|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
1-282 |
1.37e-143 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 404.99 E-value: 1.37e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 1 MATLVDFRAEK-PNWCPGCGDFTVLAALQKAAVNIGLEPEQMVTVSGVGCSGKISQYMGSYGFHSLHGRSLPVATAVKLA 79
Cdd:PRK11867 5 MLTAKDFRNDQePRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGLKLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 80 NRDLTVVAAGGDGDGYGIGMGHFIHAMRRNIDITYLVMDNHIYGLTTGQTSPTSDKGSKTKTAPDGAVEEPVHPLQMALM 159
Cdd:PRK11867 85 NPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVELALG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 160 AGCGFVAQGYSGNLKQLTELIEKGMQHRGFSLINIYSPCVTFNKVNTYDFYKSNLVNIDEDASYDKTDRFAAIRKLEEHE 239
Cdd:PRK11867 165 AGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFNNVNTFDWFKERLVKVHDAEGYDPTNALAAMKTLEEGD 244
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1199122193 240 ENVTGVLYHNPaKQAYDEVLRGYPEQAIAKNDLKITRDQWEKL 282
Cdd:PRK11867 245 PIPTGIFYQVE-RPTYEEAVRAQIEGPLALQDLLMGGDTWTVL 286
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
14-201 |
1.32e-107 |
|
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: 310.23 E-value: 1.32e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 14 WCPGCGDFTVLAALQKAAVNIGLEPEQMVTVSGVGCSGKISQYMGSYGFHSLHGRSLPVATAVKLANRDLTVVAAGGDGD 93
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 94 GYGIGMGHFIHAMRRNIDITYLVMDNHIYGLTTGQTSPTSDKGSKTKTAPDGAVEEPVHPLQMALMAGCGFVAQGYSGNL 173
Cdd:cd03375 81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160
|
170 180
....*....|....*....|....*...
gi 1199122193 174 KQLTELIEKGMQHRGFSLINIYSPCVTF 201
Cdd:cd03375 161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
12-273 |
2.49e-107 |
|
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: 313.24 E-value: 2.49e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 12 PNWCPGCGDFTVLAALQKAAVNIGLEPEQMVTVSGVGCSGKISQYMGSYGFHSLHGRSLPVATAVKLANRDLTVVAAGGD 91
Cdd:TIGR02177 1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 92 GDGYGIGMGHFIHAMRRNIDITYLVMDNHIYGLTTGQTSPTSDKGSKTKTAPDGAVEEPVHPLQMALMAGCGFVAQGYSG 171
Cdd:TIGR02177 81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 172 NLKQLTELIEKGMQHRGFSLINIYSPCVTFNKVNTYDFYKSNLVNIDEDaSYDKTDR---------FAAIRKLEEHEENV 242
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNKINTYEWYRERVYKLDEE-GYDPIVRepeefeekaAAAIKKAMEWGDRI 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 1199122193 243 -TGVLYHNPAKQAYDEVLR----GYPEQAIAKNDLK 273
Cdd:TIGR02177 240 pIGIFYKNENKPTFEERLEkilpRYMSAPPAEQEIK 275
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
7-260 |
6.24e-107 |
|
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: 310.92 E-value: 6.24e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 7 FRAEKPNWCPGCGDFTVLAALQKAAVNIgLEPEQMVTVSGVGCSGKISQYMGSYGFHSLHGRSLPVATAVKLANRDLTVV 86
Cdd:COG1013 8 LRTPGHRWCPGCGHGIILRLLLKALDEL-LDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANPDLTVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 87 A------------AggdgdgygigmgHFIHAMRRNIDITYLVMDNHIYGLTTGQTSPTSDKGSKTKTAPDGAVEEPVHPL 154
Cdd:COG1013 87 VfggdgdtydiggN------------HLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 155 QMALMAGCGFVAQGYSGNLKQLTELIEKGMQHRGFSLINIYSPCVTFNKVN---TYDFYKSNLVNIDEdasYDKTDRFAA 231
Cdd:COG1013 155 EIAAAHGATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRDpskTIEWAKEGMWPLYE---YDPGEKLRL 231
|
250 260
....*....|....*....|....*....
gi 1199122193 232 IRKLEehEENVTGVLYHNPAKqaYDEVLR 260
Cdd:COG1013 232 TYEPK--DKIPVGEFLKNQGR--FEELIE 256
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
46-194 |
1.27e-27 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 104.20 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 46 GVGCSG----------KISQYMGSYGfHSLHGRSLPVATAVKLANRDLTVVA-----AGGDGDGygigmgHFIHAMRRNI 110
Cdd:pfam02775 1 DIGCHQmwaaqyyrfrPPRRYLTSGG-LGTMGYGLPAAIGAKLARPDRPVVAiagdgGFQMNLQ------ELATAVRYNL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 111 DITYLVMDNHIYGLTTGQTSPtsdKGSKTKTAPDGAVEEPVHPLQMALMAGCGFVaqgYSGNLKQLTELIEKGMQHRGFS 190
Cdd:pfam02775 74 PITVVVLNNGGYGMTRGQQTP---FGGGRYSGPSGKILPPVDFAKLAEAYGAKGA---RVESPEELEEALKEALEHDGPA 147
|
....
gi 1199122193 191 LINI 194
Cdd:pfam02775 148 LIDV 151
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
1-282 |
1.37e-143 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 404.99 E-value: 1.37e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 1 MATLVDFRAEK-PNWCPGCGDFTVLAALQKAAVNIGLEPEQMVTVSGVGCSGKISQYMGSYGFHSLHGRSLPVATAVKLA 79
Cdd:PRK11867 5 MLTAKDFRNDQePRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGLKLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 80 NRDLTVVAAGGDGDGYGIGMGHFIHAMRRNIDITYLVMDNHIYGLTTGQTSPTSDKGSKTKTAPDGAVEEPVHPLQMALM 159
Cdd:PRK11867 85 NPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVELALG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 160 AGCGFVAQGYSGNLKQLTELIEKGMQHRGFSLINIYSPCVTFNKVNTYDFYKSNLVNIDEDASYDKTDRFAAIRKLEEHE 239
Cdd:PRK11867 165 AGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFNNVNTFDWFKERLVKVHDAEGYDPTNALAAMKTLEEGD 244
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1199122193 240 ENVTGVLYHNPaKQAYDEVLRGYPEQAIAKNDLKITRDQWEKL 282
Cdd:PRK11867 245 PIPTGIFYQVE-RPTYEEAVRAQIEGPLALQDLLMGGDTWTVL 286
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
1-264 |
1.51e-122 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 352.26 E-value: 1.51e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 1 MATLVDFRAEKPNWCPGCGDFTVLAALQKAAVNIGLEPEQMVTVSGVGCSGKISQYMGSYGFHSLHGRSLPVATAVKLAN 80
Cdd:PRK05778 7 GLTYLRYDGLPTTWCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLAN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 81 RDLTVVAAGGDGDGYGIGMGHFIHAMRRNIDITYLVMDNHIYGLTTGQTSPTSDKGSKTKTAPDGAVEEPVHPLQMALMA 160
Cdd:PRK05778 87 PDLEVIVVGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 161 GCGFVAQGYSGNLKQLTELIEKGMQHRGFSLINIYSPCVTFNKVNTYD--------FYKSNLVNIDEDASYDKTDRFAAI 232
Cdd:PRK05778 167 GATFVARSFAGDVKQLVELIKKAISHKGFAFIDVLSPCVTFNGRNTSTkspaymreYYKKRVYKLKLEEDYDPTDRDKAA 246
|
250 260 270
....*....|....*....|....*....|....*
gi 1199122193 233 RKLEEHEEN---VTGVLYHNPaKQAYDEVLRGYPE 264
Cdd:PRK05778 247 EKMLEEELGgkiPIGVFYKNE-RPTFEERLEKLIE 280
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
14-201 |
1.32e-107 |
|
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: 310.23 E-value: 1.32e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 14 WCPGCGDFTVLAALQKAAVNIGLEPEQMVTVSGVGCSGKISQYMGSYGFHSLHGRSLPVATAVKLANRDLTVVAAGGDGD 93
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 94 GYGIGMGHFIHAMRRNIDITYLVMDNHIYGLTTGQTSPTSDKGSKTKTAPDGAVEEPVHPLQMALMAGCGFVAQGYSGNL 173
Cdd:cd03375 81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160
|
170 180
....*....|....*....|....*...
gi 1199122193 174 KQLTELIEKGMQHRGFSLINIYSPCVTF 201
Cdd:cd03375 161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
12-273 |
2.49e-107 |
|
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: 313.24 E-value: 2.49e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 12 PNWCPGCGDFTVLAALQKAAVNIGLEPEQMVTVSGVGCSGKISQYMGSYGFHSLHGRSLPVATAVKLANRDLTVVAAGGD 91
Cdd:TIGR02177 1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 92 GDGYGIGMGHFIHAMRRNIDITYLVMDNHIYGLTTGQTSPTSDKGSKTKTAPDGAVEEPVHPLQMALMAGCGFVAQGYSG 171
Cdd:TIGR02177 81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 172 NLKQLTELIEKGMQHRGFSLINIYSPCVTFNKVNTYDFYKSNLVNIDEDaSYDKTDR---------FAAIRKLEEHEENV 242
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNKINTYEWYRERVYKLDEE-GYDPIVRepeefeekaAAAIKKAMEWGDRI 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 1199122193 243 -TGVLYHNPAKQAYDEVLR----GYPEQAIAKNDLK 273
Cdd:TIGR02177 240 pIGIFYKNENKPTFEERLEkilpRYMSAPPAEQEIK 275
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
7-260 |
6.24e-107 |
|
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: 310.92 E-value: 6.24e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 7 FRAEKPNWCPGCGDFTVLAALQKAAVNIgLEPEQMVTVSGVGCSGKISQYMGSYGFHSLHGRSLPVATAVKLANRDLTVV 86
Cdd:COG1013 8 LRTPGHRWCPGCGHGIILRLLLKALDEL-LDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANPDLTVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 87 A------------AggdgdgygigmgHFIHAMRRNIDITYLVMDNHIYGLTTGQTSPTSDKGSKTKTAPDGAVEEPVHPL 154
Cdd:COG1013 87 VfggdgdtydiggN------------HLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 155 QMALMAGCGFVAQGYSGNLKQLTELIEKGMQHRGFSLINIYSPCVTFNKVN---TYDFYKSNLVNIDEdasYDKTDRFAA 231
Cdd:COG1013 155 EIAAAHGATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRDpskTIEWAKEGMWPLYE---YDPGEKLRL 231
|
250 260
....*....|....*....|....*....
gi 1199122193 232 IRKLEehEENVTGVLYHNPAKqaYDEVLR 260
Cdd:COG1013 232 TYEPK--DKIPVGEFLKNQGR--FEELIE 256
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
12-263 |
3.14e-103 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 302.45 E-value: 3.14e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 12 PNWCPGCGDFTVLAALQKAAVNIGLEPEQMVTVSGVGCSGKISQYMGSYGFHSLHGRSLPVATAVKLANRDLTVVAAGGD 91
Cdd:PRK11866 7 PIWCPGCGNYGILEALRKALAELGIPPENVVVVSGIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLTVIGYGGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 92 GDGYGIGMGHFIHAMRRNIDITYLVMDNHIYGLTTGQTSPTSDKGSKTKTAPDGAVEEPVHPLQMALMAGCGFVAQGYSG 171
Cdd:PRK11866 87 GDGYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATFVARGFSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 172 NLKQLTELIEKGMQHRGFSLINIYSPCVTFNKVNTYDFYKSNLVNIdEDASYDKTDRFAAIRKLEEHEENV-TGVLY--H 248
Cdd:PRK11866 167 DVKHLKEIIKEAIKHKGFSFIDVLSPCVTFNKLNTYDWFRPRVYKL-EETGHDPTNFEQAYKKALEWGDRIpIGVFYkeE 245
|
250
....*....|....*.
gi 1199122193 249 NPA-KQAYDEVLRGYP 263
Cdd:PRK11866 246 KPTyEEELDEILKNPP 261
|
|
| PRK11869 |
PRK11869 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
14-262 |
3.11e-86 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183349 [Multi-domain] Cd Length: 280 Bit Score: 259.33 E-value: 3.11e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 14 WCPGCGDFTVLAALQKAAVNIGLEPEQMVTVSGVGCSGKISQYMGSYGFHSLHGRSLPVATAVKLANRDLTVVAAGGDGD 93
Cdd:PRK11869 10 WCPGCGNFGIRNALMKALSELNLKPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTVIAEGGDGD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 94 GYGIGMGHFIHAMRRNIDITYLVMDNHIYGLTTGQTSPTSDKGSKTKTAPDGAVEEPVHPLQMALMAGCGFVAQGYSGNL 173
Cdd:PRK11869 90 MYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASFVARTFSGDI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 174 KQLTELIEKGMQHRGFSLINIYSPCVTFNKVNTYDFYKSNLVNIDEdasYDKTDRFAAIRKLEEHEENVTGVLYHNpAKQ 253
Cdd:PRK11869 170 EETKEILKEAIKHKGLAIVDIFQPCVSFNKVNTYQWYRENTYYLKD---HDPTDRELAFKRALETEKLPLGIFYIN-EKP 245
|
....*....
gi 1199122193 254 AYDEVLRGY 262
Cdd:PRK11869 246 TFEELVPAY 254
|
|
| oorB |
PRK09628 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; |
14-260 |
1.11e-49 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
Pssm-ID: 182003 [Multi-domain] Cd Length: 277 Bit Score: 165.67 E-value: 1.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 14 WCPGCGDFTVLAALQKAAVNIGLEPEQMVTVSGVGCSGKISQYMGSYGFHSLHGRSLPVATAVKLANRDLTVVAAGGDGD 93
Cdd:PRK09628 18 WCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGIKLANPDKHVIVVSGDGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 94 GYGIGMGHFIHAMRRNIDITYLVMDNHIYGLTTGQTSPTSDKGSKTKTAPDGAVEEPVHPLQMALMAGCGFVAQGYSGNL 173
Cdd:PRK09628 98 GLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKLATAAGASFVARESVIDP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 174 KQLTELIEKGMQHRGFSLINIYSPC-VTFNKVNTYDFYKSNLVNIDeDASYDKTdRFAAIRKLEEHEENVTGVLYHNPAK 252
Cdd:PRK09628 178 QKLEKLLVKGFSHKGFSFFDVFSNChINLGRKNKMGEAVQMLKWIE-SRTVSKR-KFDALSPEERVGKFPTGILKHDTDR 255
|
250
....*....|..
gi 1199122193 253 ----QAYDEVLR 260
Cdd:PRK09628 256 keycEAYEEVIE 267
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
46-194 |
1.27e-27 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 104.20 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 46 GVGCSG----------KISQYMGSYGfHSLHGRSLPVATAVKLANRDLTVVA-----AGGDGDGygigmgHFIHAMRRNI 110
Cdd:pfam02775 1 DIGCHQmwaaqyyrfrPPRRYLTSGG-LGTMGYGLPAAIGAKLARPDRPVVAiagdgGFQMNLQ------ELATAVRYNL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 111 DITYLVMDNHIYGLTTGQTSPtsdKGSKTKTAPDGAVEEPVHPLQMALMAGCGFVaqgYSGNLKQLTELIEKGMQHRGFS 190
Cdd:pfam02775 74 PITVVVLNNGGYGMTRGQQTP---FGGGRYSGPSGKILPPVDFAKLAEAYGAKGA---RVESPEELEEALKEALEHDGPA 147
|
....
gi 1199122193 191 LINI 194
Cdd:pfam02775 148 LIDV 151
|
|
| TPP_PFOR |
cd02018 |
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ... |
15-206 |
4.36e-19 |
|
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: 84.07 E-value: 4.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 15 CPGCGDFT----VLAALQKaavniglePEQMVTVSGVGCSgkiSQYMGSYGF--------HSLHGRSLPVATAVK----- 77
Cdd:cd02018 8 CAGCGEVTavrvVLAALPA--------PEDTVIANSTGCS---SVYASTAPFnswavpwvNSLFEDANAVASGLKrglka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 78 ----LANRDL--TVVAAGGDGDGYGIGMGHFIHAMRRNIDITYLVMDNHIYGLTTGQTSPTSDKGSKTKTAPDGAVEEPV 151
Cdd:cd02018 77 rfpkDRELDKkkDVVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1199122193 152 HPLQMALMAGCGFVAQ---GYSG-NLKQLTELIekgMQHRGFSLINIYSPCVTFNKVNT 206
Cdd:cd02018 157 DLVLIAATHGCVYVARlspALKKhFLKVVKEAI---SRTDGPTFIHAYTPCITEWGIGS 212
|
|
| PFO_beta_C |
pfam12367 |
Pyruvate ferredoxin oxidoreductase beta subunit C terminal; This domain family is found in ... |
198-261 |
5.36e-19 |
|
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: 78.69 E-value: 5.36e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1199122193 198 CVTFNKVNTYDFYKSNLVNIDEDasYDKTDRFAAIRK-LEEHEENVTGVLYHNPaKQAYDEVLRG 261
Cdd:pfam12367 1 CVTFNKVNTYDWYKERVYKLDED--HDPTDREAAMEKaLEWGDRIPIGIFYKEE-RPTFEERLPV 62
|
|
| PRK11865 |
PRK11865 |
pyruvate synthase subunit beta; |
15-200 |
1.96e-11 |
|
pyruvate synthase subunit beta;
Pssm-ID: 183346 [Multi-domain] Cd Length: 299 Bit Score: 63.19 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 15 CPGCGDFTVLAALQKAAvniglePEQMVTVSGVGCSgKISQYMGSY----------GFHSLHGRSLPVATAVKLANRDLT 84
Cdd:PRK11865 21 CAGCGAAIAMRLALKAL------GKNTVIVVATGCL-EVITTPYPEtawnvpwihvAFENAAAVASGIERAVKALGKKVN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 85 VVAAGGDGDGYGIGMGHFIHAMRRNIDITYLVMDNHIYGLTTGQTSPTSDKGSKTKTAPDGAV----EEPVHPLQMALMA 160
Cdd:PRK11865 94 VVAIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKYsrgeDRPKKNMPLIMAA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1199122193 161 -GCGFVAQGYSGNLKQLTELIEKGMQHRGFSLINIYSPCVT 200
Cdd:PRK11865 174 hGIPYVATASIGYPEDFMEKVKKAKEVEGPAYIQVLQPCPT 214
|
|
| TPP_PFOR_porB_like |
cd03376 |
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ... |
15-200 |
3.86e-11 |
|
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: 61.49 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 15 CPGCGDFTVLAALQKAAvniglePEQMVTVSGVGCSGKISqymGSYG--------FHSLHGRSLPVATAVKLA------N 80
Cdd:cd03376 8 CAGCGAALALRHVLKAL------GPDTVVVNPTGCLEVIT---TPYPytawrvpwIHVAFENAAAVASGIEAAlkalgrG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 81 RDLTVVAAGGDGDGYGIGMGHFIHAMRRNIDITYLVMDNHIYGLTTGQTSPTSDKGSKTKTAPDGAVE--EPVHPLQMAL 158
Cdd:cd03376 79 KDITVVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTTPVGKVSfgKKQPKKDLPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1199122193 159 -MAGCG--FVAQGYSGNLKQLTELIEKGMQHRGFSLINIYSPCVT 200
Cdd:cd03376 159 iMAAHNipYVATASVAYPEDLYKKVKKALSIEGPAYIHILSPCPT 203
|
|
| PRK11864 |
PRK11864 |
3-methyl-2-oxobutanoate dehydrogenase subunit beta; |
105-200 |
1.08e-06 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
Pssm-ID: 237005 [Multi-domain] Cd Length: 300 Bit Score: 48.93 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 105 AMRRNIDITYLVMDNHIYgLTTG-QTSPTSDKGSKTKTAPDGAVE--EPVhPLQMAlMAGCGFVAQGYSGNLKQLTELIE 181
Cdd:PRK11864 115 AAERNHDILYIMYDNEAY-MNTGiQRSSSTPYGAWTTTTPGGKREhkKPV-PDIMA-AHKVPYVATASIAYPEDFIRKLK 191
|
90
....*....|....*....
gi 1199122193 182 KGMQHRGFSLINIYSPCVT 200
Cdd:PRK11864 192 KAKEIRGFKFIHLLAPCPP 210
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
22-194 |
3.70e-06 |
|
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: 46.09 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 22 TVLAALQKAAvniglePEQMVTVSGVGCSGKIS----------QYMGSYGFHSLhGRSLPVATAVKLANRDLTVVA---- 87
Cdd:cd00568 1 RVLAALRAAL------PEDAIVVNDAGNSAYWAyrylplrrgrRFLTSTGFGAM-GYGLPAAIGAALAAPDRPVVCiagd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 88 --AGGDGDgygigmgHFIHAMRRNIDITYLVMDNHIYGLT-TGQTSPTSDKGSKTK-TAPDGAveepvhplqmALMAGCG 163
Cdd:cd00568 74 ggFMMTGQ-------ELATAVRYGLPVIVVVFNNGGYGTIrMHQEAFYGGRVSGTDlSNPDFA----------ALAEAYG 136
|
170 180 190
....*....|....*....|....*....|..
gi 1199122193 164 fvAQGYSGN-LKQLTELIEKGMQHRGFSLINI 194
Cdd:cd00568 137 --AKGVRVEdPEDLEAALAEALAAGGPALIEV 166
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
12-198 |
2.82e-05 |
|
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: 43.81 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 12 PNWCPGCGDFTVLAALQKAAvniglEPEQMVTvSGVGCS--GKISQYMGSYGFHSLhGRSLPVATAVKLANRDLTVVAAG 89
Cdd:cd02008 4 PGLCPGCPHRPSFYALRKAF-----KKDSIVS-GDIGCYtlGALPPLNAIDTCTCM-GASIGVAIGMAKASEDKKVVAVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 90 GDGDgygigmghFIH--------AMRRNIDITYLVMDNHIYGLTTGQTSPTsdkgsktkTAPDGAVEEPVHPLQMALMA- 160
Cdd:cd02008 77 GDST--------FFHsgilglinAVYNKANITVVILDNRTTAMTGGQPHPG--------TGKTLTEPTTVIDIEALVRAi 140
|
170 180 190
....*....|....*....|....*....|....*...
gi 1199122193 161 GCGFVAQGYSGNLKQLTELIEKGMQHRGFSLINIYSPC 198
Cdd:cd02008 141 GVKRVVVVDPYDLKAIREELKEALAVPGVSVIIAKRPC 178
|
|
| TPP_PFOR_PNO |
cd03377 |
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ... |
105-199 |
7.62e-05 |
|
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of proteins similar to the single subunit pyruvate ferredoxin oxidoreductase (PFOR) of Desulfovibrio Africanus, present in bacteria and amitochondriate eukaryotes. This subfamily also includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). These enzymes are dependent on TPP and a divalent metal cation as cofactors. PFOR and PNO catalyze 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 PFOR from cyanobacterium Anabaena (NifJ) is required for the transfer of electrons from pyruvate to flavodoxin, which reduces nitrogenase. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO.
Pssm-ID: 239472 Cd Length: 365 Bit Score: 43.75 E-value: 7.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1199122193 105 AMRRNIDItyLVMDNHIYGLTTGQTSPTSDKGSKTKTAPDGaveEPVHPLQMALMA---GCGFVAQ---GYSGN--LKQL 176
Cdd:cd03377 176 ASGENVNI--LVLDTEVYSNTGGQASKATPLGAVAKFAAAG---KRTGKKDLGMIAmsyGNVYVAQialGANDNqtLKAF 250
|
90 100
....*....|....*....|...
gi 1199122193 177 TELIEkgmqHRGFSLINIYSPCV 199
Cdd:cd03377 251 REAEA----YDGPSLIIAYSPCI 269
|
|
| |
