|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
14-348 |
4.00e-159 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 446.60 E-value: 4.00e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 14 KLKASDYASDQEPRWCPGCGDYSVLKQIHTVLAELGHKREDTAFISGIGCSSRLPYYMDTYGIHGIHGRATAIAEGLKIA 93
Cdd:PRK11867 5 MLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGLKLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 94 RPDINVWIATGDGDALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKGQFSPTSRVGQKTVTTPMGTIEYPVNAMAISLG 173
Cdd:PRK11867 85 NPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVELALG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 174 AGATFVARTIDRSPAQIRDIMLRADRHRGASLIEVYQNCPIF-NDGAFSIFTEKSTKtdstvileqdkplifgennnkgv 252
Cdd:PRK11867 165 AGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFnNVNTFDWFKERLVK----------------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 253 kldgtkpivvdlendnvsandlwIHDETDYVKASILARlfeMPSGEMNLPRPFGIFYAEDRFTYEDALDAQIKEAqakqk 332
Cdd:PRK11867 222 -----------------------VHDAEGYDPTNALAA---MKTLEEGDPIPTGIFYQVERPTYEEAVRAQIEGP----- 270
|
330
....*....|....*.
gi 193088675 333 ADLYELFKGATTWEIK 348
Cdd:PRK11867 271 LALQDLLMGGDTWTVL 286
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
28-215 |
4.32e-110 |
|
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: 318.70 E-value: 4.32e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 28 WCPGCGDYSVLKQIHTVLAELGHKREDTAFISGIGCSSRLPYYMDTYGIHGIHGRATAIAEGLKIARPDINVWIATGDGD 107
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 108 ALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKGQFSPTSRVGQKTVTTPMGTIEYPVNAMAISLGAGATFVARTIDRSP 187
Cdd:cd03375 81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160
|
170 180
....*....|....*....|....*...
gi 193088675 188 AQIRDIMLRADRHRGASLIEVYQNCPIF 215
Cdd:cd03375 161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
14-217 |
2.57e-101 |
|
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: 299.37 E-value: 2.57e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 14 KLKASDYASDQEPRWCPGCGDYSVLKQIHTVLAELGhKREDTAFISGIGCSSRLPYYMDTYGIHGIHGRATAIAEGLKIA 93
Cdd:COG1013 1 VLKKKDLLRTPGHRWCPGCGHGIILRLLLKALDELL-DGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 94 RPDINVWIATGDGDALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKGQFSPTSRVGQKTVTTPMGTIEYPVNAMAISLG 173
Cdd:COG1013 80 NPDLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 193088675 174 AGATFVARTIDRSPAQIRDIMLRADRHRGASLIEVYQNCPIFND 217
Cdd:COG1013 160 HGATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWG 203
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
26-217 |
6.31e-82 |
|
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: 250.84 E-value: 6.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 26 PRWCPGCGDYSVLKQIHTVLAELGHKREDTAFISGIGCSSRLPYYMDTYGIHGIHGRATAIAEGLKIARPDINVWIATGD 105
Cdd:TIGR02177 1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 106 GDALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKGQFSPTSRVGQKTVTTPMGTIEYPVNAMAISLGAGATFVARTIDR 185
Cdd:TIGR02177 81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160
|
170 180 190
....*....|....*....|....*....|..
gi 193088675 186 SPAQIRDIMLRADRHRGASLIEVYQNCPIFND 217
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNK 192
|
|
| Oxoac_fdxbeta_Archa |
NF041171 |
2-oxoacid:ferredoxin oxidoreductase subunit beta; |
28-224 |
2.23e-71 |
|
2-oxoacid:ferredoxin oxidoreductase subunit beta;
Pssm-ID: 469082 [Multi-domain] Cd Length: 296 Bit Score: 224.05 E-value: 2.23e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 28 WCPGCGDYSVLKQIHTVLAELGHKREDTAFISGIGCSSRLPYYMDTYGIHGIHGRATAIAEGLKIARPDINVWIATGDGD 107
Cdd:NF041171 5 WCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGDGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 108 ALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKGQFSPTSRVGQKTVTTPMGTIEYPVNAMAISLGAGATFVARTIDRSP 187
Cdd:NF041171 85 LLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAYDV 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 193088675 188 AQIRDIMLRADRHRGASLIEVYQNCPIFNDgafsIFT 224
Cdd:NF041171 165 KHLKELIKAAIKHKGLAFIDVLQPCPTYND----INT 197
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
60-208 |
2.81e-31 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 115.38 E-value: 2.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 60 GIGCSS---------RLPYYMDTYGIHGIHGRATAIAEGLKIARPDINVWIATGDGDALAIgLNHFLQLLRRNLNVNVIL 130
Cdd:pfam02775 1 DIGCHQmwaaqyyrfRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMN-LQELATAVRYNLPITVVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 131 LNNEIYGLTKGQfspTSRVGQKTVTTPMGTIEYPVN--AMAISLGAGATFVartidRSPAQIRDIMLRADRHRGASLIEV 208
Cdd:pfam02775 80 LNNGGYGMTRGQ---QTPFGGGRYSGPSGKILPPVDfaKLAEAYGAKGARV-----ESPEELEEALKEALEHDGPALIDV 151
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
14-348 |
4.00e-159 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 446.60 E-value: 4.00e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 14 KLKASDYASDQEPRWCPGCGDYSVLKQIHTVLAELGHKREDTAFISGIGCSSRLPYYMDTYGIHGIHGRATAIAEGLKIA 93
Cdd:PRK11867 5 MLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGLKLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 94 RPDINVWIATGDGDALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKGQFSPTSRVGQKTVTTPMGTIEYPVNAMAISLG 173
Cdd:PRK11867 85 NPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVELALG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 174 AGATFVARTIDRSPAQIRDIMLRADRHRGASLIEVYQNCPIF-NDGAFSIFTEKSTKtdstvileqdkplifgennnkgv 252
Cdd:PRK11867 165 AGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFnNVNTFDWFKERLVK----------------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 253 kldgtkpivvdlendnvsandlwIHDETDYVKASILARlfeMPSGEMNLPRPFGIFYAEDRFTYEDALDAQIKEAqakqk 332
Cdd:PRK11867 222 -----------------------VHDAEGYDPTNALAA---MKTLEEGDPIPTGIFYQVERPTYEEAVRAQIEGP----- 270
|
330
....*....|....*.
gi 193088675 333 ADLYELFKGATTWEIK 348
Cdd:PRK11867 271 LALQDLLMGGDTWTVL 286
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
28-215 |
4.32e-110 |
|
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: 318.70 E-value: 4.32e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 28 WCPGCGDYSVLKQIHTVLAELGHKREDTAFISGIGCSSRLPYYMDTYGIHGIHGRATAIAEGLKIARPDINVWIATGDGD 107
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 108 ALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKGQFSPTSRVGQKTVTTPMGTIEYPVNAMAISLGAGATFVARTIDRSP 187
Cdd:cd03375 81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160
|
170 180
....*....|....*....|....*...
gi 193088675 188 AQIRDIMLRADRHRGASLIEVYQNCPIF 215
Cdd:cd03375 161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
14-217 |
2.57e-101 |
|
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: 299.37 E-value: 2.57e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 14 KLKASDYASDQEPRWCPGCGDYSVLKQIHTVLAELGhKREDTAFISGIGCSSRLPYYMDTYGIHGIHGRATAIAEGLKIA 93
Cdd:COG1013 1 VLKKKDLLRTPGHRWCPGCGHGIILRLLLKALDELL-DGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 94 RPDINVWIATGDGDALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKGQFSPTSRVGQKTVTTPMGTIEYPVNAMAISLG 173
Cdd:COG1013 80 NPDLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 193088675 174 AGATFVARTIDRSPAQIRDIMLRADRHRGASLIEVYQNCPIFND 217
Cdd:COG1013 160 HGATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWG 203
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
28-335 |
3.71e-94 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 282.54 E-value: 3.71e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 28 WCPGCGDYSVLKQIHTVLAELGHKREDTAFISGIGCSSRLPYYMDTYGIHGIHGRATAIAEGLKIARPDINVWIATGDGD 107
Cdd:PRK05778 20 WCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLANPDLEVIVVGGDGD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 108 ALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKGQFSPTSRVGQKTVTTPMGTIEYPVNAMAISLGAGATFVARTIDRSP 187
Cdd:PRK05778 100 LASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAAGATFVARSFAGDV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 188 AQIRDIMLRADRHRGASLIEVYQNCPIFNDgafsIFTekSTKTDSTVILeqdkpliFGENNnkgvkldgtkpiVVDLEND 267
Cdd:PRK05778 180 KQLVELIKKAISHKGFAFIDVLSPCVTFNG----RNT--STKSPAYMRE-------YYKKR------------VYKLKLE 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193088675 268 NVsandlwiHDETDYVKAsiLARLFEMPSGEMnlpRPFGIFYAEDRFTYEDALDAQIKEAQAKQKADL 335
Cdd:PRK05778 235 ED-------YDPTDRDKA--AEKMLEEELGGK---IPIGVFYKNERPTFEERLEKLIEPLLELPPAAL 290
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
20-327 |
2.26e-85 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 259.30 E-value: 2.26e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 20 YASDQEPRWCPGCGDYSVLKQIHTVLAELGHKREDTAFISGIGCSSRLPYYMDTYGIHGIHGRATAIAEGLKIARPDINV 99
Cdd:PRK11866 1 YAVKRPPIWCPGCGNYGILEALRKALAELGIPPENVVVVSGIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 100 WIATGDGDALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKGQFSPTSRVGQKTVTTPMGTIEYPVNAMAISLGAGATFV 179
Cdd:PRK11866 81 IGYGGDGDGYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 180 ARTIDRSPAQIRDIMLRADRHRGASLIEVYQNCPIFND-GAFSIFTEKstktdstvileqdkplifgennnkgvkldgtk 258
Cdd:PRK11866 161 ARGFSGDVKHLKEIIKEAIKHKGFSFIDVLSPCVTFNKlNTYDWFRPR-------------------------------- 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193088675 259 piVVDLENDNvsandlwiHDETDYVKASILArlFEMPSgemnlPRPFGIFYAEDRFTYEDALDAQIKEA 327
Cdd:PRK11866 209 --VYKLEETG--------HDPTNFEQAYKKA--LEWGD-----RIPIGVFYKEEKPTYEEELDEILKNP 260
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
26-217 |
6.31e-82 |
|
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: 250.84 E-value: 6.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 26 PRWCPGCGDYSVLKQIHTVLAELGHKREDTAFISGIGCSSRLPYYMDTYGIHGIHGRATAIAEGLKIARPDINVWIATGD 105
Cdd:TIGR02177 1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 106 GDALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKGQFSPTSRVGQKTVTTPMGTIEYPVNAMAISLGAGATFVARTIDR 185
Cdd:TIGR02177 81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160
|
170 180 190
....*....|....*....|....*....|..
gi 193088675 186 SPAQIRDIMLRADRHRGASLIEVYQNCPIFND 217
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNK 192
|
|
| Oxoac_fdxbeta_Archa |
NF041171 |
2-oxoacid:ferredoxin oxidoreductase subunit beta; |
28-224 |
2.23e-71 |
|
2-oxoacid:ferredoxin oxidoreductase subunit beta;
Pssm-ID: 469082 [Multi-domain] Cd Length: 296 Bit Score: 224.05 E-value: 2.23e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 28 WCPGCGDYSVLKQIHTVLAELGHKREDTAFISGIGCSSRLPYYMDTYGIHGIHGRATAIAEGLKIARPDINVWIATGDGD 107
Cdd:NF041171 5 WCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGDGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 108 ALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKGQFSPTSRVGQKTVTTPMGTIEYPVNAMAISLGAGATFVARTIDRSP 187
Cdd:NF041171 85 LLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAYDV 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 193088675 188 AQIRDIMLRADRHRGASLIEVYQNCPIFNDgafsIFT 224
Cdd:NF041171 165 KHLKELIKAAIKHKGLAFIDVLQPCPTYND----INT 197
|
|
| PRK11869 |
PRK11869 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
23-327 |
1.12e-61 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183349 [Multi-domain] Cd Length: 280 Bit Score: 198.47 E-value: 1.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 23 DQEPRWCPGCGDYSVLKQIHTVLAELGHKREDTAFISGIGCSSRLPYYMDTYGIHGIHGRATAIAEGLKIARPDINVWIA 102
Cdd:PRK11869 5 KYDIAWCPGCGNFGIRNALMKALSELNLKPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTVIAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 103 TGDGDALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKGQFSPTSRVGQKTVTTPMGTIEYPVNAMAISLGAGATFVART 182
Cdd:PRK11869 85 GGDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASFVART 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 183 IDRSPAQIRDIMLRADRHRGASLIEVYQNCPIFND-GAFSIFTEkstktdstvileqdkplifgennnkgvkldgtkpiv 261
Cdd:PRK11869 165 FSGDIEETKEILKEAIKHKGLAIVDIFQPCVSFNKvNTYQWYRE------------------------------------ 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193088675 262 vdlendnvsaNDLWI--HDETDYVKAsiLARLFEmpsgemNLPRPFGIFYAEDRFTYEDALDAQIKEA 327
Cdd:PRK11869 209 ----------NTYYLkdHDPTDRELA--FKRALE------TEKLPLGIFYINEKPTFEELVPAYKGDK 258
|
|
| oorB |
PRK09628 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; |
28-214 |
2.44e-55 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
Pssm-ID: 182003 [Multi-domain] Cd Length: 277 Bit Score: 182.24 E-value: 2.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 28 WCPGCGDYSVLKQIHTVLAELGHKREDTAFISGIGCSSRLPYYMDTYGIHGIHGRATAIAEGLKIARPDINVWIATGDGD 107
Cdd:PRK09628 18 WCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGIKLANPDKHVIVVSGDGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 108 ALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKGQFSPTSRVGQKTVTTPMGTIEYPVNAMAISLGAGATFVARTIDRSP 187
Cdd:PRK09628 98 GLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKLATAAGASFVARESVIDP 177
|
170 180
....*....|....*....|....*..
gi 193088675 188 AQIRDIMLRADRHRGASLIEVYQNCPI 214
Cdd:PRK09628 178 QKLEKLLVKGFSHKGFSFFDVFSNCHI 204
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
60-208 |
2.81e-31 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 115.38 E-value: 2.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 60 GIGCSS---------RLPYYMDTYGIHGIHGRATAIAEGLKIARPDINVWIATGDGDALAIgLNHFLQLLRRNLNVNVIL 130
Cdd:pfam02775 1 DIGCHQmwaaqyyrfRPPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMN-LQELATAVRYNLPITVVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 131 LNNEIYGLTKGQfspTSRVGQKTVTTPMGTIEYPVN--AMAISLGAGATFVartidRSPAQIRDIMLRADRHRGASLIEV 208
Cdd:pfam02775 80 LNNGGYGMTRGQ---QTPFGGGRYSGPSGKILPPVDfaKLAEAYGAKGARV-----ESPEELEEALKEALEHDGPALIDV 151
|
|
| TPP_PFOR |
cd02018 |
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ... |
29-219 |
8.58e-23 |
|
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: 95.25 E-value: 8.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 29 CPGCGDYSVLKQIHTVLaelgHKREDTAFISGIGCSS-RLPYYMDT-YGIHGIHGR-------ATAIAEGLKIARPDI-- 97
Cdd:cd02018 8 CAGCGEVTAVRVVLAAL----PAPEDTVIANSTGCSSvYASTAPFNsWAVPWVNSLfedanavASGLKRGLKARFPKDre 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 98 -----NVWIATGDGDALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKGQFSPTSRVGQKTVTTPMGTIEYPVNAMAISL 172
Cdd:cd02018 84 ldkkkDVVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKKDLVLIAA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 193088675 173 GAGATFVARTIDRSPAQIRDIMLRAD-RHRGASLIEVYQNCPI---FNDGA 219
Cdd:cd02018 164 THGCVYVARLSPALKKHFLKVVKEAIsRTDGPTFIHAYTPCITewgIGSGK 214
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
43-208 |
1.60e-13 |
|
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: 67.67 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 43 TVLAELG-HKREDTAFISGIGCSS---------RLPYYMDTYGIHGIHGRATAIAEGLKIARPDINVWIATGDGDALAiG 112
Cdd:cd00568 1 RVLAALRaALPEDAIVVNDAGNSAywayrylplRRGRRFLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMM-T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 113 LNHFLQLLRRNLNVNVILLNNEIYGLTKGQfsptSRVGQKTVTTPMGTIEYPVNAMAISLGAGATFVartidRSPAQIRD 192
Cdd:cd00568 80 GQELATAVRYGLPVIVVVFNNGGYGTIRMH----QEAFYGGRVSGTDLSNPDFAALAEAYGAKGVRV-----EDPEDLEA 150
|
170
....*....|....*.
gi 193088675 193 IMLRADRHRGASLIEV 208
Cdd:cd00568 151 ALAEALAAGGPALIEV 166
|
|
| TPP_PFOR_porB_like |
cd03376 |
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ... |
27-213 |
6.07e-13 |
|
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: 67.65 E-value: 6.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 27 RWCPGCGDYSVLKQihtVLAELGhkrEDTAFISGIGCSSRL--PYYMDTYGIHGIH-----GRATA--IAEGLKI-ARP- 95
Cdd:cd03376 6 RACAGCGAALALRH---VLKALG---PDTVVVNPTGCLEVIttPYPYTAWRVPWIHvafenAAAVAsgIEAALKAlGRGk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 96 DINVWIATGDGDALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKGQFSPTSRVGQKTVTTPMGTI-----EYPVNAMAI 170
Cdd:cd03376 80 DITVVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTTPVGKVsfgkkQPKKDLPLI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 193088675 171 SLGAGATFVARTidrSPAQIRDIMLRADRHR---GASLIEVYQNCP 213
Cdd:cd03376 160 MAAHNIPYVATA---SVAYPEDLYKKVKKALsieGPAYIHILSPCP 202
|
|
| PRK11865 |
PRK11865 |
pyruvate synthase subunit beta; |
27-213 |
2.69e-12 |
|
pyruvate synthase subunit beta;
Pssm-ID: 183346 [Multi-domain] Cd Length: 299 Bit Score: 66.66 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 27 RWCPGCGDYSVLKQIhtvLAELGhkrEDTAFISGIGCSSRL--PYYMDTYGIHGIH-----GRATA--IAEGLKIARPDI 97
Cdd:PRK11865 19 RACAGCGAAIAMRLA---LKALG---KNTVIVVATGCLEVIttPYPETAWNVPWIHvafenAAAVAsgIERAVKALGKKV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 98 NVWIATGDGDALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKGQFSPTSRVGQKTVTTPMGTIEY----PVNAMAISLG 173
Cdd:PRK11865 93 NVVAIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKYSRgedrPKKNMPLIMA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 193088675 174 A-GATFVARTIDRSPAQIRDIMLRADRHRGASLIEVYQNCP 213
Cdd:PRK11865 173 AhGIPYVATASIGYPEDFMEKVKKAKEVEGPAYIQVLQPCP 213
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
35-208 |
3.31e-08 |
|
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of proteins similar to benzaldehyde lyase (BZL), oxalyl-CoA decarboxylase (OCoD) and 2-hydroxyphytanoyl-CoA lyase (2-HPCL). Pseudomonas fluorescens biovar I BZL cleaves the acyloin linkage of benzoin producing 2 molecules of benzaldehyde and enabling the Pseudomonas to grow on benzoin as the sole carbon and energy source. OCoD has a role in the detoxification of oxalate, catalyzing the decarboxylation of oxalyl-CoA to formate. 2-HPCL is a peroxisomal enzyme which plays a role in the alpha-oxidation of 3-methyl-branched fatty acids, catalyzing the cleavage of 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde. All these enzymes depend on Mg2+ and TPP for activity.
Pssm-ID: 238962 [Multi-domain] Cd Length: 172 Bit Score: 52.53 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 35 YSVLKQIHTVLAE---LGHKREDTAFISGIGCSSRLPY-YMD--TYGIHGIhGRATAIAegLKIARPDINVWIATGDGdA 108
Cdd:cd02004 2 YRVLHELQEALPDdaiIVSDGGNTMDWARYILRPRKPRhRLDagTFGTLGV-GLGYAIA--AALARPDKRVVLVEGDG-A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 109 LAIGLNHFLQLLRRNLNVNVILLNNE-IYGLTKGQfsPTSRVGQKTVTTPMGTIEYpvNAMAISLGAGATFVartidRSP 187
Cdd:cd02004 78 FGFSGMELETAVRYNLPIVVVVGNNGgWYQGLDGQ--QLSYGLGLPVTTLLPDTRY--DLVAEAFGGKGELV-----TTP 148
|
170 180
....*....|....*....|.
gi 193088675 188 AQIRDIMLRADRHRGASLIEV 208
Cdd:cd02004 149 EELKPALKRALASGKPALINV 169
|
|
| PRK11864 |
PRK11864 |
3-methyl-2-oxobutanoate dehydrogenase subunit beta; |
29-214 |
1.03e-07 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
Pssm-ID: 237005 [Multi-domain] Cd Length: 300 Bit Score: 52.79 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 29 CPGCGDYSVLKqihTVLAELGHKredTAFISGIGCSSRLPYYMDTYGI-----HGIHGRATAIAEGLKIA-----RPDIN 98
Cdd:PRK11864 21 CPGCGAPLGLR---YLLKALGEK---TVLVIPASCSTVIQGDTPKSPLtvpvlHTAFAATAAVASGIEEAlkargEKGVI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 99 VWIATGDGDALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKGQFSPTSRVGQKTVTTPMGTIEYPVNAMAISLGAGATF 178
Cdd:PRK11864 95 VVGWAGDGGTADIGFQALSGAAERNHDILYIMYDNEAYMNTGIQRSSSTPYGAWTTTTPGGKREHKKPVPDIMAAHKVPY 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 193088675 179 VARTidrSPAQIRDI---MLRADRHRGASLIEVYQNCPI 214
Cdd:PRK11864 175 VATA---SIAYPEDFirkLKKAKEIRGFKFIHLLAPCPP 210
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
75-208 |
1.14e-07 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 53.23 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 75 GIHGIhGRATAIAEGLKIARPDINVWIATGDGdalaiGLNHF---LQLLRR-NLNVNVILLNNEIYGLTKGqfSPTSRVG 150
Cdd:PRK06112 435 GLAGL-GWGVPMAIGAKVARPGAPVICLVGDG-----GFAHVwaeLETARRmGVPVTIVVLNNGILGFQKH--AETVKFG 506
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 193088675 151 QKTVTTPMGTIEYPvnAMAISLGAGATFVARtidrsPAQIRDIMLRADRHRGASLIEV 208
Cdd:PRK06112 507 THTDACHFAAVDHA--AIARACGCDGVRVED-----PAELAQALAAAMAAPGPTLIEV 557
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
85-208 |
4.16e-07 |
|
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: 51.31 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 85 AIaeGLKIARPDINVWIATGDGDalaiglnhFLQLL-------RRNLNVNVILLNNEIYGLTKGQFspTSRVGQKTVTTP 157
Cdd:COG0028 421 AI--GAKLARPDRPVVAITGDGG--------FQMNLqelatavRYGLPVKVVVLNNGGLGMVRQWQ--ELFYGGRYSGTD 488
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 193088675 158 MGTIEYPvnAMAISLGAgatfVARTIDRsPAQIRDIMLRADRHRGASLIEV 208
Cdd:COG0028 489 LPNPDFA--KLAEAFGA----KGERVET-PEELEAALEEALASDGPALIDV 532
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
26-212 |
4.90e-07 |
|
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: 49.20 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 26 PRWCPGC---GDYSVLKQIhtvlaelghKREDTAFISGIGCSSrLPYYMDTYGIHGI--HGRATAIAEGLKIARPDINVw 100
Cdd:cd02008 4 PGLCPGCphrPSFYALRKA---------FKKDSIVSGDIGCYT-LGALPPLNAIDTCtcMGASIGVAIGMAKASEDKKV- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 101 IAT-GDGDALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKGQFSPTSRVGQKTVTTPMGtIEypvnamAISLGAGATFV 179
Cdd:cd02008 73 VAViGDSTFFHSGILGLINAVYNKANITVVILDNRTTAMTGGQPHPGTGKTLTEPTTVID-IE------ALVRAIGVKRV 145
|
170 180 190
....*....|....*....|....*....|....
gi 193088675 180 aRTIDR-SPAQIRDIMLRADRHRGASLIEVYQNC 212
Cdd:cd02008 146 -VVVDPyDLKAIREELKEALAVPGVSVIIAKRPC 178
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
41-208 |
3.10e-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: 46.82 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 41 IHTVLAELGHKREDTAFISGIGCSSRLP------------YYMDTYGihGIhGRATAIAEGLKIARPDINVWIATGDGDA 108
Cdd:cd02002 3 PEYLAAALAAALPEDAIIVDEAVTNGLPlrdqlpltrpgsYFTLRGG--GL-GWGLPAAVGAALANPDRKVVAIIGDGSF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 109 L-AIglnhflQLL----RRNLNVNVILLNNEIYGLTKgqfSPTSRVGQKTVTTP---MGTIEYP-VNAMAISLGAGATfv 179
Cdd:cd02002 80 MyTI------QALwtaaRYGLPVTVVILNNRGYGALR---SFLKRVGPEGPGENapdGLDLLDPgIDFAAIAKAFGVE-- 148
|
170 180
....*....|....*....|....*....
gi 193088675 180 ARTIDRsPAQIRDIMLRADRHRGASLIEV 208
Cdd:cd02002 149 AERVET-PEELDEALREALAEGGPALIEV 176
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
44-149 |
2.16e-05 |
|
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed of proteins similar to sulfopyruvate decarboxylase beta subunit (ComE) and phosphonopyruvate decarboxylase (Ppyr decarboxylase). Methanococcus jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits which, catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. Ppyr decarboxylase is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. Ppyr decarboxylase and ComDE require TPP and divalent metal cation cofactors.
Pssm-ID: 238959 [Multi-domain] Cd Length: 157 Bit Score: 44.02 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 44 VLAELGHKREDTAFISGIGCSSRLPYYMDTYGIH----GIHGRATAIAEGLKIARPDiNVWIATGDGdALAIGLNHFLQL 119
Cdd:cd02001 4 AIAEIIEASGDTPIVSTTGYASRELYDVQDRDGHfymlGSMGLAGSIGLGLALGLSR-KVIVVDGDG-SLLMNPGVLLTA 81
|
90 100 110
....*....|....*....|....*....|.
gi 193088675 120 LRRN-LNVNVILLNNEIYGLTKGQFSPTSRV 149
Cdd:cd02001 82 GEFTpLNLILVVLDNRAYGSTGGQPTPSSNV 112
|
|
| TPP_PFOR_PNO |
cd03377 |
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ... |
99-212 |
2.21e-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: 45.67 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 99 VWIATGDGDALAI---GLNHFLQLlrrNLNVNVILLNNEIYGLTKGQFS---PTSRV------GQKTVTTPMGTIeypvn 166
Cdd:cd03377 154 VWIIGGDGWAYDIgygGLDHVLAS---GENVNILVLDTEVYSNTGGQASkatPLGAVakfaaaGKRTGKKDLGMI----- 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 193088675 167 AMA--------ISLGAgatfvartidrSPAQIRDIMLRADRHRGASLIEVYQNC 212
Cdd:cd03377 226 AMSygnvyvaqIALGA-----------NDNQTLKAFREAEAYDGPSLIIAYSPC 268
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
53-208 |
1.29e-04 |
|
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors.
Pssm-ID: 239468 [Multi-domain] Cd Length: 188 Bit Score: 42.30 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 53 EDTAFISGIGCSSR-LPYYMDTYGIH--------GIHGRATAIAEGLKIARPDINVWIATGDGDAL-------AIGlNHF 116
Cdd:cd03371 14 ATAAVVSTTGMTSReLFELRDRPGGGhaqdfltvGSMGHASQIALGIALARPDRKVVCIDGDGAALmhmgglaTIG-GLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 117 LQllrrnlNVNVILLNNEIYGLTKGQfsPTsrVGQKTVTTpmgtieypvnAMAISLGAGATFVARTIDrspaQIRDIMLR 196
Cdd:cd03371 93 PA------NLIHIVLNNGAHDSVGGQ--PT--VSFDVSLP----------AIAKACGYRAVYEVPSLE----ELVAALAK 148
|
170
....*....|..
gi 193088675 197 ADRHRGASLIEV 208
Cdd:cd03371 149 ALAADGPAFIEV 160
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
44-149 |
2.01e-04 |
|
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.
Pssm-ID: 239469 [Multi-domain] Cd Length: 179 Bit Score: 41.50 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 44 VLAELGHKREDTAFISGIGCSSR---------LPYYMdtygiHGIHGRATAIAEGLKIARPDiNVWIATGDGDALaIGLN 114
Cdd:cd03372 4 AIKTLIADLKDELVVSNIGFPSKelyaagdrpLNFYM-----LGSMGLASSIGLGLALAQPR-KVIVIDGDGSLL-MNLG 76
|
90 100 110
....*....|....*....|....*....|....*.
gi 193088675 115 HFLQLLRRN-LNVNVILLNNEIYGLTKGQFSPTSRV 149
Cdd:cd03372 77 ALATIAAEKpKNLIIVVLDNGAYGSTGNQPTHAGKK 112
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
52-208 |
5.81e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 40.58 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 52 REDTAFISGIG-------CSSRLP--YYMdtygiHGIHGRATAIAEGLKIARPDINVWIATGDGDALaiglnhfLQL--- 119
Cdd:PRK06163 27 KDEEAVIGGIGntnfdlwAAGQRPqnFYM-----LGSMGLAFPIALGVALAQPKRRVIALEGDGSLL-------MQLgal 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 120 ----LRRNLNVNVILLNNEIYGLTKGQFSPTSRVgqktvttpmgtieypVNAMAISLGAGATFVARTIDrsPAQIRDIML 195
Cdd:PRK06163 95 gtiaALAPKNLTIIVMDNGVYQITGGQPTLTSQT---------------VDVVAIARGAGLENSHWAAD--EAHFEALVD 157
|
170
....*....|...
gi 193088675 196 RADRHRGASLIEV 208
Cdd:PRK06163 158 QALSGPGPSFIAV 170
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
77-208 |
8.65e-04 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 41.13 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 77 HGIHGRATAIAEGL------KIARPDINVWIATGDGdALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKG----QFspt 146
Cdd:PRK07064 398 ANVHALGGGIGQGLamaigaALAGPGRKTVGLVGDG-GLMLNLGELATAVQENANMVIVLMNDGGYGVIRNiqdaQY--- 473
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193088675 147 srvGQKTVTTPMGTIEYPvnAMAISLGAGATFVartidRSPAQIRDIMLRADRHRGASLIEV 208
Cdd:PRK07064 474 ---GGRRYYVELHTPDFA--LLAASLGLPHWRV-----TSADDFEAVLREALAKEGPVLVEV 525
|
|
| PRK05858 |
PRK05858 |
acetolactate synthase; |
75-197 |
1.13e-03 |
|
acetolactate synthase;
Pssm-ID: 235629 [Multi-domain] Cd Length: 542 Bit Score: 40.86 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 75 GIHGIHGRATAIAEGLKIARPDINVWIATGDGdALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTKGqfsptsrvgqktv 154
Cdd:PRK05858 404 GPFGCLGTGPGYALAARLARPSRQVVLLQGDG-AFGFSLMDVDTLVRHNLPVVSVIGNNGIWGLEKH------------- 469
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 193088675 155 ttPMGTIE-YPVNA----------MAISLGAGATFVARtidrsPAQIRDIMLRA 197
Cdd:PRK05858 470 --PMEALYgYDVAAdlrpgtrydeVVRALGGHGELVTV-----PAELGPALERA 516
|
|
| PFO_beta_C |
pfam12367 |
Pyruvate ferredoxin oxidoreductase beta subunit C terminal; This domain family is found in ... |
261-321 |
1.64e-03 |
|
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: 36.32 E-value: 1.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193088675 261 VVDLENDnvsandlwiHDETDYVKAsiLARLFEMpsGEmnlPRPFGIFYAEDRFTYEDALD 321
Cdd:pfam12367 17 VYKLDED---------HDPTDREAA--MEKALEW--GD---RIPIGIFYKEERPTFEERLP 61
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
84-208 |
2.11e-03 |
|
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: 38.63 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 84 TAIaeGLKIARPDINVWIATGDGdalAIGLN-HFLQLLRR-NLNVNVILLNNEIYGLT--------KGQFSPTsrvgqkt 153
Cdd:cd02015 58 AAI--GAKVARPDKTVICIDGDG---SFQMNiQELATAAQyNLPVKIVILNNGSLGMVrqwqelfyEGRYSHT------- 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 193088675 154 vttpmgTIEYPVNAMAISLGAGAtfVARTIDrSPAQIRDIMLRADRHRGASLIEV 208
Cdd:cd02015 126 ------TLDSNPDFVKLAEAYGI--KGLRVE-KPEELEAALKEALASDGPVLLDV 171
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
76-208 |
2.64e-03 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 39.59 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193088675 76 IHGIHGRATAIAEGLKIARPDINVWIATGDGdALAIGLNHFLQLLRRNLNVNVILLNNEIYGLTK------GQfsPtsrv 149
Cdd:PRK06546 406 RHGSMANALPHAIGAQLADPGRQVISMSGDG-GLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVKlemlvdGL--P---- 478
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 193088675 150 gqktvttPMGTIEYPVNAMAISLGAGAtFVARTIDrsPAQIRDIMLRADRHRGASLIEV 208
Cdd:PRK06546 479 -------DFGTDHPPVDYAAIAAALGI-HAVRVED--PKDVRGALREAFAHPGPALVDV 527
|
|
| |
