|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
3-333 |
5.99e-171 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 476.26 E-value: 5.99e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 3 TTNTLSARDFSSDQEVKWCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGL 82
Cdd:PRK11867 2 TDPMLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 83 KITNPDLSIWVITGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLAL 162
Cdd:PRK11867 82 KLANPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 163 ALGADASFVARSIDRDPKHLREILSASHQHKGTSFIEVYQNCNVF-NDGTFLNFTDKKLKDENVllleegqplvydqgkk 241
Cdd:PRK11867 162 ALGAGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFnNVNTFDWFKERLVKVHDA---------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 242 girlnglkpeivnleegaslndlwihDSRDATKAYVLSRFFDDSLPRPFGIFYQEDRPCYEDDLLDQIdhakgvQGEGDL 321
Cdd:PRK11867 226 --------------------------EGYDPTNALAAMKTLEEGDPIPTGIFYQVERPTYEEAVRAQI------EGPLAL 273
|
330
....*....|..
gi 1900713664 322 DDLLRGKRSWTV 333
Cdd:PRK11867 274 QDLLMGGDTWTV 285
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
20-212 |
7.78e-125 |
|
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: 355.68 E-value: 7.78e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 20 WCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVITGDGD 99
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 100 GLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALGADASFVARSIDRDP 179
Cdd:cd03375 81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160
|
170 180 190
....*....|....*....|....*....|...
gi 1900713664 180 KHLREILSASHQHKGTSFIEVYQNCNVFNDGTF 212
Cdd:cd03375 161 KQLKEIIKKAIQHKGFSFVEVLSPCPTFPLGVF 193
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
6-209 |
2.47e-108 |
|
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: 316.32 E-value: 2.47e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 6 TLSARDFSSDQEVKWCPGCGDYSILKQMQSVVPELGIaREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKIT 85
Cdd:COG1013 1 VLKKKDLLRTPGHRWCPGCGHGIILRLLLKALDELLD-GDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 86 NPDLSIWVITGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALG 165
Cdd:COG1013 80 NPDLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1900713664 166 ADASFVARSIDRDPKHLREILSASHQHKGTSFIEVYQNCNVFND 209
Cdd:COG1013 160 HGATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWG 203
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
18-306 |
3.95e-92 |
|
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: 276.26 E-value: 3.95e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 18 VKWCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVITGD 97
Cdd:TIGR02177 1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 98 GDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALGADASFVARSIDR 177
Cdd:TIGR02177 81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 178 DPKHLREILSASHQHKGTSFIEVYQNCNVFNDgtfLNfTDKKLKDENVLLLEEG-QPLVYDQGKkgirlnglkpeivnle 256
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNK---IN-TYEWYRERVYKLDEEGyDPIVREPEE---------------- 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1900713664 257 egaslndlwihDSRDATKAYVLSRFFDDSLprPFGIFYQ-EDRPCYEDDLL 306
Cdd:TIGR02177 221 -----------FEEKAAAAIKKAMEWGDRI--PIGIFYKnENKPTFEERLE 258
|
|
| Oxoac_fdxbeta_Archa |
NF041171 |
2-oxoacid:ferredoxin oxidoreductase subunit beta; |
18-306 |
2.09e-85 |
|
2-oxoacid:ferredoxin oxidoreductase subunit beta;
Pssm-ID: 469082 [Multi-domain] Cd Length: 296 Bit Score: 259.48 E-value: 2.09e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 18 VKWCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVITGD 97
Cdd:NF041171 3 VDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 98 GDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALGADASFVARSIDR 177
Cdd:NF041171 83 GDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 178 DPKHLREILSASHQHKGTSFIEVYQNCNVFNDGTFLNFTDK---KLKDEnvllleegqplvydqgkkgirlNGLKPEIVN 254
Cdd:NF041171 163 DVKHLKELIKAAIKHKGLAFIDVLQPCPTYNDINTKEWYDKrvyKLDDE----------------------PGWDPVVRS 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1900713664 255 LEEgaslndlwihDSRDATKAYVLSRFFDDSLprPFGIFYQ-EDRPCYEDDLL 306
Cdd:NF041171 221 PEE----------ADEKMAKAIEKALEWGDRI--PIGIFYQnELVPTFEERIA 261
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
52-200 |
3.21e-35 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 125.39 E-value: 3.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 52 GIGCSSRF---------PYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVITGDGDGLSIgGNHLIHLLRRNVDLNVLL 122
Cdd:pfam02775 1 DIGCHQMWaaqyyrfrpPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMN-LQELATAVRYNLPITVVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 123 FNNQIYGLTKGQYSPTselGKKTKSSPLGSLDHPFNP--LALALGADASFVarsidRDPKHLREILSASHQHKGTSFIEV 200
Cdd:pfam02775 80 LNNGGYGMTRGQQTPF---GGGRYSGPSGKILPPVDFakLAEAYGAKGARV-----ESPEELEEALKEALEHDGPALIDV 151
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
3-333 |
5.99e-171 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 476.26 E-value: 5.99e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 3 TTNTLSARDFSSDQEVKWCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGL 82
Cdd:PRK11867 2 TDPMLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 83 KITNPDLSIWVITGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLAL 162
Cdd:PRK11867 82 KLANPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 163 ALGADASFVARSIDRDPKHLREILSASHQHKGTSFIEVYQNCNVF-NDGTFLNFTDKKLKDENVllleegqplvydqgkk 241
Cdd:PRK11867 162 ALGAGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFnNVNTFDWFKERLVKVHDA---------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 242 girlnglkpeivnleegaslndlwihDSRDATKAYVLSRFFDDSLPRPFGIFYQEDRPCYEDDLLDQIdhakgvQGEGDL 321
Cdd:PRK11867 226 --------------------------EGYDPTNALAAMKTLEEGDPIPTGIFYQVERPTYEEAVRAQI------EGPLAL 273
|
330
....*....|..
gi 1900713664 322 DDLLRGKRSWTV 333
Cdd:PRK11867 274 QDLLMGGDTWTV 285
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
20-212 |
7.78e-125 |
|
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: 355.68 E-value: 7.78e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 20 WCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVITGDGD 99
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 100 GLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALGADASFVARSIDRDP 179
Cdd:cd03375 81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160
|
170 180 190
....*....|....*....|....*....|...
gi 1900713664 180 KHLREILSASHQHKGTSFIEVYQNCNVFNDGTF 212
Cdd:cd03375 161 KQLKEIIKKAIQHKGFSFVEVLSPCPTFPLGVF 193
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
4-305 |
6.82e-111 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 324.52 E-value: 6.82e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 4 TNTLSARDFSSD-QEVKWCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGL 82
Cdd:PRK05778 3 KNALGLTYLRYDgLPTTWCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 83 KITNPDLSIWVITGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLAL 162
Cdd:PRK05778 83 KLANPDLEVIVVGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 163 ALGADASFVARSIDRDPKHLREILSASHQHKGTSFIEVYQNCNVFNDgtflNFTDKKLKDENVLLLEEGqplVYDqgkkg 242
Cdd:PRK05778 163 ALAAGATFVARSFAGDVKQLVELIKKAISHKGFAFIDVLSPCVTFNG----RNTSTKSPAYMREYYKKR---VYK----- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1900713664 243 irlnglkpeiVNLEEGaslndlwiHDSRDATKAyvlsrfFDDSLPR------PFGIFYQEDRPCYEDDL 305
Cdd:PRK05778 231 ----------LKLEED--------YDPTDRDKA------AEKMLEEelggkiPIGVFYKNERPTFEERL 275
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
6-209 |
2.47e-108 |
|
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: 316.32 E-value: 2.47e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 6 TLSARDFSSDQEVKWCPGCGDYSILKQMQSVVPELGIaREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKIT 85
Cdd:COG1013 1 VLKKKDLLRTPGHRWCPGCGHGIILRLLLKALDELLD-GDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 86 NPDLSIWVITGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALG 165
Cdd:COG1013 80 NPDLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1900713664 166 ADASFVARSIDRDPKHLREILSASHQHKGTSFIEVYQNCNVFND 209
Cdd:COG1013 160 HGATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWG 203
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
20-306 |
1.13e-93 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 279.72 E-value: 1.13e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 20 WCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVITGDGD 99
Cdd:PRK11866 9 WCPGCGNYGILEALRKALAELGIPPENVVVVSGIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLTVIGYGGDGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 100 GLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALGADASFVARSIDRDP 179
Cdd:PRK11866 89 GYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATFVARGFSGDV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 180 KHLREILSASHQHKGTSFIEVYQNCNVFNdgtflnftdkklkdenvllleegqplvydqgkkgiRLNG---LKPEIVNLE 256
Cdd:PRK11866 169 KHLKEIIKEAIKHKGFSFIDVLSPCVTFN-----------------------------------KLNTydwFRPRVYKLE 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1900713664 257 EGAslndlwiHDSRDATKAYVLSRFFDDSLprPFGIFYQEDRPCYEDDLL 306
Cdd:PRK11866 214 ETG-------HDPTNFEQAYKKALEWGDRI--PIGVFYKEEKPTYEEELD 254
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
18-306 |
3.95e-92 |
|
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: 276.26 E-value: 3.95e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 18 VKWCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVITGD 97
Cdd:TIGR02177 1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 98 GDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALGADASFVARSIDR 177
Cdd:TIGR02177 81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 178 DPKHLREILSASHQHKGTSFIEVYQNCNVFNDgtfLNfTDKKLKDENVLLLEEG-QPLVYDQGKkgirlnglkpeivnle 256
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNK---IN-TYEWYRERVYKLDEEGyDPIVREPEE---------------- 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1900713664 257 egaslndlwihDSRDATKAYVLSRFFDDSLprPFGIFYQ-EDRPCYEDDLL 306
Cdd:TIGR02177 221 -----------FEEKAAAAIKKAMEWGDRI--PIGIFYKnENKPTFEERLE 258
|
|
| Oxoac_fdxbeta_Archa |
NF041171 |
2-oxoacid:ferredoxin oxidoreductase subunit beta; |
18-306 |
2.09e-85 |
|
2-oxoacid:ferredoxin oxidoreductase subunit beta;
Pssm-ID: 469082 [Multi-domain] Cd Length: 296 Bit Score: 259.48 E-value: 2.09e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 18 VKWCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVITGD 97
Cdd:NF041171 3 VDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 98 GDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALGADASFVARSIDR 177
Cdd:NF041171 83 GDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 178 DPKHLREILSASHQHKGTSFIEVYQNCNVFNDGTFLNFTDK---KLKDEnvllleegqplvydqgkkgirlNGLKPEIVN 254
Cdd:NF041171 163 DVKHLKELIKAAIKHKGLAFIDVLQPCPTYNDINTKEWYDKrvyKLDDE----------------------PGWDPVVRS 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1900713664 255 LEEgaslndlwihDSRDATKAYVLSRFFDDSLprPFGIFYQ-EDRPCYEDDLL 306
Cdd:NF041171 221 PEE----------ADEKMAKAIEKALEWGDRI--PIGIFYQnELVPTFEERIA 261
|
|
| PRK11869 |
PRK11869 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
15-305 |
4.00e-73 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183349 [Multi-domain] Cd Length: 280 Bit Score: 227.36 E-value: 4.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 15 DQEVKWCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVI 94
Cdd:PRK11869 5 KYDIAWCPGCGNFGIRNALMKALSELNLKPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTVIAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 95 TGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALGADASFVARS 174
Cdd:PRK11869 85 GGDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASFVART 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 175 IDRDPKHLREILSASHQHKGTSFIEVYQNCNVFND-GTFLNFTdkklkdENVLLLEEgqplvydqgkkgirlnglkpeiv 253
Cdd:PRK11869 165 FSGDIEETKEILKEAIKHKGLAIVDIFQPCVSFNKvNTYQWYR------ENTYYLKD----------------------- 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1900713664 254 nleegaslndlwiHDSRDATKAyvlsrfFDDSL---PRPFGIFYQEDRPCYEDDL 305
Cdd:PRK11869 216 -------------HDPTDRELA------FKRALeteKLPLGIFYINEKPTFEELV 251
|
|
| oorB |
PRK09628 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; |
20-206 |
2.90e-67 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
Pssm-ID: 182003 [Multi-domain] Cd Length: 277 Bit Score: 212.28 E-value: 2.90e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 20 WCPGCGDYSILKQMQSVVPELGIAREDIVFISGIGCSSRFPYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVITGDGD 99
Cdd:PRK09628 18 WCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGIKLANPDKHVIVVSGDGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 100 GLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLALALGADASFVARSIDRDP 179
Cdd:PRK09628 98 GLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKLATAAGASFVARESVIDP 177
|
170 180
....*....|....*....|....*..
gi 1900713664 180 KHLREILSASHQHKGTSFIEVYQNCNV 206
Cdd:PRK09628 178 QKLEKLLVKGFSHKGFSFFDVFSNCHI 204
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
52-200 |
3.21e-35 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 125.39 E-value: 3.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 52 GIGCSSRF---------PYYMNTYGMHSIHGRAPAIATGLKITNPDLSIWVITGDGDGLSIgGNHLIHLLRRNVDLNVLL 122
Cdd:pfam02775 1 DIGCHQMWaaqyyrfrpPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMN-LQELATAVRYNLPITVVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 123 FNNQIYGLTKGQYSPTselGKKTKSSPLGSLDHPFNP--LALALGADASFVarsidRDPKHLREILSASHQHKGTSFIEV 200
Cdd:pfam02775 80 LNNGGYGMTRGQQTPF---GGGRYSGPSGKILPPVDFakLAEAYGAKGARV-----ESPEELEEALKEALEHDGPALIDV 151
|
|
| TPP_PFOR |
cd02018 |
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ... |
21-223 |
1.56e-22 |
|
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: 94.09 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 21 CPGCGDYSILKQMQSVVPelgiAREDIVFISGIGCSS----RFPYymNTYGMHSIH---GRAPAIATGLK-----ITNPD 88
Cdd:cd02018 8 CAGCGEVTAVRVVLAALP----APEDTVIANSTGCSSvyasTAPF--NSWAVPWVNslfEDANAVASGLKrglkaRFPKD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 89 L------SIWVITGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLDHPFNPLAL 162
Cdd:cd02018 82 ReldkkkDVVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKKDLVLI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1900713664 163 ALGADASFVARSIDRDPKH-LREILSASHQHKGTSFIEVYQNCNV---FNDGTFLNFTDKKLKDE 223
Cdd:cd02018 162 AATHGCVYVARLSPALKKHfLKVVKEAISRTDGPTFIHAYTPCITewgIGSGKSLELARKAVKSR 226
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
29-200 |
2.69e-18 |
|
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: 80.76 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 29 ILKQMQSVVPElgiareDIVFISGIGCSSRFPYYM---------NTYGMHSIHGRAPAIATGLKITNPDLSIWVITGDGd 99
Cdd:cd00568 2 VLAALRAALPE------DAIVVNDAGNSAYWAYRYlplrrgrrfLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDG- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 100 GLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYsptselGKKTKSSPLGSLDHP--FNPLALALGADASFVarsidR 177
Cdd:cd00568 75 GFMMTGQELATAVRYGLPVIVVVFNNGGYGTIRMHQ------EAFYGGRVSGTDLSNpdFAALAEAYGAKGVRV-----E 143
|
170 180
....*....|....*....|...
gi 1900713664 178 DPKHLREILSASHQHKGTSFIEV 200
Cdd:cd00568 144 DPEDLEAALAEALAAGGPALIEV 166
|
|
| PRK11865 |
PRK11865 |
pyruvate synthase subunit beta; |
21-204 |
2.87e-12 |
|
pyruvate synthase subunit beta;
Pssm-ID: 183346 [Multi-domain] Cd Length: 299 Bit Score: 66.28 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 21 CPGCGDYSILKQMqsvvpeLGIAREDIVFISGIGCSS--RFPYYMNTYGMHSIH---GRAPAIATG----LKITNPDLSI 91
Cdd:PRK11865 21 CAGCGAAIAMRLA------LKALGKNTVIVVATGCLEviTTPYPETAWNVPWIHvafENAAAVASGieraVKALGKKVNV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 92 WVITGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSL----DHPFNPLALALGA- 166
Cdd:PRK11865 95 VAIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKYsrgeDRPKKNMPLIMAAh 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1900713664 167 DASFVARSIDRDPKHLREILSASHQHKGTSFIEVYQNC 204
Cdd:PRK11865 175 GIPYVATASIGYPEDFMEKVKKAKEVEGPAYIQVLQPC 212
|
|
| TPP_PFOR_porB_like |
cd03376 |
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ... |
21-204 |
1.80e-08 |
|
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: 54.17 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 21 CPGCGDYSILKQMqsvvpeLGIAREDIVFISGIGCSSRF--PYYMNTYGMHSIH---GRAPAIATG----LKIT--NPDL 89
Cdd:cd03376 8 CAGCGAALALRHV------LKALGPDTVVVNPTGCLEVIttPYPYTAWRVPWIHvafENAAAVASGieaaLKALgrGKDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 90 SIWVITGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSPTSELGKKTKSSPLGSLD-----HPFNPLALAL 164
Cdd:cd03376 82 TVVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTTPVGKVSfgkkqPKKDLPLIMA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1900713664 165 GADASFVARSIDRDPKHLREILSASHQHKGTSFIEVYQNC 204
Cdd:cd03376 162 AHNIPYVATASVAYPEDLYKKVKKALSIEGPAYIHILSPC 201
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
28-200 |
1.54e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 52.71 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 28 SILKQMQSVVPELGIAREDIvfiSGIGCSSR--FPYYM-NTY---GMHSIHGRAPAIATGLKITNPDLSIWVITGDGdGL 101
Cdd:PRK08266 357 SYLRAIREALPDDGIFVDEL---SQVGFASWfaFPVYApRTFvtcGYQGTLGYGFPTALGAKVANPDRPVVSITGDG-GF 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 102 SIGGNHLIHLLRRNVDLNVLLFNNQIYG----LTKGQYsptselGKKTKSSPLGSLDhpFNPLALALGADASFVarsidR 177
Cdd:PRK08266 433 MFGVQELATAVQHNIGVVTVVFNNNAYGnvrrDQKRRF------GGRVVASDLVNPD--FVKLAESFGVAAFRV-----D 499
|
170 180
....*....|....*....|...
gi 1900713664 178 DPKHLREILSASHQHKGTSFIEV 200
Cdd:PRK08266 500 SPEELRAALEAALAHGGPVLIEV 522
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
43-200 |
2.08e-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: 47.69 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 43 AREDIVFISGIGCSSRFPY-YMNTYGMHSIH--------GRAPAIATGLKITNPDLSIWVITGDG------DGLSIGGNH 107
Cdd:cd03371 12 APATAAVVSTTGMTSRELFeLRDRPGGGHAQdfltvgsmGHASQIALGIALARPDRKVVCIDGDGaalmhmGGLATIGGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 108 ----LIHllrrnvdlnvLLFNNQIYGLTKGQysPTSelgkktkssplgSLDHPFNPLALALGADASFVARSIDRDPKHLR 183
Cdd:cd03371 92 apanLIH----------IVLNNGAHDSVGGQ--PTV------------SFDVSLPAIAKACGYRAVYEVPSLEELVAALA 147
|
170
....*....|....*..
gi 1900713664 184 EILSAShqhkGTSFIEV 200
Cdd:cd03371 148 KALAAD----GPAFIEV 160
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
23-133 |
2.25e-06 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 49.22 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 23 GCGDYSIL-KQMQSVVPELGIAREDIVfISGIGCSSR-FPYYMNTYGMHSIH---GRAPAIATGLKITNPDLSIWVITGD 97
Cdd:PRK07064 354 GLGPYAKLvDALRAALPRDGNWVRDVT-ISNSTWGNRlLPIFEPRANVHALGggiGQGLAMAIGAALAGPGRKTVGLVGD 432
|
90 100 110
....*....|....*....|....*....|....*.
gi 1900713664 98 GdGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKG 133
Cdd:PRK07064 433 G-GLMLNLGELATAVQENANMVIVLMNDGGYGVIRN 467
|
|
| PFO_beta_C |
pfam12367 |
Pyruvate ferredoxin oxidoreductase beta subunit C terminal; This domain family is found in ... |
249-303 |
6.25e-06 |
|
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: 43.25 E-value: 6.25e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1900713664 249 KPEIVNLEEgaslndlwIHDSRDATKAYVLSRFFDDSLPrpFGIFYQEDRPCYED 303
Cdd:pfam12367 14 KERVYKLDE--------DHDPTDREAAMEKALEWGDRIP--IGIFYKEERPTFEE 58
|
|
| TPP_PFOR_PNO |
cd03377 |
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ... |
90-152 |
3.68e-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: 44.90 E-value: 3.68e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1900713664 90 SIWVITGDGDGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYSptselgkktKSSPLGS 152
Cdd:cd03377 153 SVWIIGGDGWAYDIGYGGLDHVLASGENVNILVLDTEVYSNTGGQAS---------KATPLGA 206
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
78-200 |
4.37e-05 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 45.14 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 78 IATGLKITNPDLSIWVITGDGdGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKgqYSPTSELGKKTKSSPLGSLDHPf 157
Cdd:PRK06112 445 MAIGAKVARPGAPVICLVGDG-GFAHVWAELETARRMGVPVTIVVLNNGILGFQK--HAETVKFGTHTDACHFAAVDHA- 520
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1900713664 158 nPLALALGADASFVarsidRDPKHLREILSASHQHKGTSFIEV 200
Cdd:PRK06112 521 -AIARACGCDGVRV-----EDPAELAQALAAAMAAPGPTLIEV 557
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
76-200 |
5.79e-05 |
|
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: 44.77 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 76 PAiATGLKITNPDLSIWVITGDGdGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLTKGQYspTSELGKKTKSSPLGSLDh 155
Cdd:COG0028 419 PA-AIGAKLARPDRPVVAITGDG-GFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRQWQ--ELFYGGRYSGTDLPNPD- 493
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1900713664 156 pFNPLALALGADASFVarsidRDPKHLREILSASHQHKGTSFIEV 200
Cdd:COG0028 494 -FAKLAEAFGAKGERV-----ETPEELEAALEEALASDGPALIDV 532
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
76-200 |
1.46e-04 |
|
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding module; composed of proteins similar to the large catalytic subunit of AHAS. AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate. 2-Acetolactate is the precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. In addition to requiring TPP and a divalent metal ion as cofactors, AHAS requires FAD.
Pssm-ID: 238973 [Multi-domain] Cd Length: 186 Bit Score: 42.10 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 76 PAiATGLKITNPDLSIWVITGDGdGLSIGGNHLIHLLRRNVDLNVLLFNNQIYGLT--------KGQYSPTselgkktks 147
Cdd:cd02015 57 PA-AIGAKVARPDKTVICIDGDG-SFQMNIQELATAAQYNLPVKIVILNNGSLGMVrqwqelfyEGRYSHT--------- 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1900713664 148 splgslDHPFNP----LALALGADASFVarsidRDPKHLREILSASHQHKGTSFIEV 200
Cdd:cd02015 126 ------TLDSNPdfvkLAEAYGIKGLRV-----EKPEELEAALKEALASDGPVLLDV 171
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
77-200 |
1.08e-03 |
|
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins similar to Rhizobium leguminosarum bv. viciae IolD. IolD plays an important role in myo-inositol catabolism.
Pssm-ID: 238961 [Multi-domain] Cd Length: 205 Bit Score: 39.60 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 77 AIATGLKITNPDLSIWVITGDGDGLsIGGNHLIHLLRRNVDLNVLLFNNQIYG------LTKGQYSPTSELgkKTKSSPL 150
Cdd:cd02003 55 AAGLGAKLAKPDREVYVLVGDGSYL-MLHSEIVTAVQEGLKIIIVLFDNHGFGcinnlqESTGSGSFGTEF--RDRDQES 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1900713664 151 GSLDHPFNPLALA-----LGADASFVarsidRDPKHLREILSASHQHKGTSFIEV 200
Cdd:cd02003 132 GQLDGALLPVDFAanarsLGARVEKV-----KTIEELKAALAKAKASDRTTVIVI 181
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
42-200 |
1.12e-03 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 40.74 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 42 IAREDIVFISGIG-CSSRFPYYMNTYGMHSI-----HGR-APAI--ATGLKITNPDLSIWVITGDGdGLSIGGNHLIHLL 112
Cdd:PRK06546 371 LAADDAVFTVDTGmCNVWAARYITPNGRRRVigsfrHGSmANALphAIGAQLADPGRQVISMSGDG-GLSMLLGELLTVK 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 113 RRNVDLNVLLFNNQIYGLTKgqysptseLGKKTKSSPLGSLDHP---FNPLALALGADASFVarsidRDPKHLREILSAS 189
Cdd:PRK06546 450 LYDLPVKVVVFNNSTLGMVK--------LEMLVDGLPDFGTDHPpvdYAAIAAALGIHAVRV-----EDPKDVRGALREA 516
|
170
....*....|.
gi 1900713664 190 HQHKGTSFIEV 200
Cdd:PRK06546 517 FAHPGPALVDV 527
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
45-139 |
1.54e-03 |
|
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: 38.62 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900713664 45 EDIVFISGIGCSSRFPYYM----NTYGMHSIHGRAPAIATGLKITNPDLsiwVITGDGDG--------LSIGGNH----L 108
Cdd:cd02001 13 GDTPIVSTTGYASRELYDVqdrdGHFYMLGSMGLAGSIGLGLALGLSRK---VIVVDGDGsllmnpgvLLTAGEFtplnL 89
|
90 100 110
....*....|....*....|....*....|.
gi 1900713664 109 IHLLrrnvdlnvllFNNQIYGLTKGQYSPTS 139
Cdd:cd02001 90 ILVV----------LDNRAYGSTGGQPTPSS 110
|
|
|