|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11869 |
PRK11869 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
9-286 |
4.02e-165 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183349 [Multi-domain] Cd Length: 280 Bit Score: 459.25 E-value: 4.02e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 9 DLDIAWCPGCGNFGILTLLKKALAELSIEPRQLVIASGIGQAAKTPHYLKSHVFNGLHGRALPAATAIKAGNPQLTVIAQ 88
Cdd:PRK11869 5 KYDIAWCPGCGNFGIRNALMKALSELNLKPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTVIAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 89 GGDGDMYGEGGNHFLHAIRRNPDLTHLVHDNMVYGLTKGQASPTSQPGFVTPLQVDGVCQEPFNPLSVAIALNASFVARI 168
Cdd:PRK11869 85 GGDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASFVART 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 169 YVGAVAHAVTVLKAALRHHGYALVDILQPCVSFNRLNTYEWFEEHCYFLeEGHDPEDRQAAFARACETERLPLGIFYRDS 248
Cdd:PRK11869 165 FSGDIEETKEILKEAIKHKGLAIVDIFQPCVSFNKVNTYQWYRENTYYL-KDHDPTDRELAFKRALETEKLPLGIFYINE 243
|
250 260 270
....*....|....*....|....*....|....*...
gi 1109567921 249 KRkTFEEHLAAYRHDSRPLYQRSPNTGRLHELINDKRL 286
Cdd:PRK11869 244 KP-TFEELVPAYKGDKTPLWKREPNFEKLKELIESKRS 280
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
12-270 |
1.89e-136 |
|
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number of anaerobic and microaerophilic species lack pyruvate dehydrogenase and have instead a four subunit, oxygen-sensitive pyruvate oxidoreductase, with either ferredoxins or flavodoxins used as the acceptor. Several related four-subunit enzymes may exist in the same species. This model describes a subfamily of beta subunits, representing mostly pyruvate and 2-ketoisovalerate specific enzymes.
Pssm-ID: 274015 [Multi-domain] Cd Length: 287 Bit Score: 386.81 E-value: 1.89e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 12 IAWCPGCGNFGILTLLKKALAELSIEPRQLVIASGIGQAAKTPHYLKSHVFNGLHGRALPAATAIKAGNPQLTVIAQGGD 91
Cdd:TIGR02177 1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 92 GDMYGEGGNHFLHAIRRNPDLTHLVHDNMVYGLTKGQASPTSQPGFVTPLQVDGVCQEPFNPLSVAIALNASFVARIYVG 171
Cdd:TIGR02177 81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 172 AVAHAVTVLKAALRHHGYALVDILQPCVSFNRLNTYEWFEEHCYFLEE-GHDPEDRQ---------AAFARACET-ERLP 240
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNKINTYEWYRERVYKLDEeGYDPIVREpeefeekaaAAIKKAMEWgDRIP 240
|
250 260 270
....*....|....*....|....*....|..
gi 1109567921 241 LGIFYRDSKRKTFEEHLAAY--RHDSRPLYQR 270
Cdd:TIGR02177 241 IGIFYKNENKPTFEERLEKIlpRYMSAPPAEQ 272
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
1-261 |
2.41e-114 |
|
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: 329.80 E-value: 2.41e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 1 MPQDYELPDLDIAWCPGCGNFGILTLLKKALAELsIEPRQLVIASGIGQAAKTPHYLKSHVFNGLHGRALPAATAIKAGN 80
Cdd:COG1013 2 LKKKDLLRTPGHRWCPGCGHGIILRLLLKALDEL-LDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 81 PQLTVIAQGGDGDMYGEGGNHFLHAIRRNPDLTHLVHDNMVYGLTKGQASPTSQPGFVTPLQVDGVCQEPFNPLSVAIAL 160
Cdd:COG1013 81 PDLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 161 NASFVARIYVGAVAHAVTVLKAALRHHGYALVDILQPCVSFNRLN---TYEWFEEHCYFLEEgHDPEDrqaAFARACET- 236
Cdd:COG1013 161 GATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRDpskTIEWAKEGMWPLYE-YDPGE---KLRLTYEPk 236
|
250 260
....*....|....*....|....*
gi 1109567921 237 ERLPLGIFYRDSKRktFEEHLAAYR 261
Cdd:COG1013 237 DKIPVGEFLKNQGR--FEELIEEIQ 259
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
14-201 |
2.43e-111 |
|
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: 319.47 E-value: 2.43e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 14 WCPGCGNFGILTLLKKALAELSIEPRQLVIASGIGQAAKTPHYLKSHVFNGLHGRALPAATAIKAGNPQLTVIAQGGDGD 93
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 94 MYGEGGNHFLHAIRRNPDLTHLVHDNMVYGLTKGQASPTSQPGFVTPLQVDGVCQEPFNPLSVAIALNASFVARIYVGAV 173
Cdd:cd03375 81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160
|
170 180
....*....|....*....|....*...
gi 1109567921 174 AHAVTVLKAALRHHGYALVDILQPCVSF 201
Cdd:cd03375 161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
49-194 |
1.77e-29 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 109.21 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 49 QAAKTPHYLKSHVFnGLHGRALPAATAIKAGNPQLTVIAQGGDGDMYGEGgNHFLHAIRRNPDLTHLVHDNMVYGLTKGQ 128
Cdd:pfam02775 14 RFRPPRRYLTSGGL-GTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNL-QELATAVRYNLPITVVVLNNGGYGMTRGQ 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109567921 129 ASPTsqpGFVTPLQVDGVCQEPFNPLSVAIALNASfVARiyVGAVAHAVTVLKAALRHHGYALVDI 194
Cdd:pfam02775 92 QTPF---GGGRYSGPSGKILPPVDFAKLAEAYGAK-GAR--VESPEELEEALKEALEHDGPALIDV 151
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11869 |
PRK11869 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
9-286 |
4.02e-165 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183349 [Multi-domain] Cd Length: 280 Bit Score: 459.25 E-value: 4.02e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 9 DLDIAWCPGCGNFGILTLLKKALAELSIEPRQLVIASGIGQAAKTPHYLKSHVFNGLHGRALPAATAIKAGNPQLTVIAQ 88
Cdd:PRK11869 5 KYDIAWCPGCGNFGIRNALMKALSELNLKPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTVIAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 89 GGDGDMYGEGGNHFLHAIRRNPDLTHLVHDNMVYGLTKGQASPTSQPGFVTPLQVDGVCQEPFNPLSVAIALNASFVARI 168
Cdd:PRK11869 85 GGDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASFVART 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 169 YVGAVAHAVTVLKAALRHHGYALVDILQPCVSFNRLNTYEWFEEHCYFLeEGHDPEDRQAAFARACETERLPLGIFYRDS 248
Cdd:PRK11869 165 FSGDIEETKEILKEAIKHKGLAIVDIFQPCVSFNKVNTYQWYRENTYYL-KDHDPTDRELAFKRALETEKLPLGIFYINE 243
|
250 260 270
....*....|....*....|....*....|....*...
gi 1109567921 249 KRkTFEEHLAAYRHDSRPLYQRSPNTGRLHELINDKRL 286
Cdd:PRK11869 244 KP-TFEELVPAYKGDKTPLWKREPNFEKLKELIESKRS 280
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
12-270 |
1.89e-136 |
|
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number of anaerobic and microaerophilic species lack pyruvate dehydrogenase and have instead a four subunit, oxygen-sensitive pyruvate oxidoreductase, with either ferredoxins or flavodoxins used as the acceptor. Several related four-subunit enzymes may exist in the same species. This model describes a subfamily of beta subunits, representing mostly pyruvate and 2-ketoisovalerate specific enzymes.
Pssm-ID: 274015 [Multi-domain] Cd Length: 287 Bit Score: 386.81 E-value: 1.89e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 12 IAWCPGCGNFGILTLLKKALAELSIEPRQLVIASGIGQAAKTPHYLKSHVFNGLHGRALPAATAIKAGNPQLTVIAQGGD 91
Cdd:TIGR02177 1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 92 GDMYGEGGNHFLHAIRRNPDLTHLVHDNMVYGLTKGQASPTSQPGFVTPLQVDGVCQEPFNPLSVAIALNASFVARIYVG 171
Cdd:TIGR02177 81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 172 AVAHAVTVLKAALRHHGYALVDILQPCVSFNRLNTYEWFEEHCYFLEE-GHDPEDRQ---------AAFARACET-ERLP 240
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNKINTYEWYRERVYKLDEeGYDPIVREpeefeekaaAAIKKAMEWgDRIP 240
|
250 260 270
....*....|....*....|....*....|..
gi 1109567921 241 LGIFYRDSKRKTFEEHLAAY--RHDSRPLYQR 270
Cdd:TIGR02177 241 IGIFYKNENKPTFEERLEKIlpRYMSAPPAEQ 272
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
3-267 |
1.10e-122 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 351.84 E-value: 1.10e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 3 QDYeLPDLDIAWCPGCGNFGILTLLKKALAELSIEPRQLVIASGIGQAAKTPHYLKSHVFNGLHGRALPAATAIKAGNPQ 82
Cdd:PRK11867 9 KDF-RNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGLKLANPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 83 LTVIAQGGDGDMYGEGGNHFLHAIRRNPDLTHLVHDNMVYGLTKGQASPTSQPGFVTPLQVDGVCQEPFNPLSVAIALNA 162
Cdd:PRK11867 88 LTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVELALGAGA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 163 SFVARIYVGAVAHAVTVLKAALRHHGYALVDILQPCVSFNRLNTYEWFEEHCYFL--EEGHDPEDRQAAFARACETERLP 240
Cdd:PRK11867 168 TFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFNNVNTFDWFKERLVKVhdAEGYDPTNALAAMKTLEEGDPIP 247
|
250 260
....*....|....*....|....*..
gi 1109567921 241 LGIFYRDSkRKTFEEHLAAYRHDSRPL 267
Cdd:PRK11867 248 TGIFYQVE-RPTYEEAVRAQIEGPLAL 273
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
1-272 |
2.09e-122 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 351.87 E-value: 2.09e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 1 MPQDYELPDLDIAWCPGCGNFGILTLLKKALAELSIEPRQLVIASGIGQAAKTPHYLKSHVFNGLHGRALPAATAIKAGN 80
Cdd:PRK05778 7 GLTYLRYDGLPTTWCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLAN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 81 PQLTVIAQGGDGDMYGEGGNHFLHAIRRNPDLTHLVHDNMVYGLTKGQASPTSQPGFVTPLQVDGVCQEPFNPLSVAIAL 160
Cdd:PRK05778 87 PDLEVIVVGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 161 NASFVARIYVGAVAHAVTVLKAALRHHGYALVDILQPCVSFNRLNTY--------EWFEEHCYFL--EEGHDPEDRQAAF 230
Cdd:PRK05778 167 GATFVARSFAGDVKQLVELIKKAISHKGFAFIDVLSPCVTFNGRNTStkspaymrEYYKKRVYKLklEEDYDPTDRDKAA 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1109567921 231 ARACETE---RLPLGIFYRDSKRkTFEEHLAAYRhdsRPLYQRSP 272
Cdd:PRK05778 247 EKMLEEElggKIPIGVFYKNERP-TFEERLEKLI---EPLLELPP 287
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
14-272 |
1.01e-114 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 331.34 E-value: 1.01e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 14 WCPGCGNFGILTLLKKALAELSIEPRQLVIASGIGQAAKTPHYLKSHVFNGLHGRALPAATAIKAGNPQLTVIAQGGDGD 93
Cdd:PRK11866 9 WCPGCGNYGILEALRKALAELGIPPENVVVVSGIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLTVIGYGGDGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 94 MYGEGGNHFLHAIRRNPDLTHLVHDNMVYGLTKGQASPTSQPGFVTPLQVDGVCQEPFNPLSVAIALNASFVARIYVGAV 173
Cdd:PRK11866 89 GYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATFVARGFSGDV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 174 AHAVTVLKAALRHHGYALVDILQPCVSFNRLNTYEWFEEHCYFLEE-GHDPEDRQAAFARACETE-RLPLGIFYrDSKRK 251
Cdd:PRK11866 169 KHLKEIIKEAIKHKGFSFIDVLSPCVTFNKLNTYDWFRPRVYKLEEtGHDPTNFEQAYKKALEWGdRIPIGVFY-KEEKP 247
|
250 260
....*....|....*....|.
gi 1109567921 252 TFEEHLAAYRHDSRPLYQRSP 272
Cdd:PRK11866 248 TYEEELDEILKNPPLADQPLQ 268
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
1-261 |
2.41e-114 |
|
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: 329.80 E-value: 2.41e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 1 MPQDYELPDLDIAWCPGCGNFGILTLLKKALAELsIEPRQLVIASGIGQAAKTPHYLKSHVFNGLHGRALPAATAIKAGN 80
Cdd:COG1013 2 LKKKDLLRTPGHRWCPGCGHGIILRLLLKALDEL-LDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 81 PQLTVIAQGGDGDMYGEGGNHFLHAIRRNPDLTHLVHDNMVYGLTKGQASPTSQPGFVTPLQVDGVCQEPFNPLSVAIAL 160
Cdd:COG1013 81 PDLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 161 NASFVARIYVGAVAHAVTVLKAALRHHGYALVDILQPCVSFNRLN---TYEWFEEHCYFLEEgHDPEDrqaAFARACET- 236
Cdd:COG1013 161 GATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRDpskTIEWAKEGMWPLYE-YDPGE---KLRLTYEPk 236
|
250 260
....*....|....*....|....*
gi 1109567921 237 ERLPLGIFYRDSKRktFEEHLAAYR 261
Cdd:COG1013 237 DKIPVGEFLKNQGR--FEELIEEIQ 259
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
14-201 |
2.43e-111 |
|
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: 319.47 E-value: 2.43e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 14 WCPGCGNFGILTLLKKALAELSIEPRQLVIASGIGQAAKTPHYLKSHVFNGLHGRALPAATAIKAGNPQLTVIAQGGDGD 93
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 94 MYGEGGNHFLHAIRRNPDLTHLVHDNMVYGLTKGQASPTSQPGFVTPLQVDGVCQEPFNPLSVAIALNASFVARIYVGAV 173
Cdd:cd03375 81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160
|
170 180
....*....|....*....|....*...
gi 1109567921 174 AHAVTVLKAALRHHGYALVDILQPCVSF 201
Cdd:cd03375 161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
|
|
| oorB |
PRK09628 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; |
14-260 |
2.91e-41 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
Pssm-ID: 182003 [Multi-domain] Cd Length: 277 Bit Score: 143.72 E-value: 2.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 14 WCPGCGNFGILTLLKKALAELSIEPRQLVIASGIGQAAKTPHYLKSHVFNGLHGRALPAATAIKAGNPQLTVIAQGGDGD 93
Cdd:PRK09628 18 WCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGIKLANPDKHVIVVSGDGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 94 MYGEGGNHFLHAIRRNPDLTHLVHDNMVYGLTKGQASPTSQPGFVTPLQVDGVCQEPFNPLSVAIALNASFVARIYVGAV 173
Cdd:PRK09628 98 GLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKLATAAGASFVARESVIDP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 174 AHAVTVLKAALRHHGYALVDILQPC-VSFNRLN-------TYEWFEEHCY----FleEGHDPEDRQAAFaraceterlPL 241
Cdd:PRK09628 178 QKLEKLLVKGFSHKGFSFFDVFSNChINLGRKNkmgeavqMLKWIESRTVskrkF--DALSPEERVGKF---------PT 246
|
250
....*....|....*....
gi 1109567921 242 GIFYRDSKRKtfeEHLAAY 260
Cdd:PRK09628 247 GILKHDTDRK---EYCEAY 262
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
49-194 |
1.77e-29 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 109.21 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 49 QAAKTPHYLKSHVFnGLHGRALPAATAIKAGNPQLTVIAQGGDGDMYGEGgNHFLHAIRRNPDLTHLVHDNMVYGLTKGQ 128
Cdd:pfam02775 14 RFRPPRRYLTSGGL-GTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNL-QELATAVRYNLPITVVVLNNGGYGMTRGQ 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109567921 129 ASPTsqpGFVTPLQVDGVCQEPFNPLSVAIALNASfVARiyVGAVAHAVTVLKAALRHHGYALVDI 194
Cdd:pfam02775 92 QTPF---GGGRYSGPSGKILPPVDFAKLAEAYGAK-GAR--VESPEELEEALKEALEHDGPALIDV 151
|
|
| PFO_beta_C |
pfam12367 |
Pyruvate ferredoxin oxidoreductase beta subunit C terminal; This domain family is found in ... |
198-258 |
4.08e-28 |
|
Pyruvate ferredoxin oxidoreductase beta subunit C terminal; This domain family is found in bacteria and archaea, and is approximately 70 amino acids in length. The family is found in association with pfam02775. There are two completely conserved residues (A and G) that may be functionally important. PFO is involved in carbon dioxide fixation via a reductive TCA cycle. It forms a heterodimer (alpha/beta). The beta subunit has binding motifs for Fe-S clusters and thiamine pyrophosphate.
Pssm-ID: 463551 [Multi-domain] Cd Length: 62 Bit Score: 102.57 E-value: 4.08e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109567921 198 CVSFNRLNTYEWFEEHCYFLEEGHDPEDRQAAFARACE-TERLPLGIFYRDSkRKTFEEHLA 258
Cdd:pfam12367 1 CVTFNKVNTYDWYKERVYKLDEDHDPTDREAAMEKALEwGDRIPIGIFYKEE-RPTFEERLP 61
|
|
| TPP_PFOR |
cd02018 |
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ... |
15-198 |
8.93e-12 |
|
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: 63.66 E-value: 8.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 15 CPGCGNFGILTLLKKALAElsiePRQLVIASGIG----QAAKTPHY-LKSHVFNGLHGRALPAATAIKAG----NPQL-- 83
Cdd:cd02018 8 CAGCGEVTAVRVVLAALPA----PEDTVIANSTGcssvYASTAPFNsWAVPWVNSLFEDANAVASGLKRGlkarFPKDre 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 84 -----TVIAQGGDGDMYGEGGNHFLHAIRRNPDLTHLVHDNMVYGLTKGQASPTSQPGFVTPLQVDGVcQEPFNPLsVAI 158
Cdd:cd02018 84 ldkkkDVVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGK-KEDKKDL-VLI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1109567921 159 ALNAS--FVARIYVGAVAHAVTVLKAAL-RHHGYALVDILQPC 198
Cdd:cd02018 162 AATHGcvYVARLSPALKKHFLKVVKEAIsRTDGPTFIHAYTPC 204
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
42-196 |
6.96e-10 |
|
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: 56.88 E-value: 6.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 42 VIASGIGQAAKTPHYLKSHVF---------NGLHGRALPAATAIKAGNPQLTVIAQGGDGDMyGEGGNHFLHAIRRNPDL 112
Cdd:cd00568 15 IVVNDAGNSAYWAYRYLPLRRgrrfltstgFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGF-MMTGQELATAVRYGLPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 113 THLVHDNMVYGLTKGQASPTsqpgfvTPLQVDGVcqEPFNPLSVAIAlnASFVARIY-VGAVAHAVTVLKAALRHHGYAL 191
Cdd:cd00568 94 IVVVFNNGGYGTIRMHQEAF------YGGRVSGT--DLSNPDFAALA--EAYGAKGVrVEDPEDLEAALAEALAAGGPAL 163
|
....*
gi 1109567921 192 VDILQ 196
Cdd:cd00568 164 IEVKT 168
|
|
| PRK11865 |
PRK11865 |
pyruvate synthase subunit beta; |
15-262 |
3.72e-08 |
|
pyruvate synthase subunit beta;
Pssm-ID: 183346 [Multi-domain] Cd Length: 299 Bit Score: 53.56 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 15 CPGCGNFGILTLLKKALAELSIeprqLVIASGIGQAAKTPhYLKS-------HV-FNGLHGRALPAATAIKAGNPQLTVI 86
Cdd:PRK11865 21 CAGCGAAIAMRLALKALGKNTV----IVVATGCLEVITTP-YPETawnvpwiHVaFENAAAVASGIERAVKALGKKVNVV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 87 AQGGDGDMYGEGGNHFLHAIRRNPDLTHLVHDNMVYGLTKGQASPTSQPGFVT----PLQVDGVCQEPFNPLS-VAIALN 161
Cdd:PRK11865 96 AIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTttspAGKYSRGEDRPKKNMPlIMAAHG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 162 ASFVARIYVGAVAHAVTVLKAALRHHGYALVDILQPCvsfnrlnTYEWfeehcyfleeGHDPEdRQAAFAR-ACETERLP 240
Cdd:PRK11865 176 IPYVATASIGYPEDFMEKVKKAKEVEGPAYIQVLQPC-------PTGW----------GFPPE-KTIEIGRlAVETGYWP 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 1109567921 241 L--------GIFYRDSK-----RKTFEEHLAA---YRH 262
Cdd:PRK11865 238 LfeiengkfKITYEPLHldrrtRKPIEEYLKVqgrFKH 275
|
|
| TPP_PFOR_porB_like |
cd03376 |
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ... |
15-199 |
4.85e-07 |
|
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: 49.54 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 15 CPGCGNFGILTLLKKALAELSIeprqLVIASGIGQAAKTPHYLKSH---VFNGLHGRALPAATAIKAGNPQL------TV 85
Cdd:cd03376 8 CAGCGAALALRHVLKALGPDTV----VVNPTGCLEVITTPYPYTAWrvpWIHVAFENAAAVASGIEAALKALgrgkdiTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 86 IAQGGDGDMYGEGGNHFLHAIRRNPDLTHLVHDNMVYGLTKGQASPTSQPGFVT---PL--QVDGVCQEPFNPLSVAIAL 160
Cdd:cd03376 84 VAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTtttPVgkVSFGKKQPKKDLPLIMAAH 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 1109567921 161 NASFVARIYVGAVAHAVTVLKAALRHHGYALVDILQPCV 199
Cdd:cd03376 164 NIPYVATASVAYPEDLYKKVKKALSIEGPAYIHILSPCP 202
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
64-134 |
1.53e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 44.82 E-value: 1.53e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109567921 64 GLHGRALPAATAIKAGNPQLTVIAQGGDGDMYGEGGNHFLHAIRRNPDLTHLVHDNMVYGLTKGQASPTSQ 134
Cdd:PRK06163 57 GSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTIAALAPKNLTIIVMDNGVYQITGGQPTLTSQ 127
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
64-126 |
2.18e-04 |
|
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity.
Pssm-ID: 238971 [Multi-domain] Cd Length: 196 Bit Score: 41.34 E-value: 2.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109567921 64 GLHGRALPAATAIKAGNPQLTVIAQGGDGdMYGEGGNHFLHAIRRNPDLTHLVHDNMVYGLTK 126
Cdd:cd02013 53 GNCGYALPAIIGAKAAAPDRPVVAIAGDG-AWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEK 114
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
38-123 |
5.75e-03 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 37.93 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109567921 38 PRQLVIASGIGQAAKTPHylKSHVFNGLH----------GRALPAATAIKAGNPQLTVIAQGGDGD--MYGEggnHFLHA 105
Cdd:PRK08199 381 PADAIITNGAGNYATWLH--RFFRFRRYRtqlaptsgsmGYGLPAAIAAKLLFPERTVVAFAGDGCflMNGQ---ELATA 455
|
90
....*....|....*...
gi 1109567921 106 IRRNPDLTHLVHDNMVYG 123
Cdd:PRK08199 456 VQYGLPIIVIVVNNGMYG 473
|
|
| |
