|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11869 |
PRK11869 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
15-292 |
1.95e-153 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183349 [Multi-domain] Cd Length: 280 Bit Score: 429.97 E-value: 1.95e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 15 ELDIAWCPGCGNFGILNILKKALEEMEeITPNNFVLVSGIGQAAKIPHYFKNNAFNGLHGRTLPVAFAIKATNPDLYVVA 94
Cdd:PRK11869 5 KYDIAWCPGCGNFGIRNALMKALSELN-LKPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTVIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 95 ESGDGDMYGEGGNHFIHNMRRNINITNIVHDNRVYGLTKGQASPTSQHGMVTPVQVNGVILNPFNPIAVAIANGATFVAR 174
Cdd:PRK11869 84 EGGDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASFVAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 175 AFVGDMQNTKEVIKKAIRHNGYALIDLFQPCVTFNKINTYAWFNEHTYKLgEDYDPSDKIQALQIAFQEDKIPLGIIYEE 254
Cdd:PRK11869 164 TFSGDIEETKEILKEAIKHKGLAIVDIFQPCVSFNKVNTYQWYRENTYYL-KDHDPTDRELAFKRALETEKLPLGIFYIN 242
|
250 260 270
....*....|....*....|....*....|....*...
gi 160359581 255 KsKPTFEEQLTIYKQNKDPLFKRSIDLNKLEDFINSMR 292
Cdd:PRK11869 243 E-KPTFEELVPAYKGDKTPLWKREPNFEKLKELIESKR 279
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
18-290 |
1.10e-130 |
|
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: 372.56 E-value: 1.10e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 18 IAWCPGCGNFGILNILKKALEEMEeITPNNFVLVSGIGQAAKIPHYFKNNAFNGLHGRTLPVAFAIKATNPDLYVVAESG 97
Cdd:TIGR02177 1 PDWCPGCGDFGILSALQRALAELN-LDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 98 DGDMYGEGGNHFIHNMRRNINITNIVHDNRVYGLTKGQASPTSQHGMVTPVQVNGVILNPFNPIAVAIANGATFVARAFV 177
Cdd:TIGR02177 80 DGDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 178 GDMQNTKEVIKKAIRHNGYALIDLFQPCVTFNKINTYAWFNEHTYKLGED-YDPSDK---------IQALQIAFQ-EDKI 246
Cdd:TIGR02177 160 GDVAHLKEIIKEAINHKGYALVDILQPCVTYNKINTYEWYRERVYKLDEEgYDPIVRepeefeekaAAAIKKAMEwGDRI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 160359581 247 PLGIIYEEKSKPTFEEQLTIYKQNK--DPLFKRSID--LNKLEDFINS 290
Cdd:TIGR02177 240 PIGIFYKNENKPTFEERLEKILPRYmsAPPAEQEIKppIEKPKELLEE 287
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
14-264 |
1.08e-118 |
|
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: 340.97 E-value: 1.08e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 14 KELDIAWCPGCGNFGILNILKKALEEMeeITPNNFVLVSGIGQAAKIPHYFKNNAFNGLHGRTLPVAFAIKATNPDLYVV 93
Cdd:COG1013 9 RTPGHRWCPGCGHGIILRLLLKALDEL--LDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANPDLTVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 94 AESGDGDMYGEGGNHFIHNMRRNINITNIVHDNRVYGLTKGQASPTSQHGMVTPVQVNGVILNPFNPIAVAIANGATFVA 173
Cdd:COG1013 87 VFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHGATYVA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 174 RAFVGDMQNTKEVIKKAIRHNGYALIDLFQPCVTFNKIN---TYAWFNEHTYKLgEDYDPSDKIQALQIAfqEDKIPLGI 250
Cdd:COG1013 167 RASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRDpskTIEWAKEGMWPL-YEYDPGEKLRLTYEP--KDKIPVGE 243
|
250
....*....|....
gi 160359581 251 IYEEKSKptFEEQL 264
Cdd:COG1013 244 FLKNQGR--FEELI 255
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
20-208 |
4.71e-115 |
|
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: 329.10 E-value: 4.71e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 20 WCPGCGNFGILNILKKALEEMEeITPNNFVLVSGIGQAAKIPHYFKNNAFNGLHGRTLPVAFAIKATNPDLYVVAESGDG 99
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELG-IDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 100 DMYGEGGNHFIHNMRRNINITNIVHDNRVYGLTKGQASPTSQHGMVTPVQVNGVILNPFNPIAVAIANGATFVARAFVGD 179
Cdd:cd03375 80 DLAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGD 159
|
170 180
....*....|....*....|....*....
gi 160359581 180 MQNTKEVIKKAIRHNGYALIDLFQPCVTF 208
Cdd:cd03375 160 IKQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
56-200 |
1.96e-33 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 119.61 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 56 QAAKIPHYFkNNAFNGLHGRTLPVAFAIKATNPDLYVVAESGDGDMYGEGgNHFIHNMRRNINITNIVHDNRVYGLTKGQ 135
Cdd:pfam02775 14 RFRPPRRYL-TSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNL-QELATAVRYNLPITVVVLNNGGYGMTRGQ 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160359581 136 ASPtsqHGMVTPVQVNGVILNPFNPIAVAIANGATFvarAFVGDMQNTKEVIKKAIRHNGYALID 200
Cdd:pfam02775 92 QTP---FGGGRYSGPSGKILPPVDFAKLAEAYGAKG---ARVESPEELEEALKEALEHDGPALID 150
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11869 |
PRK11869 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
15-292 |
1.95e-153 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183349 [Multi-domain] Cd Length: 280 Bit Score: 429.97 E-value: 1.95e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 15 ELDIAWCPGCGNFGILNILKKALEEMEeITPNNFVLVSGIGQAAKIPHYFKNNAFNGLHGRTLPVAFAIKATNPDLYVVA 94
Cdd:PRK11869 5 KYDIAWCPGCGNFGIRNALMKALSELN-LKPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTVIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 95 ESGDGDMYGEGGNHFIHNMRRNINITNIVHDNRVYGLTKGQASPTSQHGMVTPVQVNGVILNPFNPIAVAIANGATFVAR 174
Cdd:PRK11869 84 EGGDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASFVAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 175 AFVGDMQNTKEVIKKAIRHNGYALIDLFQPCVTFNKINTYAWFNEHTYKLgEDYDPSDKIQALQIAFQEDKIPLGIIYEE 254
Cdd:PRK11869 164 TFSGDIEETKEILKEAIKHKGLAIVDIFQPCVSFNKVNTYQWYRENTYYL-KDHDPTDRELAFKRALETEKLPLGIFYIN 242
|
250 260 270
....*....|....*....|....*....|....*...
gi 160359581 255 KsKPTFEEQLTIYKQNKDPLFKRSIDLNKLEDFINSMR 292
Cdd:PRK11869 243 E-KPTFEELVPAYKGDKTPLWKREPNFEKLKELIESKR 279
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
18-290 |
1.10e-130 |
|
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: 372.56 E-value: 1.10e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 18 IAWCPGCGNFGILNILKKALEEMEeITPNNFVLVSGIGQAAKIPHYFKNNAFNGLHGRTLPVAFAIKATNPDLYVVAESG 97
Cdd:TIGR02177 1 PDWCPGCGDFGILSALQRALAELN-LDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 98 DGDMYGEGGNHFIHNMRRNINITNIVHDNRVYGLTKGQASPTSQHGMVTPVQVNGVILNPFNPIAVAIANGATFVARAFV 177
Cdd:TIGR02177 80 DGDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 178 GDMQNTKEVIKKAIRHNGYALIDLFQPCVTFNKINTYAWFNEHTYKLGED-YDPSDK---------IQALQIAFQ-EDKI 246
Cdd:TIGR02177 160 GDVAHLKEIIKEAINHKGYALVDILQPCVTYNKINTYEWYRERVYKLDEEgYDPIVRepeefeekaAAAIKKAMEwGDRI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 160359581 247 PLGIIYEEKSKPTFEEQLTIYKQNK--DPLFKRSID--LNKLEDFINS 290
Cdd:TIGR02177 240 PIGIFYKNENKPTFEERLEKILPRYmsAPPAEQEIKppIEKPKELLEE 287
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
7-274 |
7.51e-128 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 365.32 E-value: 7.51e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 7 MFTLEN-EKELDIAWCPGCGNFGILNILKKALEEMEeITPNNFVLVSGIGQAAKIPHYFKNNAFNGLHGRTLPVAFAIKA 85
Cdd:PRK11867 5 MLTAKDfRNDQEPRWCPGCGDGSILAALQRALAELG-LDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGLKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 86 TNPDLYVVAESGDGDMYGEGGNHFIHNMRRNINITNIVHDNRVYGLTKGQASPTSQHGMVTPVQVNGVILNPFNPIAVAI 165
Cdd:PRK11867 84 ANPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVELAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 166 ANGATFVARAFVGDMQNTKEVIKKAIRHNGYALIDLFQPCVTFNKINTYAWFNEHTYKLG--EDYDPSDKIQALQIAFQE 243
Cdd:PRK11867 164 GAGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFNNVNTFDWFKERLVKVHdaEGYDPTNALAAMKTLEEG 243
|
250 260 270
....*....|....*....|....*....|.
gi 160359581 244 DKIPLGIIYEEkSKPTFEEQLTiyKQNKDPL 274
Cdd:PRK11867 244 DPIPTGIFYQV-ERPTYEEAVR--AQIEGPL 271
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
7-270 |
2.99e-127 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 364.20 E-value: 2.99e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 7 MFTLENEKELDIAWCPGCGNFGILNILKKALEEMEeITPNNFVLVSGIGQAAKIPHYFKNNAFNGLHGRTLPVAFAIKAT 86
Cdd:PRK05778 7 GLTYLRYDGLPTTWCPGCGNFGILNAIIQALAELG-LDPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 87 NPDLYVVAESGDGDMYGEGGNHFIHNMRRNINITNIVHDNRVYGLTKGQASPTSQHGMVTPVQVNGVILNPFNPIAVAIA 166
Cdd:PRK05778 86 NPDLEVIVVGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 167 NGATFVARAFVGDMQNTKEVIKKAIRHNGYALIDLFQPCVTFNKINTY--------AWFNEHTYKL--GEDYDPSDKIQA 236
Cdd:PRK05778 166 AGATFVARSFAGDVKQLVELIKKAISHKGFAFIDVLSPCVTFNGRNTStkspaymrEYYKKRVYKLklEEDYDPTDRDKA 245
|
250 260 270
....*....|....*....|....*....|....*..
gi 160359581 237 LQIAFQ---EDKIPLGIIYEEkSKPTFEEQLTIYKQN 270
Cdd:PRK05778 246 AEKMLEeelGGKIPIGVFYKN-ERPTFEERLEKLIEP 281
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
14-264 |
1.08e-118 |
|
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: 340.97 E-value: 1.08e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 14 KELDIAWCPGCGNFGILNILKKALEEMeeITPNNFVLVSGIGQAAKIPHYFKNNAFNGLHGRTLPVAFAIKATNPDLYVV 93
Cdd:COG1013 9 RTPGHRWCPGCGHGIILRLLLKALDEL--LDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANPDLTVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 94 AESGDGDMYGEGGNHFIHNMRRNINITNIVHDNRVYGLTKGQASPTSQHGMVTPVQVNGVILNPFNPIAVAIANGATFVA 173
Cdd:COG1013 87 VFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHGATYVA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 174 RAFVGDMQNTKEVIKKAIRHNGYALIDLFQPCVTFNKIN---TYAWFNEHTYKLgEDYDPSDKIQALQIAfqEDKIPLGI 250
Cdd:COG1013 167 RASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRDpskTIEWAKEGMWPL-YEYDPGEKLRLTYEP--KDKIPVGE 243
|
250
....*....|....
gi 160359581 251 IYEEKSKptFEEQL 264
Cdd:COG1013 244 FLKNQGR--FEELI 255
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
20-208 |
4.71e-115 |
|
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: 329.10 E-value: 4.71e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 20 WCPGCGNFGILNILKKALEEMEeITPNNFVLVSGIGQAAKIPHYFKNNAFNGLHGRTLPVAFAIKATNPDLYVVAESGDG 99
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELG-IDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 100 DMYGEGGNHFIHNMRRNINITNIVHDNRVYGLTKGQASPTSQHGMVTPVQVNGVILNPFNPIAVAIANGATFVARAFVGD 179
Cdd:cd03375 80 DLAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGD 159
|
170 180
....*....|....*....|....*....
gi 160359581 180 MQNTKEVIKKAIRHNGYALIDLFQPCVTF 208
Cdd:cd03375 160 IKQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
20-264 |
3.91e-114 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 330.18 E-value: 3.91e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 20 WCPGCGNFGILNILKKALEEMEeITPNNFVLVSGIGQAAKIPHYFKNNAFNGLHGRTLPVAFAIKATNPDLYVVAESGDG 99
Cdd:PRK11866 9 WCPGCGNYGILEALRKALAELG-IPPENVVVVSGIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLTVIGYGGDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 100 DMYGEGGNHFIHNMRRNINITNIVHDNRVYGLTKGQASPTSQHGMVTPVQVNGVILNPFNPIAVAIANGATFVARAFVGD 179
Cdd:PRK11866 88 DGYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATFVARGFSGD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 180 MQNTKEVIKKAIRHNGYALIDLFQPCVTFNKINTYAWFNEHTYKLGE-DYDPSDKIQALQIAFQ-EDKIPLGIIYEEKsK 257
Cdd:PRK11866 168 VKHLKEIIKEAIKHKGFSFIDVLSPCVTFNKLNTYDWFRPRVYKLEEtGHDPTNFEQAYKKALEwGDRIPIGVFYKEE-K 246
|
....*..
gi 160359581 258 PTFEEQL 264
Cdd:PRK11866 247 PTYEEEL 253
|
|
| oorB |
PRK09628 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; |
20-262 |
3.15e-47 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
Pssm-ID: 182003 [Multi-domain] Cd Length: 277 Bit Score: 159.51 E-value: 3.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 20 WCPGCGNFGILNILKKALEEMEeITPNNFVLVSGIGQAAKIPHYFKNNAFNGLHGRTLPVAFAIKATNPDLYVVAESGDG 99
Cdd:PRK09628 18 WCWGCGDGVILKSIIRAIDKLG-WNMDDVCVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGIKLANPDKHVIVVSGDG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 100 DMYGEGGNHFIHNMRRNINITNIVHDNRVYGLTKGQASPTSQHGMVTPVQVNGVILNPFNPIAVAIANGATFVARAFVGD 179
Cdd:PRK09628 97 DGLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKLATAAGASFVARESVID 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 180 MQNTKEVIKKAIRHNGYALIDLFQPC-VTFNKINTYA-------WFNEHTYklgedydPSDKIQALQIAFQEDKIPLGII 251
Cdd:PRK09628 177 PQKLEKLLVKGFSHKGFSFFDVFSNChINLGRKNKMGeavqmlkWIESRTV-------SKRKFDALSPEERVGKFPTGIL 249
|
250
....*....|.
gi 160359581 252 YEEKSKPTFEE 262
Cdd:PRK09628 250 KHDTDRKEYCE 260
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
56-200 |
1.96e-33 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 119.61 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 56 QAAKIPHYFkNNAFNGLHGRTLPVAFAIKATNPDLYVVAESGDGDMYGEGgNHFIHNMRRNINITNIVHDNRVYGLTKGQ 135
Cdd:pfam02775 14 RFRPPRRYL-TSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNL-QELATAVRYNLPITVVVLNNGGYGMTRGQ 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160359581 136 ASPtsqHGMVTPVQVNGVILNPFNPIAVAIANGATFvarAFVGDMQNTKEVIKKAIRHNGYALID 200
Cdd:pfam02775 92 QTP---FGGGRYSGPSGKILPPVDFAKLAEAYGAKG---ARVESPEELEEALKEALEHDGPALID 150
|
|
| PFO_beta_C |
pfam12367 |
Pyruvate ferredoxin oxidoreductase beta subunit C terminal; This domain family is found in ... |
205-264 |
5.04e-30 |
|
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: 107.96 E-value: 5.04e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160359581 205 CVTFNKINTYAWFNEHTYKLGEDYDPSDKIQALQIAFQ-EDKIPLGIIYEEkSKPTFEEQL 264
Cdd:pfam12367 1 CVTFNKVNTYDWYKERVYKLDEDHDPTDREAAMEKALEwGDRIPIGIFYKE-ERPTFEERL 60
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
37-201 |
1.74e-16 |
|
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: 75.37 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 37 LEEMEEITPNNFVLVSGIGQAAKIPHYFK---------NNAFNGLHGRTLPVAFAIKATNPDLYVVAESGDGDMyGEGGN 107
Cdd:cd00568 3 LAALRAALPEDAIVVNDAGNSAYWAYRYLplrrgrrflTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGF-MMTGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 108 HFIHNMRRNINITNIVHDNRVYGLTKGqasptsQHGMVTPVQVNGVILNPFNPIAVAIANGATFVARAFVGDMqntKEVI 187
Cdd:cd00568 82 ELATAVRYGLPVIVVVFNNGGYGTIRM------HQEAFYGGRVSGTDLSNPDFAALAEAYGAKGVRVEDPEDL---EAAL 152
|
170
....*....|....
gi 160359581 188 KKAIRHNGYALIDL 201
Cdd:cd00568 153 AEALAAGGPALIEV 166
|
|
| TPP_PFOR |
cd02018 |
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ... |
21-213 |
2.24e-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: 76.37 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 21 CPGCGNFGILNILKKALEEMEEItpnnfVLVSGIG----QAAKIPHYFKNNAF-NGLHGRTLPVAFAIKA-----TNPDL 90
Cdd:cd02018 8 CAGCGEVTAVRVVLAALPAPEDT-----VIANSTGcssvYASTAPFNSWAVPWvNSLFEDANAVASGLKRglkarFPKDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 91 Y------VVAESGDGDMYGEGGNHFIHNMRRNINITNIVHDNRVYGLTKGQASPTSQHGMVTPVQVNGVILNPFNPIAVA 164
Cdd:cd02018 83 EldkkkdVVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKKDLVLIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 160359581 165 IANGATFVARAFVGDMQNTKEVIKKAI-RHNGYALIDLFQPCVTFNKINT 213
Cdd:cd02018 163 ATHGCVYVARLSPALKKHFLKVVKEAIsRTDGPTFIHAYTPCITEWGIGS 212
|
|
| PRK11865 |
PRK11865 |
pyruvate synthase subunit beta; |
21-291 |
3.05e-13 |
|
pyruvate synthase subunit beta;
Pssm-ID: 183346 [Multi-domain] Cd Length: 299 Bit Score: 68.59 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 21 CPGCGNFGILNILKKALEEmeeitpnNFVLVSGIGQAAKIPHYFKNNAFNG--LHgrtlpVAF------------AIKAT 86
Cdd:PRK11865 21 CAGCGAAIAMRLALKALGK-------NTVIVVATGCLEVITTPYPETAWNVpwIH-----VAFenaaavasgierAVKAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 87 NPDLYVVAESGDGDMYGEGGNHFIHNMRRNINITNIVHDNRVYGLTKGQASPTSQHGMVTPVQVNGVIL-----NPFNPI 161
Cdd:PRK11865 89 GKKVNVVAIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKYSrgedrPKKNMP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 162 AVAIANGATFVARAFVGDMQNTKEVIKKAIRHNGYALIDLFQPCvtfnkinTYAWFnehtyklgedYDPSDKIQALQIAF 241
Cdd:PRK11865 169 LIMAAHGIPYVATASIGYPEDFMEKVKKAKEVEGPAYIQVLQPC-------PTGWG----------FPPEKTIEIGRLAV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 160359581 242 QEDKIPLGIIYEEKSKPTFeEQLTIYKQNKDPL---------FK--RSIDLNKLEDFINSM 291
Cdd:PRK11865 232 ETGYWPLFEIENGKFKITY-EPLHLDRRTRKPIeeylkvqgrFKhlTEEDIEILQKYIDEK 291
|
|
| TPP_PFOR_porB_like |
cd03376 |
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ... |
21-253 |
9.08e-12 |
|
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: 63.41 E-value: 9.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 21 CPGCGNFGILNILKKALEEmeeitpnNFVLVSGIG-----------QAAKIPHYfkNNAFNGLHGRTLPVAFAIKA-TNP 88
Cdd:cd03376 8 CAGCGAALALRHVLKALGP-------DTVVVNPTGclevittpypyTAWRVPWI--HVAFENAAAVASGIEAALKAlGRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 89 DLY-VVAESGDGDMYGEGGNHFIHNMRRNINITNIVHDNRVYGLTKGQASPTSQHGMVT---PV--QVNGVILNPFNPIA 162
Cdd:cd03376 79 KDItVVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTtttPVgkVSFGKKQPKKDLPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 163 VAIANGATFVARAFVGDMQNTKEVIKKAIRHNGYALIDLFQPCVTfnkintyawfnehtyklGEDYDPSDKIQALQIAFQ 242
Cdd:cd03376 159 IMAAHNIPYVATASVAYPEDLYKKVKKALSIEGPAYIHILSPCPT-----------------GWRFDPSKTIEIARLAVE 221
|
250
....*....|.
gi 160359581 243 EDKIPLgiiYE 253
Cdd:cd03376 222 TGFWPL---YE 229
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
71-199 |
1.08e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 48.29 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 71 GLHGRTLPVAFAIKATNPDLYVVAESGDGDMYGEGGNHFIHNMRRNINITNIVHDNRVYGLTKGQASPTSQHGMVtpvqv 150
Cdd:PRK06163 57 GSMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTIAALAPKNLTIIVMDNGVYQITGGQPTLTSQTVDV----- 131
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 160359581 151 ngvilnpfnpiaVAIANGATFVARAFVGDMQNTKEVIKKAIRHNGYALI 199
Cdd:PRK06163 132 ------------VAIARGAGLENSHWAADEAHFEALVDQALSGPGPSFI 168
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
36-200 |
3.22e-06 |
|
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: 48.23 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 36 ALEEMEEITPNNFVLVSGIGQ----AAkipHYFKNNAFNGLHGRT--------LPVAFAIKATNPDLYVVAESGDGDmyg 103
Cdd:COG0028 368 VIAALREALPDDAIVVTDVGQhqmwAA---RYLRFRRPRRFLTSGglgtmgygLPAAIGAKLARPDRPVVAITGDGG--- 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 104 eggnhFIHNM-------RRNINITNIVHDNRVYGLTKGQasptsQHgMVTPVQVNGVILNPFNPIAVAIANGATFVAraf 176
Cdd:COG0028 442 -----FQMNLqelatavRYGLPVKVVVLNNGGLGMVRQW-----QE-LFYGGRYSGTDLPNPDFAKLAEAFGAKGER--- 507
|
170 180
....*....|....*....|....
gi 160359581 177 VGDMQNTKEVIKKAIRHNGYALID 200
Cdd:COG0028 508 VETPEELEAALEEALASDGPALID 531
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
33-130 |
3.31e-06 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 48.33 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 33 LKKALEEMEEITPNNFVLVSGIGQAAKIPH-YFKNNAF-------NGLHGRTLPVAFAIKATNPDLYVVAESGDGD--MY 102
Cdd:PRK08199 369 LGEVMAWLRERLPADAIITNGAGNYATWLHrFFRFRRYrtqlaptSGSMGYGLPAAIAAKLLFPERTVVAFAGDGCflMN 448
|
90 100
....*....|....*....|....*...
gi 160359581 103 GEggnHFIHNMRRNINITNIVHDNRVYG 130
Cdd:PRK08199 449 GQ---ELATAVQYGLPIIVIVVNNGMYG 473
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
39-201 |
5.62e-06 |
|
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238960 [Multi-domain] Cd Length: 178 Bit Score: 45.66 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 39 EMEEITPNNFVLVS-GIGQAAKIPHYFKNNAFNGLHGRT-------LPVAFAIKATNPDLYVVAESGDGD-MYGeggnhf 109
Cdd:cd02002 9 ALAAALPEDAIIVDeAVTNGLPLRDQLPLTRPGSYFTLRggglgwgLPAAVGAALANPDRKVVAIIGDGSfMYT------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 110 IHNM----RRNINITNIVHDNRVYGLTKGQASPTSQHGMVTPVQVNGVILNPfNPIAVAIANGATFVARaFVGDMQNTKE 185
Cdd:cd02002 83 IQALwtaaRYGLPVTVVILNNRGYGALRSFLKRVGPEGPGENAPDGLDLLDP-GIDFAAIAKAFGVEAE-RVETPEELDE 160
|
170
....*....|....*.
gi 160359581 186 VIKKAIRHNGYALIDL 201
Cdd:cd02002 161 ALREALAEGGPALIEV 176
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
35-200 |
5.36e-05 |
|
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding module; composed of proteins similar to the large catalytic subunit of AHAS. AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate. 2-Acetolactate is the precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. In addition to requiring TPP and a divalent metal ion as cofactors, AHAS requires FAD.
Pssm-ID: 238973 [Multi-domain] Cd Length: 186 Bit Score: 42.87 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 35 KALEEMEEITPNNFVLVSGIGQ----AAkipHYFKNNAFNGLH--------GRTLPVAFAIKATNPDLYVVAESGDGDmy 102
Cdd:cd02015 5 EVIKELSELTPGDAIVTTDVGQhqmwAA---QYYRFKKPRSWLtsgglgtmGFGLPAAIGAKVARPDKTVICIDGDGS-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 103 geggnhFIHNM-------RRNINITNIVHDNRVYgltkgqasptsqhGMVTPVQV---NGVI---LNPFNPIAVAIANGa 169
Cdd:cd02015 80 ------FQMNIqelataaQYNLPVKIVILNNGSL-------------GMVRQWQElfyEGRYshtTLDSNPDFVKLAEA- 139
|
170 180 190
....*....|....*....|....*....|..
gi 160359581 170 tFVARAF-VGDMQNTKEVIKKAIRHNGYALID 200
Cdd:cd02015 140 -YGIKGLrVEKPEELEAALKEALASDGPVLLD 170
|
|
| PRK11864 |
PRK11864 |
3-methyl-2-oxobutanoate dehydrogenase subunit beta; |
19-274 |
1.07e-04 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
Pssm-ID: 237005 [Multi-domain] Cd Length: 300 Bit Score: 43.16 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 19 AWCPGCGNFGILNILKKALEEmeeitpnNFVLVSGIGQAAKIPhyfKNNAFNGLHGRTLPVAF------------AIKAT 86
Cdd:PRK11864 19 AACPGCGAPLGLRYLLKALGE-------KTVLVIPASCSTVIQ---GDTPKSPLTVPVLHTAFaataavasgieeALKAR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 87 NPDLYVVAE-SGDGDMYGEGGNHFIHNMRRNINITNIVHDNRVYGLTKGQASPTSQHGMVTPVQVNGVILNPFNPIAVAI 165
Cdd:PRK11864 89 GEKGVIVVGwAGDGGTADIGFQALSGAAERNHDILYIMYDNEAYMNTGIQRSSSTPYGAWTTTTPGGKREHKKPVPDIMA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 166 ANGATFVARAFVGDMQNTKEVIKKAIRHNGYALIDLFQPCVTfnkintyawfnehtyklGEDYDPSDKIQALQIAFQEDK 245
Cdd:PRK11864 169 AHKVPYVATASIAYPEDFIRKLKKAKEIRGFKFIHLLAPCPP-----------------GWRFDPDKTIEIARLAVETGV 231
|
250 260
....*....|....*....|....*....
gi 160359581 246 IPLGIIYEEKSKPTFEEQLTIYKQNKDPL 274
Cdd:PRK11864 232 WPLFEYENGKFKLNSPSKTLLDKKKRKPV 260
|
|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
34-133 |
4.06e-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: 40.57 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 34 KKALEEMEEITPNNFVLVSGIG----QAAKIPHYFKNNAF-----NGLHGRTLPVAFAIKATNPDLYVVAESGDGdMYGE 104
Cdd:cd02013 7 RQVLRELEKAMPEDAIVSTDIGnicsVANSYLRFEKPRSFiaplsFGNCGYALPAIIGAKAAAPDRPVVAIAGDG-AWGM 85
|
90 100
....*....|....*....|....*....
gi 160359581 105 GGNHFIHNMRRNINITNIVHDNRVYGLTK 133
Cdd:cd02013 86 SMMEIMTAVRHKLPVTAVVFRNRQWGAEK 114
|
|
| TPP_PFOR_PNO |
cd03377 |
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ... |
97-206 |
1.13e-03 |
|
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: 39.89 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 97 GDGDMY--GEGG-NHFIHNmRRNINItnIVHDNRVYGLTKGQASPTSQHGMVTPVQVNGVILNPFNPIAVAIANGATFVA 173
Cdd:cd03377 159 GDGWAYdiGYGGlDHVLAS-GENVNI--LVLDTEVYSNTGGQASKATPLGAVAKFAAAGKRTGKKDLGMIAMSYGNVYVA 235
|
90 100 110
....*....|....*....|....*....|....
gi 160359581 174 R-AFVGDMQNTKEVIKKAIRHNGYALIDLFQPCV 206
Cdd:cd03377 236 QiALGANDNQTLKAFREAEAYDGPSLIIAYSPCI 269
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
77-200 |
5.45e-03 |
|
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; composed of proteins similar to Lactobacillus plantarum POX, which plays a key role in controlling acetate production under aerobic conditions. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. It requires FAD in addition to TPP and a divalent cation as cofactors.
Pssm-ID: 238972 [Multi-domain] Cd Length: 178 Bit Score: 37.12 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 77 LPVAFAIKATNPDLYVVAESGDGDM---YGEggnhFIHNMRRNINITNIVHDNRVYgltkgqasptsqhGMVTPVQVngV 153
Cdd:cd02014 57 LPGAIAAKLAYPDRQVIALSGDGGFamlMGD----LITAVKYNLPVIVVVFNNSDL-------------GFIKWEQE--V 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 160359581 154 ILNPFNPIAVAIANGATFvARA------FVGDMQNTKEVIKKAIRHNGYALID 200
Cdd:cd02014 118 MGQPEFGVDLPNPDFAKI-AEAmgikgiRVEDPDELEAALDEALAADGPVVID 169
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|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
21-205 |
6.29e-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: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 21 CPGCGNFGILNILKKAleemeeITPNNFVLvSGIGqaakiPHYFKNNA-FNGLHGRT-----LPVAFAIKATNPDLYVVA 94
Cdd:cd02008 7 CPGCPHRPSFYALRKA------FKKDSIVS-GDIG-----CYTLGALPpLNAIDTCTcmgasIGVAIGMAKASEDKKVVA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160359581 95 ESGDGDMYGEGGNHFIHNMRRNINITNIVHDNRVYGLTKGQASPTSQHGMVTPVQVngvilnpFNPIAVAIANGATFVAR 174
Cdd:cd02008 75 VIGDSTFFHSGILGLINAVYNKANITVVILDNRTTAMTGGQPHPGTGKTLTEPTTV-------IDIEALVRAIGVKRVVV 147
|
170 180 190
....*....|....*....|....*....|.
gi 160359581 175 AFVGDMQNTKEVIKKAIRHNGYALIDLFQPC 205
Cdd:cd02008 148 VDPYDLKAIREELKEALAVPGVSVIIAKRPC 178
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