|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
1-281 |
2.15e-119 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 343.36 E-value: 2.15e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 1 MATMKDLRGDVST-WCPGCGHFSVMAGIQKAIVELGYEPHEFAIISGIGCSGKVSEYIRSNGFHTIHGRSLPVAQGVKMG 79
Cdd:PRK11867 5 MLTAKDFRNDQEPrWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGLKLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 80 NPDLKVIASGGDGDGYGIGLGHFVHASRRNIDMSYIVMDNNIYGLTKGQTSPRSMHGFETKSAAASNKEYPVDPITTSIV 159
Cdd:PRK11867 85 NPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVELALG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 160 NGATFVAQGYSGNIKELSTILKRAIEHRGFSHVNIYSPCVTFNKINTYDYYKENLVSIEAPfETRDE-----AISAIREN 234
Cdd:PRK11867 165 AGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFNNVNTFDWFKERLVKVHDA-EGYDPtnalaAMKTLEEG 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 297143584 235 NGLVTGILYEESRDDFQTKlgtkfdMQSLESGPMDEELLKKVQKKFE 281
Cdd:PRK11867 244 DPIPTGIFYQVERPTYEEA------VRAQIEGPLALQDLLMGGDTWT 284
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
14-201 |
5.30e-97 |
|
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: 282.88 E-value: 5.30e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 14 WCPGCGHFSVMAGIQKAIVELGYEPHEFAIISGIGCSGKVSEYIRSNGFHTIHGRSLPVAQGVKMGNPDLKVIASGGDGD 93
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 94 GYGIGLGHFVHASRRNIDMSYIVMDNNIYGLTKGQTSPRSMHGFETKSAAASNKEYPVDPITTSIVNGATFVAQGYSGNI 173
Cdd:cd03375 81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160
|
170 180
....*....|....*....|....*...
gi 297143584 174 KELSTILKRAIEHRGFSHVNIYSPCVTF 201
Cdd:cd03375 161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
3-245 |
6.60e-94 |
|
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: 277.80 E-value: 6.60e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 3 TMKD-LRGDVSTWCPGCGHFSVMAGIQKAIVELGyEPHEFAIISGIGCSGKVSEYIRSNGFHTIHGRSLPVAQGVKMGNP 81
Cdd:COG1013 3 KKKDlLRTPGHRWCPGCGHGIILRLLLKALDELL-DGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 82 DLKVIA------------SggdgdgygiglgHFVHASRRNIDMSYIVMDNNIYGLTKGQTSPRSMHGFETKSAAASNKEY 149
Cdd:COG1013 82 DLTVIVfggdgdtydiggN------------HLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 150 PVDPITTSIVNGATFVAQGYSGNIKELSTILKRAIEHRGFSHVNIYSPCVTFNKIN---TYDYYKENLVSIEApFETRDE 226
Cdd:COG1013 150 PKDPAEIAAAHGATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRDpskTIEWAKEGMWPLYE-YDPGEK 228
|
250
....*....|....*....
gi 297143584 227 AISAIRENNGLVTGILYEE 245
Cdd:COG1013 229 LRLTYEPKDKIPVGEFLKN 247
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
14-254 |
8.93e-90 |
|
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: 268.17 E-value: 8.93e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 14 WCPGCGHFSVMAGIQKAIVELGYEPHEFAIISGIGCSGKVSEYIRSNGFHTIHGRSLPVAQGVKMGNPDLKVIASGGDGD 93
Cdd:TIGR02177 3 WCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGDGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 94 GYGIGLGHFVHASRRNIDMSYIVMDNNIYGLTKGQTSPRSMHGFETKSAAASNKEYPVDPITTSIVNGATFVAQGYSGNI 173
Cdd:TIGR02177 83 LYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSGDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 174 KELSTILKRAIEHRGFSHVNIYSPCVTFNKINTYDYYKENLVSIE---------APFETRDEAISAIRE----NNGLVTG 240
Cdd:TIGR02177 163 AHLKEIIKEAINHKGYALVDILQPCVTYNKINTYEWYRERVYKLDeegydpivrEPEEFEEKAAAAIKKamewGDRIPIG 242
|
250
....*....|....*
gi 297143584 241 ILY-EESRDDFQTKL 254
Cdd:TIGR02177 243 IFYkNENKPTFEERL 257
|
|
| Oxoac_fdxbeta_Archa |
NF041171 |
2-oxoacid:ferredoxin oxidoreductase subunit beta; |
14-212 |
4.43e-82 |
|
2-oxoacid:ferredoxin oxidoreductase subunit beta;
Pssm-ID: 469082 [Multi-domain] Cd Length: 296 Bit Score: 248.70 E-value: 4.43e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 14 WCPGCGHFSVMAGIQKAIVELGYEPHEFAIISGIGCSGKVSEYIRSNGFHTIHGRSLPVAQGVKMGNPDLKVIASGGDGD 93
Cdd:NF041171 5 WCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGDGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 94 GYGIGLGHFVHASRRNIDMSYIVMDNNIYGLTKGQTSPRSMHGFETKSAAASNKEYPVDPITTSIVNGATFVAQGYSGNI 173
Cdd:NF041171 85 LLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAYDV 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 297143584 174 KELSTILKRAIEHRGFSHVNIYSPCVTFNKINTYDYYKE 212
Cdd:NF041171 165 KHLKELIKAAIKHKGLAFIDVLQPCPTYNDINTKEWYDK 203
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
46-194 |
4.17e-24 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 94.96 E-value: 4.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 46 GIGCSGK-VSEYIRSN--------GFHTIHGRSLPVAQGVKMGNPDLKVIA-----SggdgdgYGIGLGHFVHASRRNID 111
Cdd:pfam02775 1 DIGCHQMwAAQYYRFRpprryltsGGLGTMGYGLPAAIGAKLARPDRPVVAiagdgG------FQMNLQELATAVRYNLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 112 MSYIVMDNNIYGLTKGQTSPrsmHGFETKSAAASNKEYPVDPITTSIVNGATFVaqgYSGNIKELSTILKRAIEHRGFSH 191
Cdd:pfam02775 75 ITVVVLNNGGYGMTRGQQTP---FGGGRYSGPSGKILPPVDFAKLAEAYGAKGA---RVESPEELEEALKEALEHDGPAL 148
|
...
gi 297143584 192 VNI 194
Cdd:pfam02775 149 IDV 151
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
1-281 |
2.15e-119 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 343.36 E-value: 2.15e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 1 MATMKDLRGDVST-WCPGCGHFSVMAGIQKAIVELGYEPHEFAIISGIGCSGKVSEYIRSNGFHTIHGRSLPVAQGVKMG 79
Cdd:PRK11867 5 MLTAKDFRNDQEPrWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGLKLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 80 NPDLKVIASGGDGDGYGIGLGHFVHASRRNIDMSYIVMDNNIYGLTKGQTSPRSMHGFETKSAAASNKEYPVDPITTSIV 159
Cdd:PRK11867 85 NPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVELALG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 160 NGATFVAQGYSGNIKELSTILKRAIEHRGFSHVNIYSPCVTFNKINTYDYYKENLVSIEAPfETRDE-----AISAIREN 234
Cdd:PRK11867 165 AGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFNNVNTFDWFKERLVKVHDA-EGYDPtnalaAMKTLEEG 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 297143584 235 NGLVTGILYEESRDDFQTKlgtkfdMQSLESGPMDEELLKKVQKKFE 281
Cdd:PRK11867 244 DPIPTGIFYQVERPTYEEA------VRAQIEGPLALQDLLMGGDTWT 284
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
1-256 |
7.24e-114 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 329.92 E-value: 7.24e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 1 MATMKDLRGDVSTWCPGCGHFSVMAGIQKAIVELGYEPHEFAIISGIGCSGKVSEYIRSNGFHTIHGRSLPVAQGVKMGN 80
Cdd:PRK05778 7 GLTYLRYDGLPTTWCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLAN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 81 PDLKVIASGGDGDGYGIGLGHFVHASRRNIDMSYIVMDNNIYGLTKGQTSPRSMHGFETKSAAASNKEYPVDPITTSIVN 160
Cdd:PRK05778 87 PDLEVIVVGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 161 GATFVAQGYSGNIKELSTILKRAIEHRGFSHVNIYSPCVTFNKINTYD--------YYKENLVSIEAPFET----RDEAI 228
Cdd:PRK05778 167 GATFVARSFAGDVKQLVELIKKAISHKGFAFIDVLSPCVTFNGRNTSTkspaymreYYKKRVYKLKLEEDYdptdRDKAA 246
|
250 260 270
....*....|....*....|....*....|.
gi 297143584 229 SAIRE---NNGLVTGILYEESRDDFQTKLGT 256
Cdd:PRK05778 247 EKMLEeelGGKIPIGVFYKNERPTFEERLEK 277
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
14-201 |
5.30e-97 |
|
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: 282.88 E-value: 5.30e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 14 WCPGCGHFSVMAGIQKAIVELGYEPHEFAIISGIGCSGKVSEYIRSNGFHTIHGRSLPVAQGVKMGNPDLKVIASGGDGD 93
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 94 GYGIGLGHFVHASRRNIDMSYIVMDNNIYGLTKGQTSPRSMHGFETKSAAASNKEYPVDPITTSIVNGATFVAQGYSGNI 173
Cdd:cd03375 81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160
|
170 180
....*....|....*....|....*...
gi 297143584 174 KELSTILKRAIEHRGFSHVNIYSPCVTF 201
Cdd:cd03375 161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
3-245 |
6.60e-94 |
|
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: 277.80 E-value: 6.60e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 3 TMKD-LRGDVSTWCPGCGHFSVMAGIQKAIVELGyEPHEFAIISGIGCSGKVSEYIRSNGFHTIHGRSLPVAQGVKMGNP 81
Cdd:COG1013 3 KKKDlLRTPGHRWCPGCGHGIILRLLLKALDELL-DGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 82 DLKVIA------------SggdgdgygiglgHFVHASRRNIDMSYIVMDNNIYGLTKGQTSPRSMHGFETKSAAASNKEY 149
Cdd:COG1013 82 DLTVIVfggdgdtydiggN------------HLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 150 PVDPITTSIVNGATFVAQGYSGNIKELSTILKRAIEHRGFSHVNIYSPCVTFNKIN---TYDYYKENLVSIEApFETRDE 226
Cdd:COG1013 150 PKDPAEIAAAHGATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRDpskTIEWAKEGMWPLYE-YDPGEK 228
|
250
....*....|....*....
gi 297143584 227 AISAIRENNGLVTGILYEE 245
Cdd:COG1013 229 LRLTYEPKDKIPVGEFLKN 247
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
14-254 |
8.93e-90 |
|
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: 268.17 E-value: 8.93e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 14 WCPGCGHFSVMAGIQKAIVELGYEPHEFAIISGIGCSGKVSEYIRSNGFHTIHGRSLPVAQGVKMGNPDLKVIASGGDGD 93
Cdd:TIGR02177 3 WCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGDGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 94 GYGIGLGHFVHASRRNIDMSYIVMDNNIYGLTKGQTSPRSMHGFETKSAAASNKEYPVDPITTSIVNGATFVAQGYSGNI 173
Cdd:TIGR02177 83 LYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSGDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 174 KELSTILKRAIEHRGFSHVNIYSPCVTFNKINTYDYYKENLVSIE---------APFETRDEAISAIRE----NNGLVTG 240
Cdd:TIGR02177 163 AHLKEIIKEAINHKGYALVDILQPCVTYNKINTYEWYRERVYKLDeegydpivrEPEEFEEKAAAAIKKamewGDRIPIG 242
|
250
....*....|....*
gi 297143584 241 ILY-EESRDDFQTKL 254
Cdd:TIGR02177 243 IFYkNENKPTFEERL 257
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
14-218 |
4.00e-89 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 266.24 E-value: 4.00e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 14 WCPGCGHFSVMAGIQKAIVELGYEPHEFAIISGIGCSGKVSEYIRSNGFHTIHGRSLPVAQGVKMGNPDLKVIASGGDGD 93
Cdd:PRK11866 9 WCPGCGNYGILEALRKALAELGIPPENVVVVSGIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLTVIGYGGDGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 94 GYGIGLGHFVHASRRNIDMSYIVMDNNIYGLTKGQTSPRSMHGFETKSAAASNKEYPVDPITTSIVNGATFVAQGYSGNI 173
Cdd:PRK11866 89 GYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATFVARGFSGDV 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 297143584 174 KELSTILKRAIEHRGFSHVNIYSPCVTFNKINTYDYYKENLVSIE 218
Cdd:PRK11866 169 KHLKEIIKEAIKHKGFSFIDVLSPCVTFNKLNTYDWFRPRVYKLE 213
|
|
| Oxoac_fdxbeta_Archa |
NF041171 |
2-oxoacid:ferredoxin oxidoreductase subunit beta; |
14-212 |
4.43e-82 |
|
2-oxoacid:ferredoxin oxidoreductase subunit beta;
Pssm-ID: 469082 [Multi-domain] Cd Length: 296 Bit Score: 248.70 E-value: 4.43e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 14 WCPGCGHFSVMAGIQKAIVELGYEPHEFAIISGIGCSGKVSEYIRSNGFHTIHGRSLPVAQGVKMGNPDLKVIASGGDGD 93
Cdd:NF041171 5 WCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGDGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 94 GYGIGLGHFVHASRRNIDMSYIVMDNNIYGLTKGQTSPRSMHGFETKSAAASNKEYPVDPITTSIVNGATFVAQGYSGNI 173
Cdd:NF041171 85 LLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAYDV 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 297143584 174 KELSTILKRAIEHRGFSHVNIYSPCVTFNKINTYDYYKE 212
Cdd:NF041171 165 KHLKELIKAAIKHKGLAFIDVLQPCPTYNDINTKEWYDK 203
|
|
| PRK11869 |
PRK11869 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
10-254 |
5.15e-77 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183349 [Multi-domain] Cd Length: 280 Bit Score: 235.45 E-value: 5.15e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 10 DVStWCPGCGHFSVMAGIQKAIVELGYEPHEFAIISGIGCSGKVSEYIRSNGFHTIHGRSLPVAQGVKMGNPDLKVIASG 89
Cdd:PRK11869 7 DIA-WCPGCGNFGIRNALMKALSELNLKPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTVIAEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 90 GDGDGYGIGLGHFVHASRRNIDMSYIVMDNNIYGLTKGQTSPRSMHGFETKSAAASNKEYPVDPITTSIVNGATFVAQGY 169
Cdd:PRK11869 86 GDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASFVARTF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 170 SGNIKELSTILKRAIEHRGFSHVNIYSPCVTFNKINTYDYYKENLVSIEA--PFEtRDEAISAIRENNGLVTGILYEESR 247
Cdd:PRK11869 166 SGDIEETKEILKEAIKHKGLAIVDIFQPCVSFNKVNTYQWYRENTYYLKDhdPTD-RELAFKRALETEKLPLGIFYINEK 244
|
....*..
gi 297143584 248 DDFQTKL 254
Cdd:PRK11869 245 PTFEELV 251
|
|
| oorB |
PRK09628 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; |
14-245 |
1.48e-49 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
Pssm-ID: 182003 [Multi-domain] Cd Length: 277 Bit Score: 164.90 E-value: 1.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 14 WCPGCGHFSVMAGIQKAIVELGYEPHEFAIISGIGCSGKVSEYIRSNGFHTIHGRSLPVAQGVKMGNPDLKVIASGGDGD 93
Cdd:PRK09628 18 WCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGIKLANPDKHVIVVSGDGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 94 GYGIGLGHFVHASRRNIDMSYIVMDNNIYGLTKGQTSPRSMHGFETKSAAASNKEYPVDPITTSIVNGATFVAQGYSGNI 173
Cdd:PRK09628 98 GLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKLATAAGASFVARESVIDP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 297143584 174 KELSTILKRAIEHRGFSHVNIYSPC-VTFNKINTYDYYKENLVSIEAPF--ETRDEAISAIRENNGLVTGILYEE 245
Cdd:PRK09628 178 QKLEKLLVKGFSHKGFSFFDVFSNChINLGRKNKMGEAVQMLKWIESRTvsKRKFDALSPEERVGKFPTGILKHD 252
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
46-194 |
4.17e-24 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 94.96 E-value: 4.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 46 GIGCSGK-VSEYIRSN--------GFHTIHGRSLPVAQGVKMGNPDLKVIA-----SggdgdgYGIGLGHFVHASRRNID 111
Cdd:pfam02775 1 DIGCHQMwAAQYYRFRpprryltsGGLGTMGYGLPAAIGAKLARPDRPVVAiagdgG------FQMNLQELATAVRYNLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 112 MSYIVMDNNIYGLTKGQTSPrsmHGFETKSAAASNKEYPVDPITTSIVNGATFVaqgYSGNIKELSTILKRAIEHRGFSH 191
Cdd:pfam02775 75 ITVVVLNNGGYGMTRGQQTP---FGGGRYSGPSGKILPPVDFAKLAEAYGAKGA---RVESPEELEEALKEALEHDGPAL 148
|
...
gi 297143584 192 VNI 194
Cdd:pfam02775 149 IDV 151
|
|
| TPP_PFOR |
cd02018 |
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ... |
15-206 |
1.58e-15 |
|
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: 74.06 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 15 CPGCGHfsvmAGIQKAIVELGYEPHEFAIISGIGCSGKVSEYIRSNGF--HTIH---GRSLPVAQGVKMG---------- 79
Cdd:cd02018 8 CAGCGE----VTAVRVVLAALPAPEDTVIANSTGCSSVYASTAPFNSWavPWVNslfEDANAVASGLKRGlkarfpkdre 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 80 ---NPDLKVIASGGDGdgYGIGLGHFVHASRRNIDMSYIVMDNNIYGLTKGQTSPRSMHGFETKSAAASNKEYPVDPITT 156
Cdd:cd02018 84 ldkKKDVVVIGGDGAT--YDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKKDLVLI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 297143584 157 SIVNGATFVAQGYSGNIKELSTILKRAI-EHRGFSHVNIYSPCVTFNKINT 206
Cdd:cd02018 162 AATHGCVYVARLSPALKKHFLKVVKEAIsRTDGPTFIHAYTPCITEWGIGS 212
|
|
| PFO_beta_C |
pfam12367 |
Pyruvate ferredoxin oxidoreductase beta subunit C terminal; This domain family is found in ... |
198-255 |
8.54e-15 |
|
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: 67.52 E-value: 8.54e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 297143584 198 CVTFNKINTYDYYKENLVSIEAPFET--RDEAISAIREN-NGLVTGILYEESRDDFQTKLG 255
Cdd:pfam12367 1 CVTFNKVNTYDWYKERVYKLDEDHDPtdREAAMEKALEWgDRIPIGIFYKEERPTFEERLP 61
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
15-198 |
3.64e-06 |
|
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: 46.12 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 15 CPGCGH---FSVMAGIQKAIVelgyephefaIISG-IGCS--GKVSEYIRSNGFhTIHGRSLPVAQGVKMGNPDLKVIA- 87
Cdd:cd02008 7 CPGCPHrpsFYALRKAFKKDS----------IVSGdIGCYtlGALPPLNAIDTC-TCMGASIGVAIGMAKASEDKKVVAv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 88 ---SGgdgdgygiglghFVH--------ASRRNIDMSYIVMDNNIYGLTKGQTSPRSMHGFETKSaaasnkeyPVDPITT 156
Cdd:cd02008 76 igdST------------FFHsgilglinAVYNKANITVVILDNRTTAMTGGQPHPGTGKTLTEPT--------TVIDIEA 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 297143584 157 SI-VNGATFVAQGYSGNIKELSTILKRAIEHRGFSHVNIYSPC 198
Cdd:cd02008 136 LVrAIGVKRVVVVDPYDLKAIREELKEALAVPGVSVIIAKRPC 178
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
23-188 |
1.39e-05 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 44.55 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 23 VMAGIQKAIvelgyePHEFAIISGIGCSGKVS----EYIRSNGFHTIH-----GRSLPVAQGVKMGNPDLKVIA------ 87
Cdd:cd00568 2 VLAALRAAL------PEDAIVVNDAGNSAYWAyrylPLRRGRRFLTSTgfgamGYGLPAAIGAALAAPDRPVVCiagdgg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 88 ---SggdgdgygigLGHFVHASRRNIDMSYIVMDNNIYGLTKGQtsprsmHGFETKSAAASNKEYPVDPITtsivngatf 164
Cdd:cd00568 76 fmmT----------GQELATAVRYGLPVIVVVFNNGGYGTIRMH------QEAFYGGRVSGTDLSNPDFAA--------- 130
|
170 180 190
....*....|....*....|....*....|
gi 297143584 165 VAQGYSGN------IKELSTILKRAIEHRG 188
Cdd:cd00568 131 LAEAYGAKgvrvedPEDLEAALAEALAAGG 160
|
|
| PRK11864 |
PRK11864 |
3-methyl-2-oxobutanoate dehydrogenase subunit beta; |
105-200 |
1.19e-04 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
Pssm-ID: 237005 [Multi-domain] Cd Length: 300 Bit Score: 42.77 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 105 ASRRNIDMSYIVMDNNIYGLTKGQTSPRSMHGFETKSAAASNKEYPVDPITTSIVNGATFVAQGYSGNIKELSTILKRAI 184
Cdd:PRK11864 115 AAERNHDILYIMYDNEAYMNTGIQRSSSTPYGAWTTTTPGGKREHKKPVPDIMAAHKVPYVATASIAYPEDFIRKLKKAK 194
|
90
....*....|....*.
gi 297143584 185 EHRGFSHVNIYSPCVT 200
Cdd:PRK11864 195 EIRGFKFIHLLAPCPP 210
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
39-133 |
2.95e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 40.97 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 39 HEFAIISGIG-------CSGKvseyiRSNGFHTI--HGRSLPVAQGVKMGNPDLKVIASGGDGDGYGIGLGHFVHASRRN 109
Cdd:PRK06163 28 DEEAVIGGIGntnfdlwAAGQ-----RPQNFYMLgsMGLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTIAALAP 102
|
90 100
....*....|....*....|....
gi 297143584 110 IDMSYIVMDNNIYGLTKGQTSPRS 133
Cdd:PRK06163 103 KNLTIIVMDNGVYQITGGQPTLTS 126
|
|
| PRK11865 |
PRK11865 |
pyruvate synthase subunit beta; |
15-200 |
1.76e-03 |
|
pyruvate synthase subunit beta;
Pssm-ID: 183346 [Multi-domain] Cd Length: 299 Bit Score: 39.31 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 15 CPGCGHFSVMAGIQKAIVElgyephEFAIISGIGCSgkvsEYIRSNGFHT------IH---GRSLPVAQGV----KMGNP 81
Cdd:PRK11865 21 CAGCGAAIAMRLALKALGK------NTVIVVATGCL----EVITTPYPETawnvpwIHvafENAAAVASGIeravKALGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297143584 82 DLKVIASGGDGDGYGIGLGHFVHASRRNIDMSYIVMDNNIYGLTKGQTSPRSMHGFETKSAAASNKEYPVD------PIT 155
Cdd:PRK11865 91 KVNVVAIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKYSRGEDrpkknmPLI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 297143584 156 TsIVNGATFVAQGYSGNIKELSTILKRAIEHRGFSHVNIYSPCVT 200
Cdd:PRK11865 171 M-AAHGIPYVATASIGYPEDFMEKVKKAKEVEGPAYIQVLQPCPT 214
|
|
|