|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
4-336 |
3.20e-148 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 418.86 E-value: 3.20e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 4 TTVEKYTFKDFTSDQEVRWCPGCDDYVILRSMQKALPEMGLKREDVVFISGIGCSSRFPYYMDTYGMHSIHGRATAVASG 83
Cdd:PRK11867 1 MTDPMLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 84 VKLANPKLSVWVVTGDGDSMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSPTSLVGQKTKSSPYGNTQPPFSPGE 163
Cdd:PRK11867 81 LKLANPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 164 LAIGAQARFFARIGGNTPKEMTELFIQAEKFKGTSLIEILQNCVIF-NDNCFVKYTDKDVRedkqlfvehgkpmifgknk 242
Cdd:PRK11867 161 LALGAGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFnNVNTFDWFKERLVK------------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 243 dkglvlnrlklevvtlgengitevdilVHDAKEQDPTLHQMLVRLE---YPLVTGIIRsfdDVTLEEREDALTAKVKAGS 319
Cdd:PRK11867 222 ---------------------------VHDAEGYDPTNALAAMKTLeegDPIPTGIFY---QVERPTYEEAVRAQIEGPL 271
|
330
....*....|....*..
gi 1309057203 320 NFtktDDLFFSGETYEI 336
Cdd:PRK11867 272 AL---QDLLMGGDTWTV 285
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
22-209 |
5.67e-114 |
|
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: 328.33 E-value: 5.67e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 22 WCPGCDDYVILRSMQKALPEMGLKREDVVFISGIGCSSRFPYYMDTYGMHSIHGRATAVASGVKLANPKLSVWVVTGDGD 101
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 102 SMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSPTSLVGQKTKSSPYGNTQPPFSPGELAIGAQARFFARIGGNTP 181
Cdd:cd03375 81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160
|
170 180
....*....|....*....|....*...
gi 1309057203 182 KEMTELFIQAEKFKGTSLIEILQNCVIF 209
Cdd:cd03375 161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
8-239 |
1.43e-107 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440637 [Multi-domain] Cd Length: 262 Bit Score: 314.77 E-value: 1.43e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 8 KYTFKDFTSDQEVRWCPGCDDYVILRSMQKALPEMgLKREDVVFISGIGCSSRFPYYMDTYGMHSIHGRATAVASGVKLA 87
Cdd:COG1013 1 VLKKKDLLRTPGHRWCPGCGHGIILRLLLKALDEL-LDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 88 NPKLSVWVVTGDGDSMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSPTSLVGQKTKSSPYGNTQPPFSPGELAIG 167
Cdd:COG1013 80 NPDLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 168 AQARFFARIGGNTPKEMTELFIQAEKFKGTSLIEILQNCVIFND-----------NCFVKYTDKDVREDKQLFVEHGKPM 236
Cdd:COG1013 160 HGATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGrdpsktiewakEGMWPLYEYDPGEKLRLTYEPKDKI 239
|
...
gi 1309057203 237 IFG 239
Cdd:COG1013 240 PVG 242
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
20-211 |
4.25e-85 |
|
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: 258.54 E-value: 4.25e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 20 VRWCPGCDDYVILRSMQKALPEMGLKREDVVFISGIGCSSRFPYYMDTYGMHSIHGRATAVASGVKLANPKLSVWVVTGD 99
Cdd:TIGR02177 1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 100 GDSMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSPTSLVGQKTKSSPYGNTQPPFSPGELAIGAQARFFARIGGN 179
Cdd:TIGR02177 81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160
|
170 180 190
....*....|....*....|....*....|..
gi 1309057203 180 TPKEMTELFIQAEKFKGTSLIEILQNCVIFND 211
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNK 192
|
|
| Oxoac_fdxbeta_Archa |
NF041171 |
2-oxoacid:ferredoxin oxidoreductase subunit beta; |
20-222 |
8.93e-77 |
|
2-oxoacid:ferredoxin oxidoreductase subunit beta;
Pssm-ID: 469082 [Multi-domain] Cd Length: 296 Bit Score: 237.53 E-value: 8.93e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 20 VRWCPGCDDYVILRSMQKALPEMGLKREDVVFISGIGCSSRFPYYMDTYGMHSIHGRATAVASGVKLANPKLSVWVVTGD 99
Cdd:NF041171 3 VDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 100 GDSMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSPTSLVGQKTKSSPYGNTQPPFSPGELAIGAQARFFARIGGN 179
Cdd:NF041171 83 GDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAY 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1309057203 180 TPKEMTELFIQAEKFKGTSLIEILQNCVIFNDNCFVKYTDKDV 222
Cdd:NF041171 163 DVKHLKELIKAAIKHKGLAFIDVLQPCPTYNDINTKEWYDKRV 205
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
54-202 |
9.03e-36 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 126.93 E-value: 9.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 54 GIGCSSRF---------PYYMDTYGMHSIHGRATAVASGVKLANPKLSVWVVTGDGDSMAIgGNHFIHVLRRNINLNILL 124
Cdd:pfam02775 1 DIGCHQMWaaqyyrfrpPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMN-LQELATAVRYNLPITVVV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1309057203 125 FNNEIYGLTKGQfspTSLVGQKTKSSPYGNTQPPFSPGELAIGAQARfFARIggNTPKEMTELFIQAEKFKGTSLIEI 202
Cdd:pfam02775 80 LNNGGYGMTRGQ---QTPFGGGRYSGPSGKILPPVDFAKLAEAYGAK-GARV--ESPEELEEALKEALEHDGPALIDV 151
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
4-336 |
3.20e-148 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 418.86 E-value: 3.20e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 4 TTVEKYTFKDFTSDQEVRWCPGCDDYVILRSMQKALPEMGLKREDVVFISGIGCSSRFPYYMDTYGMHSIHGRATAVASG 83
Cdd:PRK11867 1 MTDPMLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 84 VKLANPKLSVWVVTGDGDSMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSPTSLVGQKTKSSPYGNTQPPFSPGE 163
Cdd:PRK11867 81 LKLANPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 164 LAIGAQARFFARIGGNTPKEMTELFIQAEKFKGTSLIEILQNCVIF-NDNCFVKYTDKDVRedkqlfvehgkpmifgknk 242
Cdd:PRK11867 161 LALGAGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFnNVNTFDWFKERLVK------------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 243 dkglvlnrlklevvtlgengitevdilVHDAKEQDPTLHQMLVRLE---YPLVTGIIRsfdDVTLEEREDALTAKVKAGS 319
Cdd:PRK11867 222 ---------------------------VHDAEGYDPTNALAAMKTLeegDPIPTGIFY---QVERPTYEEAVRAQIEGPL 271
|
330
....*....|....*..
gi 1309057203 320 NFtktDDLFFSGETYEI 336
Cdd:PRK11867 272 AL---QDLLMGGDTWTV 285
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
22-209 |
5.67e-114 |
|
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: 328.33 E-value: 5.67e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 22 WCPGCDDYVILRSMQKALPEMGLKREDVVFISGIGCSSRFPYYMDTYGMHSIHGRATAVASGVKLANPKLSVWVVTGDGD 101
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 102 SMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSPTSLVGQKTKSSPYGNTQPPFSPGELAIGAQARFFARIGGNTP 181
Cdd:cd03375 81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160
|
170 180
....*....|....*....|....*...
gi 1309057203 182 KEMTELFIQAEKFKGTSLIEILQNCVIF 209
Cdd:cd03375 161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
8-239 |
1.43e-107 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440637 [Multi-domain] Cd Length: 262 Bit Score: 314.77 E-value: 1.43e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 8 KYTFKDFTSDQEVRWCPGCDDYVILRSMQKALPEMgLKREDVVFISGIGCSSRFPYYMDTYGMHSIHGRATAVASGVKLA 87
Cdd:COG1013 1 VLKKKDLLRTPGHRWCPGCGHGIILRLLLKALDEL-LDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 88 NPKLSVWVVTGDGDSMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSPTSLVGQKTKSSPYGNTQPPFSPGELAIG 167
Cdd:COG1013 80 NPDLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 168 AQARFFARIGGNTPKEMTELFIQAEKFKGTSLIEILQNCVIFND-----------NCFVKYTDKDVREDKQLFVEHGKPM 236
Cdd:COG1013 160 HGATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGrdpsktiewakEGMWPLYEYDPGEKLRLTYEPKDKI 239
|
...
gi 1309057203 237 IFG 239
Cdd:COG1013 240 PVG 242
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
22-212 |
4.41e-97 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 289.47 E-value: 4.41e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 22 WCPGCDDYVILRSMQKALPEMGLKREDVVFISGIGCSSRFPYYMDTYGMHSIHGRATAVASGVKLANPKLSVWVVTGDGD 101
Cdd:PRK05778 20 WCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLANPDLEVIVVGGDGD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 102 SMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSPTSLVGQKTKSSPYGNTQPPFSPGELAIGAQARFFARIGGNTP 181
Cdd:PRK05778 100 LASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAAGATFVARSFAGDV 179
|
170 180 190
....*....|....*....|....*....|.
gi 1309057203 182 KEMTELFIQAEKFKGTSLIEILQNCVIFNDN 212
Cdd:PRK05778 180 KQLVELIKKAISHKGFAFIDVLSPCVTFNGR 210
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
20-211 |
4.25e-85 |
|
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: 258.54 E-value: 4.25e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 20 VRWCPGCDDYVILRSMQKALPEMGLKREDVVFISGIGCSSRFPYYMDTYGMHSIHGRATAVASGVKLANPKLSVWVVTGD 99
Cdd:TIGR02177 1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 100 GDSMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSPTSLVGQKTKSSPYGNTQPPFSPGELAIGAQARFFARIGGN 179
Cdd:TIGR02177 81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160
|
170 180 190
....*....|....*....|....*....|..
gi 1309057203 180 TPKEMTELFIQAEKFKGTSLIEILQNCVIFND 211
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNK 192
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
22-210 |
1.71e-80 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 246.59 E-value: 1.71e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 22 WCPGCDDYVILRSMQKALPEMGLKREDVVFISGIGCSSRFPYYMDTYGMHSIHGRATAVASGVKLANPKLSVWVVTGDGD 101
Cdd:PRK11866 9 WCPGCGNYGILEALRKALAELGIPPENVVVVSGIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLTVIGYGGDGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 102 SMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSPTSLVGQKTKSSPYGNTQPPFSPGELAIGAQARFFARIGGNTP 181
Cdd:PRK11866 89 GYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATFVARGFSGDV 168
|
170 180
....*....|....*....|....*....
gi 1309057203 182 KEMTELFIQAEKFKGTSLIEILQNCVIFN 210
Cdd:PRK11866 169 KHLKEIIKEAIKHKGFSFIDVLSPCVTFN 197
|
|
| Oxoac_fdxbeta_Archa |
NF041171 |
2-oxoacid:ferredoxin oxidoreductase subunit beta; |
20-222 |
8.93e-77 |
|
2-oxoacid:ferredoxin oxidoreductase subunit beta;
Pssm-ID: 469082 [Multi-domain] Cd Length: 296 Bit Score: 237.53 E-value: 8.93e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 20 VRWCPGCDDYVILRSMQKALPEMGLKREDVVFISGIGCSSRFPYYMDTYGMHSIHGRATAVASGVKLANPKLSVWVVTGD 99
Cdd:NF041171 3 VDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 100 GDSMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSPTSLVGQKTKSSPYGNTQPPFSPGELAIGAQARFFARIGGN 179
Cdd:NF041171 83 GDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAY 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1309057203 180 TPKEMTELFIQAEKFKGTSLIEILQNCVIFNDNCFVKYTDKDV 222
Cdd:NF041171 163 DVKHLKELIKAAIKHKGLAFIDVLQPCPTYNDINTKEWYDKRV 205
|
|
| PRK11869 |
PRK11869 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
15-229 |
2.94e-68 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183349 [Multi-domain] Cd Length: 280 Bit Score: 215.03 E-value: 2.94e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 15 TSDQEVRWCPGCDDYVILRSMQKALPEMGLKREDVVFISGIGCSSRFPYYMDTYGMHSIHGRATAVASGVKLANPKLSVW 94
Cdd:PRK11869 3 PEKYDIAWCPGCGNFGIRNALMKALSELNLKPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 95 VVTGDGDSMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSPTSLVGQKTKSSPYGNTQPPFSPGELAIGAQARFFA 174
Cdd:PRK11869 83 AEGGDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASFVA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309057203 175 RIGGNTPKEMTELFIQAEKFKGTSLIEILQNCVIFND-NCFVKY-------TDKDVREDKQLF 229
Cdd:PRK11869 163 RTFSGDIEETKEILKEAIKHKGLAIVDIFQPCVSFNKvNTYQWYrentyylKDHDPTDRELAF 225
|
|
| oorB |
PRK09628 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; |
22-208 |
3.26e-68 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
Pssm-ID: 182003 [Multi-domain] Cd Length: 277 Bit Score: 214.98 E-value: 3.26e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 22 WCPGCDDYVILRSMQKALPEMGLKREDVVFISGIGCSSRFPYYMDTYGMHSIHGRATAVASGVKLANPKLSVWVVTGDGD 101
Cdd:PRK09628 18 WCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGIKLANPDKHVIVVSGDGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 102 SMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSPTSLVGQKTKSSPYGNTQPPFSPGELAIGAQARFFARIGGNTP 181
Cdd:PRK09628 98 GLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKLATAAGASFVARESVIDP 177
|
170 180
....*....|....*....|....*..
gi 1309057203 182 KEMTELFIQAEKFKGTSLIEILQNCVI 208
Cdd:PRK09628 178 QKLEKLLVKGFSHKGFSFFDVFSNCHI 204
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
54-202 |
9.03e-36 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 126.93 E-value: 9.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 54 GIGCSSRF---------PYYMDTYGMHSIHGRATAVASGVKLANPKLSVWVVTGDGDSMAIgGNHFIHVLRRNINLNILL 124
Cdd:pfam02775 1 DIGCHQMWaaqyyrfrpPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMN-LQELATAVRYNLPITVVV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1309057203 125 FNNEIYGLTKGQfspTSLVGQKTKSSPYGNTQPPFSPGELAIGAQARfFARIggNTPKEMTELFIQAEKFKGTSLIEI 202
Cdd:pfam02775 80 LNNGGYGMTRGQ---QTPFGGGRYSGPSGKILPPVDFAKLAEAYGAK-GARV--ESPEELEEALKEALEHDGPALIDV 151
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
31-204 |
5.81e-19 |
|
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: 82.69 E-value: 5.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 31 ILRSMQKALPEmglkreDVVFISGIGCSSRFPYYMD---------TYGMHSIHGRATAVASGVKLANPKLSVWVVTGDGD 101
Cdd:cd00568 2 VLAALRAALPE------DAIVVNDAGNSAYWAYRYLplrrgrrflTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 102 SMAiGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSPtslvgqKTKSSPYGNTQPPFSPGELA--IGAQArffARIggN 179
Cdd:cd00568 76 FMM-TGQELATAVRYGLPVIVVVFNNGGYGTIRMHQEA------FYGGRVSGTDLSNPDFAALAeaYGAKG---VRV--E 143
|
170 180
....*....|....*....|....*
gi 1309057203 180 TPKEMTELFIQAEKFKGTSLIEILQ 204
Cdd:cd00568 144 DPEDLEAALAEALAAGGPALIEVKT 168
|
|
| TPP_PFOR |
cd02018 |
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ... |
23-229 |
1.82e-18 |
|
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: 82.92 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 23 CPGCDDYVILRSMQKALPEmglkREDVVFISGIGCSS----RFPYymDTYGMHSIH---GRATAVASGVK---------- 85
Cdd:cd02018 8 CAGCGEVTAVRVVLAALPA----PEDTVIANSTGCSSvyasTAPF--NSWAVPWVNslfEDANAVASGLKrglkarfpkd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 86 --LANPKlSVWVVTGDGDSMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSPTSLVGQKTKSSPYGNTQPPFSPGE 163
Cdd:cd02018 82 reLDKKK-DVVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKKDLVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 164 LAIGAQARFFARIGGNTPKEMTELFIQAE-KFKGTSLIEILQNCVI---FNDNcfVKYTDKDVREDKQLF 229
Cdd:cd02018 161 IAATHGCVYVARLSPALKKHFLKVVKEAIsRTDGPTFIHAYTPCITewgIGSG--KSLELARKAVKSRMF 228
|
|
| TPP_PFOR_porB_like |
cd03376 |
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ... |
21-207 |
6.55e-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: 64.18 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 21 RWCPGCDDYVILRSMQKALpemglkREDVVFISGIGC----SSRFPY--YMDTYgMHSIHGRATAVASGVKLA------N 88
Cdd:cd03376 6 RACAGCGAALALRHVLKAL------GPDTVVVNPTGCleviTTPYPYtaWRVPW-IHVAFENAAAVASGIEAAlkalgrG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 89 PKLSVWVVTGDGDSMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSPTSLVGQKTKSSP-----YGNTQPPFSPGE 163
Cdd:cd03376 79 KDITVVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTTPvgkvsFGKKQPKKDLPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1309057203 164 LAIGAQARFFARIGGNTPKEMTELFIQAEKFKGTSLIEILQNCV 207
Cdd:cd03376 159 IMAAHNIPYVATASVAYPEDLYKKVKKALSIEGPAYIHILSPCP 202
|
|
| PRK11865 |
PRK11865 |
pyruvate synthase subunit beta; |
21-207 |
3.84e-11 |
|
pyruvate synthase subunit beta;
Pssm-ID: 183346 [Multi-domain] Cd Length: 299 Bit Score: 62.81 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 21 RWCPGCDDYVILRSMQKALPEmglkreDVVFISGIGCSS--RFPYYMDTYGMHSIH---GRATAVASGVKLA----NPKL 91
Cdd:PRK11865 19 RACAGCGAAIAMRLALKALGK------NTVIVVATGCLEviTTPYPETAWNVPWIHvafENAAAVASGIERAvkalGKKV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 92 SVWVVTGDGDSMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSPTSLVGQKTKSSPYGNtqppFSPGE-------- 163
Cdd:PRK11865 93 NVVAIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGK----YSRGEdrpkknmp 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1309057203 164 -LAIGAQARFFARIGGNTPKEMTELFIQAEKFKGTSLIEILQNCV 207
Cdd:PRK11865 169 lIMAAHGIPYVATASIGYPEDFMEKVKKAKEVEGPAYIQVLQPCP 213
|
|
| TPP_PFOR_PNO |
cd03377 |
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ... |
89-200 |
3.94e-08 |
|
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: 54.15 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 89 PKLSVWVVTGDGDSMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSptslvgqktKSSPygntqppfspgelaIGA 168
Cdd:cd03377 150 VKKSVWIIGGDGWAYDIGYGGLDHVLASGENVNILVLDTEVYSNTGGQAS---------KATP--------------LGA 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1309057203 169 QARFfARIGGNTPKE------MT-------------------ELFIQAEKFKGTSLI 200
Cdd:cd03377 207 VAKF-AAAGKRTGKKdlgmiaMSygnvyvaqialgandnqtlKAFREAEAYDGPSLI 262
|
|
| pyruv_ox_red |
TIGR02176 |
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ... |
90-207 |
4.72e-08 |
|
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single chain form of pyruvate:ferredoxin (or flavodoxin) oxidoreductase. This enzyme may transfer electrons to nitrogenase in nitrogen-fixing species. Portions of this protein are homologous to gamma subunit of the four subunit pyruvate:ferredoxin (flavodoxin) oxidoreductase.
Pssm-ID: 131231 [Multi-domain] Cd Length: 1165 Bit Score: 54.78 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 90 KLSVWVVTGDGDSMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSPTSLVGQKTKSSPYGNTQPPFSPGELAIGAQ 169
Cdd:TIGR02176 951 KKSVWIIGGDGWAYDIGYGGLDHVLASGKDVNVLVMDTEVYSNTGGQSSKATPTGAIAKFAAAGKRTSKKDLGMMAMTYG 1030
|
90 100 110
....*....|....*....|....*....|....*....
gi 1309057203 170 ARFFARIG-GNTPKEMTELFIQAEKFKGTSLIEILQNCV 207
Cdd:TIGR02176 1031 YVYVAQVSmGANMQQTLKAFREAEAYDGPSIVIAYSPCI 1069
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
45-143 |
5.21e-06 |
|
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: 46.13 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 45 KREDVVFISGIGCSSRFPYYMD----TYGMHSIHGRATAVASGVKLANPKlSVWVVTGDGdSMAIGGNHFIHVLRRNI-N 119
Cdd:cd03372 11 DLKDELVVSNIGFPSKELYAAGdrplNFYMLGSMGLASSIGLGLALAQPR-KVIVIDGDG-SLLMNLGALATIAAEKPkN 88
|
90 100
....*....|....*....|....
gi 1309057203 120 LNILLFNNEIYGLTKGQFSPTSLV 143
Cdd:cd03372 89 LIIVVLDNGAYGSTGNQPTHAGKK 112
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
47-203 |
7.80e-06 |
|
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: 45.77 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 47 EDVVFISGIGCSSRFPY-YMDTYGMHSIH--------GRATAVASGVKLANPKLSVWVVTGDG------DSMAIGGNH-- 109
Cdd:cd03371 14 ATAAVVSTTGMTSRELFeLRDRPGGGHAQdfltvgsmGHASQIALGIALARPDRKVVCIDGDGaalmhmGGLATIGGLap 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 110 --FIHVLrrninlnillFNNEIYGLTKGQfsPTslVGQKTksspygntqpPFSpgelAIGAQARFFARIGGNTPKEMTEL 187
Cdd:cd03371 94 anLIHIV----------LNNGAHDSVGGQ--PT--VSFDV----------SLP----AIAKACGYRAVYEVPSLEELVAA 145
|
170
....*....|....*.
gi 1309057203 188 FIQAEKFKGTSLIEIL 203
Cdd:cd03371 146 LAKALAADGPAFIEVK 161
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
23-206 |
9.58e-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: 45.35 E-value: 9.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 23 CPGC---DDYVILRSMQKAlpemglkreDVVFISGIGCSSrFPYYMDTYGMHSI--HGRATAVASGVKLANPKLSVWVVT 97
Cdd:cd02008 7 CPGCphrPSFYALRKAFKK---------DSIVSGDIGCYT-LGALPPLNAIDTCtcMGASIGVAIGMAKASEDKKVVAVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 98 GDGDSMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKGQFSPTSLVGQKTKSspygntqppfspGELAIGAQARFF--AR 175
Cdd:cd02008 77 GDSTFFHSGILGLINAVYNKANITVVILDNRTTAMTGGQPHPGTGKTLTEPT------------TVIDIEALVRAIgvKR 144
|
170 180 190
....*....|....*....|....*....|....
gi 1309057203 176 IGGNTP---KEMTELFIQAEKFKGTSLIEILQNC 206
Cdd:cd02008 145 VVVVDPydlKAIREELKEALAVPGVSVIIAKRPC 178
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
44-141 |
1.75e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 44.82 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 44 LKREDVVfISGIG-------CSSRFP--YYMdtygMHSIhGRATAVASGVKLANPKLSVWVVTGDGD-SMAIGGNHFIHV 113
Cdd:PRK06163 26 LKDEEAV-IGGIGntnfdlwAAGQRPqnFYM----LGSM-GLAFPIALGVALAQPKRRVIALEGDGSlLMQLGALGTIAA 99
|
90 100
....*....|....*....|....*...
gi 1309057203 114 LRRNiNLNILLFNNEIYGLTKGQFSPTS 141
Cdd:PRK06163 100 LAPK-NLTIIVMDNGVYQITGGQPTLTS 126
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
32-131 |
2.50e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 45.77 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 32 LRSMQKALPEMGLKREDvvfISGIGCSSRFPY------------YMDTYGmhsiHGRATAVasGVKLANPKLSVWVVTGD 99
Cdd:PRK08266 359 LRAIREALPDDGIFVDE---LSQVGFASWFAFpvyaprtfvtcgYQGTLG----YGFPTAL--GAKVANPDRPVVSITGD 429
|
90 100 110
....*....|....*....|....*....|..
gi 1309057203 100 GDSMaIGGNHFIHVLRRNINLNILLFNNEIYG 131
Cdd:PRK08266 430 GGFM-FGVQELATAVQHNIGVVTVVFNNNAYG 460
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
28-203 |
4.09e-05 |
|
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: 43.74 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 28 DYVILRsMQKALPEMglkreDVVFISGIGCS----SRFP------YYMDTYGmhSIhGRATAVASGVKLANPKLSVWVVT 97
Cdd:cd02002 4 EYLAAA-LAAALPED-----AIIVDEAVTNGlplrDQLPltrpgsYFTLRGG--GL-GWGLPAAVGAALANPDRKVVAII 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 98 GDGDSMaiggnhF-IHVL----RRNINLNILLFNNEIYGLTKgqfSPTSLVGQKTKSSPYGNTQ----PPFSPGELA--I 166
Cdd:cd02002 75 GDGSFM------YtIQALwtaaRYGLPVTVVILNNRGYGALR---SFLKRVGPEGPGENAPDGLdlldPGIDFAAIAkaF 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 1309057203 167 GAQARFFAriggnTPKEMTELFIQAEKFKGTSLIEIL 203
Cdd:cd02002 146 GVEAERVE-----TPEELDEALREALAEGGPALIEVV 177
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
31-131 |
1.92e-04 |
|
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: 43.22 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 31 ILRSMQKALPEmglkreDVVFISGIGCSSRFPY-YMDTYGMHSIHGrATAVAS---------GVKLANPKLSVWVVTGDG 100
Cdd:COG0028 368 VIAALREALPD------DAIVVTDVGQHQMWAArYLRFRRPRRFLT-SGGLGTmgyglpaaiGAKLARPDRPVVAITGDG 440
|
90 100 110
....*....|....*....|....*....|...
gi 1309057203 101 D-SMAIGgnhFIHVLRR-NINLNILLFNNEIYG 131
Cdd:COG0028 441 GfQMNLQ---ELATAVRyGLPVKVVVLNNGGLG 470
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
47-143 |
9.33e-04 |
|
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: 39.39 E-value: 9.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 47 EDVVFISGIGCSSRFPYYMDT-----YGMHSIhGRATAVASGVKLANPKlSVWVVTGDGD------SMAIGGNHfihvlr 115
Cdd:cd02001 13 GDTPIVSTTGYASRELYDVQDrdghfYMLGSM-GLAGSIGLGLALGLSR-KVIVVDGDGSllmnpgVLLTAGEF------ 84
|
90 100
....*....|....*....|....*...
gi 1309057203 116 RNINLNILLFNNEIYGLTKGQFSPTSLV 143
Cdd:cd02001 85 TPLNLILVVLDNRAYGSTGGQPTPSSNV 112
|
|
| PRK06882 |
PRK06882 |
acetolactate synthase 3 large subunit; |
81-195 |
2.20e-03 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 168717 [Multi-domain] Cd Length: 574 Bit Score: 39.90 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309057203 81 ASGVKLANPKLSVWVVTGDGdSMAIGGNHFIHVLRRNINLNILLFNNEIYGLTKgQFSPTSLVGQKTKSspYGNTQPPFs 160
Cdd:PRK06882 430 AIGVKFAHPEATVVCVTGDG-SIQMNIQELSTAKQYDIPVVIVSLNNRFLGMVK-QWQDLIYSGRHSQV--YMNSLPDF- 504
|
90 100 110
....*....|....*....|....*....|....*
gi 1309057203 161 pgelAIGAQARFFARIGGNTPKEMTELFIQAEKFK 195
Cdd:PRK06882 505 ----AKLAEAYGHVGIQIDTPDELEEKLTQAFSIK 535
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
81-132 |
7.12e-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: 37.09 E-value: 7.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1309057203 81 ASGVKLANPKLSVWVVTGDGD-SMAIGGnhfIHVLRR-NINLNILLFNNEIYGL 132
Cdd:cd02015 59 AIGAKVARPDKTVICIDGDGSfQMNIQE---LATAAQyNLPVKIVILNNGSLGM 109
|
|
| |
