpnvmkgywndpeataEAFRDGW----LRTGDL-GRLD---EDGY--LYIV---G 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 312 RADQTTKIKGMFVRPEQVAQLVSHHSEISRARVVAT---REGEQDV-MTVRIESETHDAEAYGRSVAELL---KLKGRIE 384
Cdd:COG0318 344 RKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVpdeKWGERVVaFVVLRPGAELDAEELRAFLRERLaryKVPRRVE 423
|
....*....
gi 640636305 385 VVapGSLPK 393
Cdd:COG0318 424 FV--DELPR 430
|
|
| AMP-binding_C_2 |
pfam14535 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
326-392 |
5.07e-06 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 434024 [Multi-domain] Cd Length: 96 Bit Score: 44.77 E-value: 5.07e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640636305 326 PEQVAQLVSHHSEISRA-RVVATREGEQDVMTVRIE------SETHDAEAYGRSVAELLK----LKGRIEVVAPGSLP 392
Cdd:pfam14535 6 PSQIEEVLLEIPGVGPEyQIIVTREGGLDELEVKVEvaegfsDEIKDLEALEKRIAKELKsvlgVSVKVELVEPGTLP 83
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
122-272 |
9.05e-06 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 47.69 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 122 DIVHnCFGYHLTPAGMIFeSGARAVGATVLPAGTGQTELQVIAARDVgsTAYAGTPDYLKIILEKADEMGVTLK-ITRAA 200
Cdd:pfam00501 208 PLFH-DFGLSLGLLGPLL-AGATVVLPPGFPALDPAALLELIERYKV--TVLYGVPTLLNMLLEAGAPKRALLSsLRLVL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 201 VGGGALFPSLREWYSAR-GITCLQCY---------ATADLGNIAYESPSMEGMIVdEGVIVEIVTPGTGNPVPEGEVGEV 270
Cdd:pfam00501 284 SGGAPLPPELARRFRELfGGALVNGYgltettgvvTTPLPLDEDLRSLGSVGRPL-PGTEVKIVDDETGEPVPPGEPGEL 362
|
..
gi 640636305 271 VV 272
Cdd:pfam00501 363 CV 364
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
259-350 |
1.33e-04 |
|
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: 43.99 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 259 GNPVPEGEVGEVVVTTL--------NPDYPLIRFA-----TGDLSAVMAgpspcgrtnmriKGWM---GRADQTTKIKGM 322
Cdd:cd05919 278 GHTIPPGEEGDLLVRGPsaavgywnNPEKSRATFNggwyrTGDKFCRDA------------DGWYthaGRADDMLKVGGQ 345
|
90 100
....*....|....*....|....*...
gi 640636305 323 FVRPEQVAQLVSHHSEISRARVVATREG 350
Cdd:cd05919 346 WVSPVEVESLIIQHPAVAEAAVVAVPES 373
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
147-353 |
3.74e-04 |
|
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: 42.51 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 147 GATVLPAGTGQTE-----LQVIAARDVgsTAYAGTPDYLKIILEKADEMGVTlKITRAAVGGGALFPSL-REWYSARGIT 220
Cdd:cd05930 159 GATLVVLPEEVRKdpealADLLAEEGI--TVLHLTPSLLRLLLQELELAALP-SLRLVLVGGEALPPDLvRRWRELLPGA 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 221 CL-QCY--------ATA---DLGNIAYESPS-------MEGMIVDEGviveivtpgtGNPVPEGEVGEVVVT-------- 273
Cdd:cd05930 236 RLvNLYgpteatvdATYyrvPPDDEEDGRVPigrpipnTRVYVLDEN----------LRPVPPGVPGELYIGgaglargy 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 274 -----------TLNPDYPLIR-FATGDLsavmagpspcGRtnmrikgW--------MGRADQTTKIKGMFVRPEQVAQLV 333
Cdd:cd05930 306 lnrpeltaerfVPNPFGPGERmYRTGDL----------VR-------WlpdgnlefLGRIDDQVKIRGYRIELGEIEAAL 368
|
250 260
....*....|....*....|
gi 640636305 334 SHHSEISRARVVATREGEQD 353
Cdd:cd05930 369 LAHPGVREAAVVAREDGDGE 388
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
248-368 |
9.00e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 41.57 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 248 GVIVEIVTPGTGNPVPEGEVGEVVVTTL--------NPDY--PLIR---FATGDLSAVmagpSPCGRTNmrikgWMGRAD 314
Cdd:PRK06178 395 GTEFKICDFETGELLPLGAEGEIVVRTPsllkgywnKPEAtaEALRdgwLHTGDIGKI----DEQGFLH-----YLGRRK 465
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 640636305 315 QTTKIKGMFVRPEQVAQLVSHHSEISRARVVA---TREGEQDVMTVRIESE-THDAEA 368
Cdd:PRK06178 466 EMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGrpdPDKGQVPVAFVQLKPGaDLTAAA 523
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
171-272 |
1.72e-03 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 40.57 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 171 TAYAGTPDYLKIILEKADEMGVTLKITR-AAVGGGALFPSLREWYSAR--GITCLQCYATADLGNI----AYESPSME-- 241
Cdd:PRK06334 275 TFLGSTPVFFDYILKTAKKQESCLPSLRfVVIGGDAFKDSLYQEALKTfpHIQLRQGYGTTECSPVitinTVNSPKHEsc 354
|
90 100 110
....*....|....*....|....*....|..
gi 640636305 242 -GMIVdEGVIVEIVTPGTGNPVPEGEVGEVVV 272
Cdd:PRK06334 355 vGMPI-RGMDVLIVSEETKVPVSSGETGLVLT 385
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
130-272 |
4.10e-03 |
|
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: 39.13 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 130 YHLTPAGMIFESGArAVGATV--LPAGTGQTELQVIAARDVgsTAYAGTPDYLKIILEKADEMGVTLKITRAAVGGGALF 207
Cdd:cd17631 149 FHIGGLGVFTLPTL-LRGGTVviLRKFDPETVLDLIERHRV--TSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPM 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 208 PS-LREWYSARGITCLQCY----------------ATADLGNIAYESPSMEGMIVDEGviveivtpgtGNPVPEGEVGEV 270
Cdd:cd17631 226 PErLLRALQARGVKFVQGYgmtetspgvtflspedHRRKLGSAGRPVFFVEVRIVDPD----------GREVPPGEVGEI 295
|
..
gi 640636305 271 VV 272
Cdd:cd17631 296 VV 297
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
259-377 |
5.94e-03 |
|
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: 38.80 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640636305 259 GNPVPEGEVGEVVVTTL-------------------NPDYPLIR-FATGDLSavmagpspCGRTNMRIKgWMGRADQTTK 318
Cdd:cd17646 326 LRPVPVGVPGELYLGGVqlargylgrpaltaerfvpDPFGPGSRmYRTGDLA--------RWRPDGALE-FLGRSDDQVK 396
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 640636305 319 IKGMFVRPEQVAQLVSHHSEISRARVVATREGEQDV-----MTVRIESETHDAEAYGRSVAELL 377
Cdd:cd17646 397 IRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAArlvgyVVPAAGAAGPDTAALRAHLAERL 460
|
|
| |
