|
Name |
Accession |
Description |
Interval |
E-value |
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
12-245 |
1.01e-97 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440637 [Multi-domain] Cd Length: 262 Bit Score: 286.27 E-value: 1.01e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 12 VYKKPALMNDTTMHYCPGCSHGVVHKLVAEVIEEMGMSDKAVGVCPVGCAVFAYRYLDIDWQEAPHGRAPAVATGIKRLW 91
Cdd:COG1013 1 VLKKKDLLRTPGHRWCPGCGHGIILRLLLKALDELLDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 92 PDRLVFTYQGDGDLACIGTAETIHALNRGENIPIIFINNAIYGMTGGQMAPTTLIGQKTATCPYGrDPElhgYNLNITEL 171
Cdd:COG1013 81 PDLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYG-KPE---PPKDPAEI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2028863651 172 A-SHlkGTCFVTRQsvdSVASINKAKRAIRKAFEasmqGKGSSLVEIVSTCNSGWKLTPVKANEWMRENMFPEYE 245
Cdd:COG1013 157 AaAH--GATYVARA---SVGDPKDLKKKIKKAIE----HKGFSFIEVLSPCPTGWGRDPSKTIEWAKEGMWPLYE 222
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
26-223 |
2.38e-79 |
|
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity.
Pssm-ID: 239470 [Multi-domain] Cd Length: 193 Bit Score: 237.04 E-value: 2.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 26 YCPGCSHGVVHKLVAEVIEEMGMS-DKAVGVCPVGCAVFAYRYLDIDWQEAPHGRAPAVATGIKRLWPDRLVFTYQGDGD 104
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDpEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 105 LACIGTAETIHALNRGENIPIIFINNAIYGMTGGQMAPTTLIGQKTATCPYGRDPElhgyNLNITELASHLkGTCFVTRQ 184
Cdd:cd03375 81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEE----PFNPLALALAA-GATFVARG 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 2028863651 185 svdSVASINKAKRAIRKAFeasmQGKGSSLVEIVSTCNS 223
Cdd:cd03375 156 ---FSGDIKQLKEIIKKAI----QHKGFSFVEVLSPCPT 187
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
20-239 |
7.94e-42 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 144.21 E-value: 7.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 20 NDTTMHYCPGCSHGVVHKLVAEVIEEMGMS-DKAVGVCPVGCAV-FAYrYLDIDWQEAPHGRAPAVATGIKRLWPDRLVF 97
Cdd:PRK11867 13 NDQEPRWCPGCGDGSILAALQRALAELGLDpENVAVVSGIGCSGrLPG-YINTYGFHTIHGRALAIATGLKLANPDLTVI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 98 TYQGDGDLACIGTAETIHALNRGENIPIIFINNAIYGMTGGQMAPTTLIGQKTATCPYGrDPElhgYNLNITELASHLKG 177
Cdd:PRK11867 92 VVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYG-SIE---PPFNPVELALGAGA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2028863651 178 TcFVTRqSVDSvaSINKAKRAIRKAFeasmQGKGSSLVEIVSTCNSgwkLTPVKANEWMREN 239
Cdd:PRK11867 168 T-FVAR-GFDS--DVKQLTELIKAAI----NHKGFSFVEILQPCPT---FNNVNTFDWFKER 218
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
75-217 |
3.18e-20 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 84.17 E-value: 3.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 75 APHGRAPAVATGIKRLWPDRLVFTYQGDGDLACIGTaETIHALNRGENIPIIFINNAIYGMTGGQmapTTLIGQKTATCP 154
Cdd:pfam02775 28 GTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQ-ELATAVRYNLPITVVVLNNGGYGMTRGQ---QTPFGGGRYSGP 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2028863651 155 YGRDpelhGYNLNITELASHLKGTcfvtrqsvdsVASINKAKRaIRKAFEASMQGKGSSLVEI 217
Cdd:pfam02775 104 SGKI----LPPVDFAKLAEAYGAK----------GARVESPEE-LEEALKEALEHDGPALIDV 151
|
|
| Ppyr-DeCO2ase |
TIGR03297 |
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an ... |
78-181 |
6.74e-04 |
|
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an decarboxylase enzyme that produces phosphonoacetaldehyde (Pald), the second step in the biosynthesis phosphonate-containing compounds. Since the preceding enzymate step, PEP phosphomutase (AepX, TIGR02320) favors the substrate PEP energetically, the decarboxylase is required to drive the reaction in the direction of phosphonate production. Pald is a precursor of natural products including antibiotics like bialaphos and phosphonothricin in Streptomyces species, phosphonate-modified molecules such as the polysaccharide B of Bacteroides fragilis, the phosphonolipids of Tetrahymena pyroformis, the glycosylinositolphospholipids of Trypanosoma cruzi. This gene generally occurs in prokaryotic organisms adjacent to the gene for AepX. Most often an aminotansferase (aepZ) is also present which leads to the production of the most common phosphonate compound, 2-aminoethylphosphonate (AEP).
Pssm-ID: 274508 [Multi-domain] Cd Length: 361 Bit Score: 40.42 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 78 GRAPAVATGIKRLWPDRLVFTYQGDGD-LACIGTAETIhALNRGENIPIIFINNAIYGMTGGQ--MAPTTLIGQKTATCP 154
Cdd:TIGR03297 224 GHASQIALGLALARPDQRVVCLDGDGAaLMHMGGLATI-GTQGPANLIHVLFNNGAHDSVGGQptVSQHLDFAQIAKACG 302
|
90 100 110
....*....|....*....|....*....|.
gi 2028863651 155 YGRdpELHGYNLNITE----LASHLKGTCFV 181
Cdd:TIGR03297 303 YAK--VYEVSTLEELEtaltAASSANGPRLI 331
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
12-245 |
1.01e-97 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440637 [Multi-domain] Cd Length: 262 Bit Score: 286.27 E-value: 1.01e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 12 VYKKPALMNDTTMHYCPGCSHGVVHKLVAEVIEEMGMSDKAVGVCPVGCAVFAYRYLDIDWQEAPHGRAPAVATGIKRLW 91
Cdd:COG1013 1 VLKKKDLLRTPGHRWCPGCGHGIILRLLLKALDELLDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 92 PDRLVFTYQGDGDLACIGTAETIHALNRGENIPIIFINNAIYGMTGGQMAPTTLIGQKTATCPYGrDPElhgYNLNITEL 171
Cdd:COG1013 81 PDLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYG-KPE---PPKDPAEI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2028863651 172 A-SHlkGTCFVTRQsvdSVASINKAKRAIRKAFEasmqGKGSSLVEIVSTCNSGWKLTPVKANEWMRENMFPEYE 245
Cdd:COG1013 157 AaAH--GATYVARA---SVGDPKDLKKKIKKAIE----HKGFSFIEVLSPCPTGWGRDPSKTIEWAKEGMWPLYE 222
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
26-223 |
2.38e-79 |
|
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) subfamily, TPP-binding module; OGFOR catalyzes the oxidative decarboxylation of 2-oxo-acids, with ferredoxin acting as an electron acceptor. In the TCA cycle, OGFOR catalyzes the oxidative decarboxylation of 2-oxoglutarate to succinyl-CoA. In the reductive tricarboxylic acid cycle found in the anaerobic autotroph Hydrogenobacter thermophilus, OGFOR catalyzes the reductive carboxylation of succinyl-CoA to produce 2-oxoglutarate. Thauera aromatica OGFOR has been shown to provide reduced ferredoxin to benzoyl-CoA reductase, a key enzyme in the anaerobic metabolism of aromatic compounds. OGFOR is dependent on TPP and a divalent metal cation for activity.
Pssm-ID: 239470 [Multi-domain] Cd Length: 193 Bit Score: 237.04 E-value: 2.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 26 YCPGCSHGVVHKLVAEVIEEMGMS-DKAVGVCPVGCAVFAYRYLDIDWQEAPHGRAPAVATGIKRLWPDRLVFTYQGDGD 104
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDpEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 105 LACIGTAETIHALNRGENIPIIFINNAIYGMTGGQMAPTTLIGQKTATCPYGRDPElhgyNLNITELASHLkGTCFVTRQ 184
Cdd:cd03375 81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEE----PFNPLALALAA-GATFVARG 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 2028863651 185 svdSVASINKAKRAIRKAFeasmQGKGSSLVEIVSTCNS 223
Cdd:cd03375 156 ---FSGDIKQLKEIIKKAI----QHKGFSFVEVLSPCPT 187
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
20-239 |
7.94e-42 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 144.21 E-value: 7.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 20 NDTTMHYCPGCSHGVVHKLVAEVIEEMGMS-DKAVGVCPVGCAV-FAYrYLDIDWQEAPHGRAPAVATGIKRLWPDRLVF 97
Cdd:PRK11867 13 NDQEPRWCPGCGDGSILAALQRALAELGLDpENVAVVSGIGCSGrLPG-YINTYGFHTIHGRALAIATGLKLANPDLTVI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 98 TYQGDGDLACIGTAETIHALNRGENIPIIFINNAIYGMTGGQMAPTTLIGQKTATCPYGrDPElhgYNLNITELASHLKG 177
Cdd:PRK11867 92 VVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYG-SIE---PPFNPVELALGAGA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2028863651 178 TcFVTRqSVDSvaSINKAKRAIRKAFeasmQGKGSSLVEIVSTCNSgwkLTPVKANEWMREN 239
Cdd:PRK11867 168 T-FVAR-GFDS--DVKQLTELIKAAI----NHKGFSFVEILQPCPT---FNNVNTFDWFKER 218
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
27-239 |
1.03e-39 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 139.24 E-value: 1.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 27 CPGCSHGVVHKLVAEVIEEMGMS-DKAVGVCPVGCAVFAYRYLDIDWQEAPHGRAPAVATGIKRLWPDRLVFTYQGDGDL 105
Cdd:PRK05778 21 CPGCGNFGILNAIIQALAELGLDpDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLANPDLEVIVVGGDGDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 106 ACIGTAETIHALNRGENIPIIFINNAIYGMTGGQMAPTTLIGQKTATCPYGRDPElhgyNLNITELASHLKGTcFVTR-- 183
Cdd:PRK05778 101 ASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEP----PIDPCALALAAGAT-FVARsf 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2028863651 184 -----QSVDSVasinkaKRAIRKafeasmqgKGSSLVEIVSTC-----NSGWKLTPVKANEWMREN 239
Cdd:PRK05778 176 agdvkQLVELI------KKAISH--------KGFAFIDVLSPCvtfngRNTSTKSPAYMREYYKKR 227
|
|
| oorB |
PRK09628 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; |
26-243 |
1.61e-30 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
Pssm-ID: 182003 [Multi-domain] Cd Length: 277 Bit Score: 114.44 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 26 YCPGCSHGVVHKLVAEVIEEMG--MSDKAVgVCPVGCAVFAYRYLDIDWQEAPHGRAPAVATGIKRLWPDRLVFTYQGDG 103
Cdd:PRK09628 18 WCWGCGDGVILKSIIRAIDKLGwnMDDVCV-VSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGIKLANPDKHVIVVSGDG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 104 DLACIGTAETIHALNRGENIPIIFINNAIYGMTGGQMAPTTLIGQKTATCPYGR-DPelhgyNLNITELAShLKGTCFVT 182
Cdd:PRK09628 97 DGLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNiDP-----TFDACKLAT-AAGASFVA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2028863651 183 RQSVdsvasINKAKraIRKAFEASMQGKGSSLVEIVSTC--NSGWK---LTPVKANEWMRENMFPE 243
Cdd:PRK09628 171 RESV-----IDPQK--LEKLLVKGFSHKGFSFFDVFSNChiNLGRKnkmGEAVQMLKWIESRTVSK 229
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
26-251 |
1.25e-27 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 107.15 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 26 YCPGCSHGVVHKLVAEVIEEMGMSDKAVGVCP-VGCAVFAYRYLDIDWQEAPHGRAPAVATGIKRLWPDRLVFTYQGDGD 104
Cdd:PRK11866 9 WCPGCGNYGILEALRKALAELGIPPENVVVVSgIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLTVIGYGGDGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 105 LACIGTAETIHALNRGENIPIIFINNAIYGMTGGQMAPTTLIGQKTATCPYGrDPElHGYNLNITELAShlkGTCFVTRQ 184
Cdd:PRK11866 89 GYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDG-NIE-EPFNPIALALAA---GATFVARG 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2028863651 185 SVDSVASINK-AKRAIRKafeasmqgKGSSLVEIVSTCnsgwkLTPVKAN--EWMRENMFPEYEKG-DLKD 251
Cdd:PRK11866 164 FSGDVKHLKEiIKEAIKH--------KGFSFIDVLSPC-----VTFNKLNtyDWFRPRVYKLEETGhDPTN 221
|
|
| PRK11869 |
PRK11869 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
26-241 |
4.67e-26 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183349 [Multi-domain] Cd Length: 280 Bit Score: 102.94 E-value: 4.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 26 YCPGCSHGVVHKLVAEVIEEMGM-SDKAVGVCPVGCAVFAYRYLDIDWQEAPHGRAPAVATGIKRLWPDRLVFTYQGDGD 104
Cdd:PRK11869 10 WCPGCGNFGIRNALMKALSELNLkPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTVIAEGGDGD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 105 LACIGTAETIHALNRGENIPIIFINNAIYGMTGGQMAPTTLIGQKTATCPYGRDPElhgyNLNITELASHLKGTcFVTRQ 184
Cdd:PRK11869 90 MYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEE----PFNPIALAIALDAS-FVART 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2028863651 185 svdSVASINKAKRAIRKAfeasMQGKGSSLVEIVSTCNSGWKLTPVkanEWMRENMF 241
Cdd:PRK11869 165 ---FSGDIEETKEILKEA----IKHKGLAIVDIFQPCVSFNKVNTY---QWYRENTY 211
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
75-217 |
3.18e-20 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 84.17 E-value: 3.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 75 APHGRAPAVATGIKRLWPDRLVFTYQGDGDLACIGTaETIHALNRGENIPIIFINNAIYGMTGGQmapTTLIGQKTATCP 154
Cdd:pfam02775 28 GTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQ-ELATAVRYNLPITVVVLNNGGYGMTRGQ---QTPFGGGRYSGP 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2028863651 155 YGRDpelhGYNLNITELASHLKGTcfvtrqsvdsVASINKAKRaIRKAFEASMQGKGSSLVEI 217
Cdd:pfam02775 104 SGKI----LPPVDFAKLAEAYGAK----------GARVESPEE-LEEALKEALEHDGPALIDV 151
|
|
| TPP_PFOR |
cd02018 |
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ... |
27-245 |
1.03e-16 |
|
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) subfamily, TPP-binding module; PFOR catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. PFORs can be homodimeric, heterodimeric, or heterotetrameric, depending on the organism. These enzymes are dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238976 [Multi-domain] Cd Length: 237 Bit Score: 76.76 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 27 CPGCSHGVVhklVAEVIEEMGMSDKAVGVCPVGC-----AVFAYRYLDIDWQEAPHGRAPAVATGIKRLWPDRL------ 95
Cdd:cd02018 8 CAGCGEVTA---VRVVLAALPAPEDTVIANSTGCssvyaSTAPFNSWAVPWVNSLFEDANAVASGLKRGLKARFpkdrel 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 96 -----VFTYQGDGDLACIGTAETIHALNRGENIPIIFINNAIYGMTGGQMAPTTLIGQKTATCPYGRdpelHGYNLNITE 170
Cdd:cd02018 85 dkkkdVVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGK----KEDKKDLVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2028863651 171 LAShLKGTCFVTRQSVDSVASINKAKRAIRKAFEasmqgkGSSLVEIVSTCNSGWKLTPVKANEWMR----ENMFPEYE 245
Cdd:cd02018 161 IAA-THGCVYVARLSPALKKHFLKVVKEAISRTD------GPTFIHAYTPCITEWGIGSGKSLELARkavkSRMFPLFE 232
|
|
| PRK11865 |
PRK11865 |
pyruvate synthase subunit beta; |
27-250 |
1.90e-15 |
|
pyruvate synthase subunit beta;
Pssm-ID: 183346 [Multi-domain] Cd Length: 299 Bit Score: 73.98 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 27 CPGCSHGVVHKLVAevieeMGMSDKAVGVCPVGC-----AVFAYRYLDIDWQEAPHGRAPAVATGIKRLWP----DRLVF 97
Cdd:PRK11865 21 CAGCGAAIAMRLAL-----KALGKNTVIVVATGClevitTPYPETAWNVPWIHVAFENAAAVASGIERAVKalgkKVNVV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 98 TYQGDGDLACIGTAETIHALNRGENIPIIFINNAIYGMTGGQMAPTTLIGQKTATCPYGRdpELHGYNLNITEL----AS 173
Cdd:PRK11865 96 AIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGK--YSRGEDRPKKNMplimAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 174 HlkGTCFVTRQSVDSVAS-INKAKRAirkafeasMQGKGSSLVEIVSTCNSGWKLTPVKANEWMR----ENMFP--EYEK 246
Cdd:PRK11865 174 H--GIPYVATASIGYPEDfMEKVKKA--------KEVEGPAYIQVLQPCPTGWGFPPEKTIEIGRlaveTGYWPlfEIEN 243
|
....
gi 2028863651 247 GDLK 250
Cdd:PRK11865 244 GKFK 247
|
|
| TPP_PFOR_porB_like |
cd03376 |
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ... |
27-249 |
3.60e-14 |
|
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of proteins similar to the beta subunit (porB) of the Helicobacter pylori four-subunit pyruvate ferredoxin oxidoreductase (PFOR), which are also found in archaea and some hyperthermophilic bacteria. PFOR catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. The 36-kDa porB subunit contains the binding sites for the cofactors, TPP and a divalent metal cation, which are required for activity.
Pssm-ID: 239471 [Multi-domain] Cd Length: 235 Bit Score: 69.57 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 27 CPGCSHGVVHKLVAEVIEEmgmsdKAVGVCPVGCA-----VFAYRYLDIDWQEAPHGRAPAVATGIKRLWP------DRL 95
Cdd:cd03376 8 CAGCGAALALRHVLKALGP-----DTVVVNPTGCLevittPYPYTAWRVPWIHVAFENAAAVASGIEAALKalgrgkDIT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 96 VFTYQGDGDLACIGTAETIHALNRGENIPIIFINNAIYGMTGGQMAPTTLIGQKTATCPYGRDPEL-HGYNLNITEL-AS 173
Cdd:cd03376 83 VVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTTPVGKVSFGkKQPKKDLPLImAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 174 HlkGTCFVTRQSVDSVA-SINKAKRAirkafeasMQGKGSSLVEIVSTCNSGWKLTPVKANEWMR----ENMFP--EYEK 246
Cdd:cd03376 163 H--NIPYVATASVAYPEdLYKKVKKA--------LSIEGPAYIHILSPCPTGWRFDPSKTIEIARlaveTGFWPlyEYEN 232
|
...
gi 2028863651 247 GDL 249
Cdd:cd03376 233 GKF 235
|
|
| PRK11864 |
PRK11864 |
3-methyl-2-oxobutanoate dehydrogenase subunit beta; |
27-250 |
7.27e-14 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
Pssm-ID: 237005 [Multi-domain] Cd Length: 300 Bit Score: 69.73 E-value: 7.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 27 CPGCSHGVVHKLVAEVIeemgmSDKAVGVCPVGCA-----VFAYRYLDIDWQEAPHGRAPAVATGIKRLWP-----DRLV 96
Cdd:PRK11864 21 CPGCGAPLGLRYLLKAL-----GEKTVLVIPASCStviqgDTPKSPLTVPVLHTAFAATAAVASGIEEALKargekGVIV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 97 FTYQGDGDLACIGTAETIHALNRGENIPIIFINNAIYGMTGGQMAPTTLIGQKTATCPYGRD------PELhgynlnite 170
Cdd:PRK11864 96 VGWAGDGGTADIGFQALSGAAERNHDILYIMYDNEAYMNTGIQRSSSTPYGAWTTTTPGGKRehkkpvPDI--------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 171 LASHlkGTCFVtrqSVDSVASINKAKRAIRKAFEAsmqgKGSSLVEIVSTCNSGWKLTPVKANEWMR----ENMFP--EY 244
Cdd:PRK11864 167 MAAH--KVPYV---ATASIAYPEDFIRKLKKAKEI----RGFKFIHLLAPCPPGWRFDPDKTIEIARlaveTGVWPlfEY 237
|
....*.
gi 2028863651 245 EKGDLK 250
Cdd:PRK11864 238 ENGKFK 243
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
78-143 |
1.46e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 47.52 E-value: 1.46e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2028863651 78 GRAPAVATGIKRLWPDRLVFTYQGDGDLAC-IGTAETIHALNRgENIPIIFINNAIYGMTGGQMAPT 143
Cdd:PRK06163 60 GLAFPIALGVALAQPKRRVIALEGDGSLLMqLGALGTIAALAP-KNLTIIVMDNGVYQITGGQPTLT 125
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
78-218 |
5.40e-06 |
|
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors.
Pssm-ID: 239468 [Multi-domain] Cd Length: 188 Bit Score: 45.77 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 78 GRAPAVATGIKRLWPDRLVFTYQGDGdlACI---GTAETIHALNRGENIPIIFiNNAIYGMTGGQmaPTtligqktatcp 154
Cdd:cd03371 51 GHASQIALGIALARPDRKVVCIDGDG--AALmhmGGLATIGGLAPANLIHIVL-NNGAHDSVGGQ--PT----------- 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2028863651 155 ygrdpelHGYNLNITELASHLkGTCFVTrqsvdSVASINKAKRAIRKAfeasMQGKGSSLVEIV 218
Cdd:cd03371 115 -------VSFDVSLPAIAKAC-GYRAVY-----EVPSLEELVAALAKA----LAADGPAFIEVK 161
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
60-217 |
1.21e-05 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 44.55 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 60 CAVFAYRYLD--------IDWQEAPHGRAPAVATGIKRLWPDRLVFTYQGDGDLA-CIGTAETIhalnRGENIPIIFI-- 128
Cdd:cd00568 23 SAYWAYRYLPlrrgrrflTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMmTGQELATA----VRYGLPVIVVvf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 129 NNAIYGMTGGQMAPTTligqktatcpYGRDPELHGYNLNITELASHLKGTCFVtrqsVDSVAsinkakrAIRKAFEASMQ 208
Cdd:cd00568 99 NNGGYGTIRMHQEAFY----------GGRVSGTDLSNPDFAALAEAYGAKGVR----VEDPE-------DLEAALAEALA 157
|
....*....
gi 2028863651 209 GKGSSLVEI 217
Cdd:cd00568 158 AGGPALIEV 166
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
93-145 |
3.27e-04 |
|
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.
Pssm-ID: 239469 [Multi-domain] Cd Length: 179 Bit Score: 40.35 E-value: 3.27e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2028863651 93 DRLVFTYQGDGD-LACIGTAETIhALNRGENIPIIFINNAIYGMTGGQMAPTTL 145
Cdd:cd03372 59 PRKVIVIDGDGSlLMNLGALATI-AAEKPKNLIIVVLDNGAYGSTGNQPTHAGK 111
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
81-134 |
3.93e-04 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 41.40 E-value: 3.93e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2028863651 81 PAvATGIKRLWPDRLVFTYQGDGDLACIGtAETIHALNRGENIPIIFINNAIYG 134
Cdd:PRK08199 422 PA-AIAAKLLFPERTVVAFAGDGCFLMNG-QELATAVQYGLPIIVIVVNNGMYG 473
|
|
| Ppyr-DeCO2ase |
TIGR03297 |
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an ... |
78-181 |
6.74e-04 |
|
phosphonopyruvate decarboxylase; This family consists of examples of phosphonopyruvate an decarboxylase enzyme that produces phosphonoacetaldehyde (Pald), the second step in the biosynthesis phosphonate-containing compounds. Since the preceding enzymate step, PEP phosphomutase (AepX, TIGR02320) favors the substrate PEP energetically, the decarboxylase is required to drive the reaction in the direction of phosphonate production. Pald is a precursor of natural products including antibiotics like bialaphos and phosphonothricin in Streptomyces species, phosphonate-modified molecules such as the polysaccharide B of Bacteroides fragilis, the phosphonolipids of Tetrahymena pyroformis, the glycosylinositolphospholipids of Trypanosoma cruzi. This gene generally occurs in prokaryotic organisms adjacent to the gene for AepX. Most often an aminotansferase (aepZ) is also present which leads to the production of the most common phosphonate compound, 2-aminoethylphosphonate (AEP).
Pssm-ID: 274508 [Multi-domain] Cd Length: 361 Bit Score: 40.42 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 78 GRAPAVATGIKRLWPDRLVFTYQGDGD-LACIGTAETIhALNRGENIPIIFINNAIYGMTGGQ--MAPTTLIGQKTATCP 154
Cdd:TIGR03297 224 GHASQIALGLALARPDQRVVCLDGDGAaLMHMGGLATI-GTQGPANLIHVLFNNGAHDSVGGQptVSQHLDFAQIAKACG 302
|
90 100 110
....*....|....*....|....*....|.
gi 2028863651 155 YGRdpELHGYNLNITE----LASHLKGTCFV 181
Cdd:TIGR03297 303 YAK--VYEVSTLEELEtaltAASSANGPRLI 331
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
40-135 |
1.76e-03 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439799 [Multi-domain] Cd Length: 548 Bit Score: 39.37 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028863651 40 AEVIEEMG--MSDKAVGVCPVG-CAVFAYRYLDIDWQE---APHGRA------PAvATGIKRLWPDRLVFTYQGDGD--- 104
Cdd:COG0028 366 QRVIAALReaLPDDAIVVTDVGqHQMWAARYLRFRRPRrflTSGGLGtmgyglPA-AIGAKLARPDRPVVAITGDGGfqm 444
|
90 100 110
....*....|....*....|....*....|....
gi 2028863651 105 -LACIGTAetihalnRGENIPIIFI--NNAIYGM 135
Cdd:COG0028 445 nLQELATA-------VRYGLPVKVVvlNNGGLGM 471
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
82-152 |
5.73e-03 |
|
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.
Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 36.87 E-value: 5.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2028863651 82 AVATGIKRLWPDRLVFTYQGDGDLACIGTAETIHALNRGENIPIIFINNAIYGMTGGQMAPTTLIGQKTAT 152
Cdd:cd02008 58 GVAIGMAKASEDKKVVAVIGDSTFFHSGILGLINAVYNKANITVVILDNRTTAMTGGQPHPGTGKTLTEPT 128
|
|
| |
