|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
6-338 |
3.19e-148 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 418.86 E-value: 3.19e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 6 TIARTTTLKDWETDQEVRWCPGCGDYAILKAVQRTLPEIGAVPESTVFISGIGCSSRFPYYVESYGFHTIHGRAPAFATG 85
Cdd:PRK11867 1 MTDPMLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 86 LKLANPELDVWIVTGDGDGLSIGGNHTMHLIRRNLDCQIMLFNNEIYGLTKGQYSPTSRVGTNSPSTPFGSVDRPAQPCA 165
Cdd:PRK11867 81 LKLANPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 166 FALGAGARFVARGFDVS-KELPNVLKAAHAHKGAAFIEIFQNCIVYNKD-VFQDFAAPkgaedrqlwlqngepmlfakga 243
Cdd:PRK11867 161 LALGAGATFVARGFDSDvKQLTELIKAAINHKGFSFVEILQPCPTFNNVnTFDWFKER---------------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 244 kgialdqealtlkvvdvvdgdwqaaGVIVHDVTNRSVAHMLVEMRFGE--FPMALGVLYDDPRPTFEADVWRQNKaaaeg 321
Cdd:PRK11867 219 -------------------------LVKVHDAEGYDPTNALAAMKTLEegDPIPTGIFYQVERPTYEEAVRAQIE----- 268
|
330
....*....|....*..
gi 1015414101 322 KKADLQSLLKKGQTWTV 338
Cdd:PRK11867 269 GPLALQDLLMGGDTWTV 285
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
24-210 |
7.91e-103 |
|
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: 300.21 E-value: 7.91e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 24 WCPGCGDYAILKAVQRTLPEIGAVPESTVFISGIGCSSRFPYYVESYGFHTIHGRAPAFATGLKLANPELDVWIVTGDGD 103
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 104 GLSIGGNHTMHLIRRNLDCQIMLFNNEIYGLTKGQYSPTSRVGTNSPSTPFGSVDRPAQPCAFALGAGARFVARGFDVS- 182
Cdd:cd03375 81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDi 160
|
170 180
....*....|....*....|....*...
gi 1015414101 183 KELPNVLKAAHAHKGAAFIEIFQNCIVY 210
Cdd:cd03375 161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
12-212 |
5.88e-87 |
|
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: 262.39 E-value: 5.88e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 12 TLKDWETDQEVRWCPGCGDYAILKAVQRTLPEIGaVPESTVFISGIGCSSRFPYYVESYGFHTIHGRAPAFATGLKLANP 91
Cdd:COG1013 3 KKKDLLRTPGHRWCPGCGHGIILRLLLKALDELL-DGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 92 ELDVWIVTGDGDGLSIGGNHTMHLIRRNLDCQIMLFNNEIYGLTKGQYSPTSRVGTNSPSTPFGSVDRPAQPCAFALGAG 171
Cdd:COG1013 82 DLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1015414101 172 ARFVARGFDVS-KELPNVLKAAHAHKGAAFIEIFQNCIVYNK 212
Cdd:COG1013 162 ATYVARASVGDpKDLKKKIKKAIEHKGFSFIEVLSPCPTGWG 203
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
22-212 |
2.10e-78 |
|
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: 241.59 E-value: 2.10e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 22 VRWCPGCGDYAILKAVQRTLPEIGAVPESTVFISGIGCSSRFPYYVESYGFHTIHGRAPAFATGLKLANPELDVWIVTGD 101
Cdd:TIGR02177 1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 102 GDGLSIGGNHTMHLIRRNLDCQIMLFNNEIYGLTKGQYSPTSRVGTNSPSTPFGSVDRPAQPCAFALGAGARFVARGF-- 179
Cdd:TIGR02177 81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFsg 160
|
170 180 190
....*....|....*....|....*....|...
gi 1015414101 180 DVsKELPNVLKAAHAHKGAAFIEIFQNCIVYNK 212
Cdd:TIGR02177 161 DV-AHLKEIIKEAINHKGYALVDILQPCVTYNK 192
|
|
| Oxoac_fdxbeta_Archa |
NF041171 |
2-oxoacid:ferredoxin oxidoreductase subunit beta; |
22-211 |
3.86e-69 |
|
2-oxoacid:ferredoxin oxidoreductase subunit beta;
Pssm-ID: 469082 [Multi-domain] Cd Length: 296 Bit Score: 218.27 E-value: 3.86e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 22 VRWCPGCGDYAILKAVQRTLPEIGAVPESTVFISGIGCSSRFPYYVESYGFHTIHGRAPAFATGLKLANPELDVWIVTGD 101
Cdd:NF041171 3 VDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 102 GDGLSIGGNHTMHLIRRNLDCQIMLFNNEIYGLTKGQYSPTSRVGTNSPSTPFGSVDRPAQPCAFALGAGARFVARG--F 179
Cdd:NF041171 83 GDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGyaY 162
|
170 180 190
....*....|....*....|....*....|..
gi 1015414101 180 DVsKELPNVLKAAHAHKGAAFIEIFQNCIVYN 211
Cdd:NF041171 163 DV-KHLKELIKAAIKHKGLAFIDVLQPCPTYN 193
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
56-203 |
8.19e-25 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 98.04 E-value: 8.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 56 GIGCSSRF---------PYYVESYGFHTIHGRAPAFATGLKLANPELDVWIVTGDGDGLSIgGNHTMHLIRRNLDCQIML 126
Cdd:pfam02775 1 DIGCHQMWaaqyyrfrpPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMN-LQELATAVRYNLPITVVV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1015414101 127 FNNEIYGLTKGQYSPTsrvGTNSPSTPFGSVDRPAQPCAFALGAGARfVARgFDVSKELPNVLKAAHAHKGAAFIEI 203
Cdd:pfam02775 80 LNNGGYGMTRGQQTPF---GGGRYSGPSGKILPPVDFAKLAEAYGAK-GAR-VESPEELEEALKEALEHDGPALIDV 151
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
6-338 |
3.19e-148 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 418.86 E-value: 3.19e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 6 TIARTTTLKDWETDQEVRWCPGCGDYAILKAVQRTLPEIGAVPESTVFISGIGCSSRFPYYVESYGFHTIHGRAPAFATG 85
Cdd:PRK11867 1 MTDPMLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 86 LKLANPELDVWIVTGDGDGLSIGGNHTMHLIRRNLDCQIMLFNNEIYGLTKGQYSPTSRVGTNSPSTPFGSVDRPAQPCA 165
Cdd:PRK11867 81 LKLANPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 166 FALGAGARFVARGFDVS-KELPNVLKAAHAHKGAAFIEIFQNCIVYNKD-VFQDFAAPkgaedrqlwlqngepmlfakga 243
Cdd:PRK11867 161 LALGAGATFVARGFDSDvKQLTELIKAAINHKGFSFVEILQPCPTFNNVnTFDWFKER---------------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 244 kgialdqealtlkvvdvvdgdwqaaGVIVHDVTNRSVAHMLVEMRFGE--FPMALGVLYDDPRPTFEADVWRQNKaaaeg 321
Cdd:PRK11867 219 -------------------------LVKVHDAEGYDPTNALAAMKTLEegDPIPTGIFYQVERPTYEEAVRAQIE----- 268
|
330
....*....|....*..
gi 1015414101 322 KKADLQSLLKKGQTWTV 338
Cdd:PRK11867 269 GPLALQDLLMGGDTWTV 285
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
24-210 |
7.91e-103 |
|
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: 300.21 E-value: 7.91e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 24 WCPGCGDYAILKAVQRTLPEIGAVPESTVFISGIGCSSRFPYYVESYGFHTIHGRAPAFATGLKLANPELDVWIVTGDGD 103
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 104 GLSIGGNHTMHLIRRNLDCQIMLFNNEIYGLTKGQYSPTSRVGTNSPSTPFGSVDRPAQPCAFALGAGARFVARGFDVS- 182
Cdd:cd03375 81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDi 160
|
170 180
....*....|....*....|....*...
gi 1015414101 183 KELPNVLKAAHAHKGAAFIEIFQNCIVY 210
Cdd:cd03375 161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
4-308 |
1.31e-89 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 270.60 E-value: 1.31e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 4 MTTIARTTTLKDWEtDQEVRWCPGCGDYAILKAVQRTLPEIGAVPESTVFISGIGCSSRFPYYVESYGFHTIHGRAPAFA 83
Cdd:PRK05778 1 LMKNALGLTYLRYD-GLPTTWCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 84 TGLKLANPELDVWIVTGDGDGLSIGGNHTMHLIRRNLDCQIMLFNNEIYGLTKGQYSPTSRVGTNSPSTPFGSVDRPAQP 163
Cdd:PRK05778 80 TGAKLANPDLEVIVVGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 164 CAFALGAGARFVARGF--DVsKELPNVLKAAHAHKGAAFIEIFQNCIVYNkDVfqdFAAPKGAEDRQLWLQNgepmlfak 241
Cdd:PRK05778 160 CALALAAGATFVARSFagDV-KQLVELIKKAISHKGFAFIDVLSPCVTFN-GR---NTSTKSPAYMREYYKK-------- 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1015414101 242 gakgialdqealtlKVVDVVDGDwqaagviVHDVTNRSVA--HMLVEMRFGEFPmaLGVLYDDPRPTFE 308
Cdd:PRK05778 227 --------------RVYKLKLEE-------DYDPTDRDKAaeKMLEEELGGKIP--IGVFYKNERPTFE 272
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
12-212 |
5.88e-87 |
|
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: 262.39 E-value: 5.88e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 12 TLKDWETDQEVRWCPGCGDYAILKAVQRTLPEIGaVPESTVFISGIGCSSRFPYYVESYGFHTIHGRAPAFATGLKLANP 91
Cdd:COG1013 3 KKKDLLRTPGHRWCPGCGHGIILRLLLKALDELL-DGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 92 ELDVWIVTGDGDGLSIGGNHTMHLIRRNLDCQIMLFNNEIYGLTKGQYSPTSRVGTNSPSTPFGSVDRPAQPCAFALGAG 171
Cdd:COG1013 82 DLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1015414101 172 ARFVARGFDVS-KELPNVLKAAHAHKGAAFIEIFQNCIVYNK 212
Cdd:COG1013 162 ATYVARASVGDpKDLKKKIKKAIEHKGFSFIEVLSPCPTGWG 203
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
22-212 |
2.10e-78 |
|
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: 241.59 E-value: 2.10e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 22 VRWCPGCGDYAILKAVQRTLPEIGAVPESTVFISGIGCSSRFPYYVESYGFHTIHGRAPAFATGLKLANPELDVWIVTGD 101
Cdd:TIGR02177 1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 102 GDGLSIGGNHTMHLIRRNLDCQIMLFNNEIYGLTKGQYSPTSRVGTNSPSTPFGSVDRPAQPCAFALGAGARFVARGF-- 179
Cdd:TIGR02177 81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFsg 160
|
170 180 190
....*....|....*....|....*....|...
gi 1015414101 180 DVsKELPNVLKAAHAHKGAAFIEIFQNCIVYNK 212
Cdd:TIGR02177 161 DV-AHLKEIIKEAINHKGYALVDILQPCVTYNK 192
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
24-212 |
2.44e-73 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 228.49 E-value: 2.44e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 24 WCPGCGDYAILKAVQRTLPEIGAVPESTVFISGIGCSSRFPYYVESYGFHTIHGRAPAFATGLKLANPELDVWIVTGDGD 103
Cdd:PRK11866 9 WCPGCGNYGILEALRKALAELGIPPENVVVVSGIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLTVIGYGGDGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 104 GLSIGGNHTMHLIRRNLDCQIMLFNNEIYGLTKGQYSPTSRVGTNSPSTPFGSVDRPAQPCAFALGAGARFVARGF--DV 181
Cdd:PRK11866 89 GYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATFVARGFsgDV 168
|
170 180 190
....*....|....*....|....*....|.
gi 1015414101 182 sKELPNVLKAAHAHKGAAFIEIFQNCIVYNK 212
Cdd:PRK11866 169 -KHLKEIIKEAIKHKGFSFIDVLSPCVTFNK 198
|
|
| Oxoac_fdxbeta_Archa |
NF041171 |
2-oxoacid:ferredoxin oxidoreductase subunit beta; |
22-211 |
3.86e-69 |
|
2-oxoacid:ferredoxin oxidoreductase subunit beta;
Pssm-ID: 469082 [Multi-domain] Cd Length: 296 Bit Score: 218.27 E-value: 3.86e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 22 VRWCPGCGDYAILKAVQRTLPEIGAVPESTVFISGIGCSSRFPYYVESYGFHTIHGRAPAFATGLKLANPELDVWIVTGD 101
Cdd:NF041171 3 VDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 102 GDGLSIGGNHTMHLIRRNLDCQIMLFNNEIYGLTKGQYSPTSRVGTNSPSTPFGSVDRPAQPCAFALGAGARFVARG--F 179
Cdd:NF041171 83 GDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGyaY 162
|
170 180 190
....*....|....*....|....*....|..
gi 1015414101 180 DVsKELPNVLKAAHAHKGAAFIEIFQNCIVYN 211
Cdd:NF041171 163 DV-KHLKELIKAAIKHKGLAFIDVLQPCPTYN 193
|
|
| PRK11869 |
PRK11869 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
19-311 |
9.53e-61 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183349 [Multi-domain] Cd Length: 280 Bit Score: 196.16 E-value: 9.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 19 DQEVRWCPGCGDYAILKAVQRTLPEIGAVPESTVFISGIGCSSRFPYYVESYGFHTIHGRAPAFATGLKLANPELDVWIV 98
Cdd:PRK11869 5 KYDIAWCPGCGNFGIRNALMKALSELNLKPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTVIAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 99 TGDGDGLSIGGNHTMHLIRRNLDCQIMLFNNEIYGLTKGQYSPTSRVGTNSPSTPFGSVDRPAQPCAFALGAGARFVARG 178
Cdd:PRK11869 85 GGDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASFVART 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 179 F--DVsKELPNVLKAAHAHKGAAFIEIFQNCIVYNK-DVFQDFaapkgaEDRQLWLQNgepmlfakgakgialdqealtl 255
Cdd:PRK11869 165 FsgDI-EETKEILKEAIKHKGLAIVDIFQPCVSFNKvNTYQWY------RENTYYLKD---------------------- 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1015414101 256 kvvdvvdgdwqaagvivHDVTNRSVAhmlVEMRFGEFPMALGVLYDDPRPTFEADV 311
Cdd:PRK11869 216 -----------------HDPTDRELA---FKRALETEKLPLGIFYINEKPTFEELV 251
|
|
| oorB |
PRK09628 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; |
24-207 |
8.11e-60 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
Pssm-ID: 182003 [Multi-domain] Cd Length: 277 Bit Score: 193.41 E-value: 8.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 24 WCPGCGDYAILKAVQRTLPEIGAVPESTVFISGIGCSSRFPYYVESYGFHTIHGRAPAFATGLKLANPELDVWIVTGDGD 103
Cdd:PRK09628 18 WCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGIKLANPDKHVIVVSGDGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 104 GLSIGGNHTMHLIRRNLDCQIMLFNNEIYGLTKGQYSPTSRVGTNSPSTPFGSVDRPAQPCAFALGAGARFVARGFDV-S 182
Cdd:PRK09628 98 GLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKLATAAGASFVARESVIdP 177
|
170 180
....*....|....*....|....*
gi 1015414101 183 KELPNVLKAAHAHKGAAFIEIFQNC 207
Cdd:PRK09628 178 QKLEKLLVKGFSHKGFSFFDVFSNC 202
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
56-203 |
8.19e-25 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 98.04 E-value: 8.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 56 GIGCSSRF---------PYYVESYGFHTIHGRAPAFATGLKLANPELDVWIVTGDGDGLSIgGNHTMHLIRRNLDCQIML 126
Cdd:pfam02775 1 DIGCHQMWaaqyyrfrpPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMN-LQELATAVRYNLPITVVV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1015414101 127 FNNEIYGLTKGQYSPTsrvGTNSPSTPFGSVDRPAQPCAFALGAGARfVARgFDVSKELPNVLKAAHAHKGAAFIEI 203
Cdd:pfam02775 80 LNNGGYGMTRGQQTPF---GGGRYSGPSGKILPPVDFAKLAEAYGAK-GAR-VESPEELEEALKEALEHDGPALIDV 151
|
|
| TPP_PFOR |
cd02018 |
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ... |
25-177 |
1.30e-16 |
|
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) subfamily, TPP-binding module; PFOR catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. PFORs can be homodimeric, heterodimeric, or heterotetrameric, depending on the organism. These enzymes are dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238976 [Multi-domain] Cd Length: 237 Bit Score: 77.91 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 25 CPGCGDYAILKAVQRTLPEigavPESTVFISGIGCSS----RFPYyvESYGFHTIH---GRAPAFATGLKLA----NPEL 93
Cdd:cd02018 8 CAGCGEVTAVRVVLAALPA----PEDTVIANSTGCSSvyasTAPF--NSWAVPWVNslfEDANAVASGLKRGlkarFPKD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 94 -------DVWIVTGDGDGLSIGGNHTMHLIRRNLDCQIMLFNNEIYGLTKGQYSPTSRVGTNSPSTPFGSVDRPAQPCAF 166
Cdd:cd02018 82 reldkkkDVVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKKDLVLI 161
|
170
....*....|.
gi 1015414101 167 ALGAGARFVAR 177
Cdd:cd02018 162 AATHGCVYVAR 172
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
46-175 |
5.31e-09 |
|
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: 54.57 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 46 AVPESTVFISGIGCSSRFPYYV------ESYGFHTIHGR---APAFATGLKLANPELDVWIVTGDGdGLSIGGNHTMHLI 116
Cdd:cd00568 9 ALPEDAIVVNDAGNSAYWAYRYlplrrgRRFLTSTGFGAmgyGLPAAIGAALAAPDRPVVCIAGDG-GFMMTGQELATAV 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1015414101 117 RRNLDCQIMLFNNEIYGLTKGQYSPtsrvgtNSPSTPFGSVDRPAQPCAFALGAGARFV 175
Cdd:cd00568 88 RYGLPVIVVVFNNGGYGTIRMHQEA------FYGGRVSGTDLSNPDFAALAEAYGAKGV 140
|
|
| PRK11865 |
PRK11865 |
pyruvate synthase subunit beta; |
23-176 |
5.92e-07 |
|
pyruvate synthase subunit beta;
Pssm-ID: 183346 [Multi-domain] Cd Length: 299 Bit Score: 50.48 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 23 RWCPGCGDYAILKAVQRtlpeigAVPESTVFISGIGCSS----RFPYyvESYGFHTIH---GRAPAFATG----LKLANP 91
Cdd:PRK11865 19 RACAGCGAAIAMRLALK------ALGKNTVIVVATGCLEvittPYPE--TAWNVPWIHvafENAAAVASGieraVKALGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 92 ELDVWIVTGDGDGLSIGGNHTMHLIRRNLDCQIMLFNNEIYGLTKGQYSPTSRVGTNSPSTPFGSV----DRPAQPCAFA 167
Cdd:PRK11865 91 KVNVVAIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKYsrgeDRPKKNMPLI 170
|
170
....*....|
gi 1015414101 168 LGA-GARFVA 176
Cdd:PRK11865 171 MAAhGIPYVA 180
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
31-154 |
3.33e-05 |
|
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: 43.67 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 31 YAILKAVQRTLPE--I----GAvpeSTVFISGIGCSSRFPY-YVESYGFHTIhGRAPAFATGLKLANPELDVWIVTGDGD 103
Cdd:cd02004 2 YRVLHELQEALPDdaIivsdGG---NTMDWARYILRPRKPRhRLDAGTFGTL-GVGLGYAIAAALARPDKRVVLVEGDGA 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1015414101 104 -GLSIGGNHTMhlIRRNLDCQIMLFNNE-IYGLTKGQ---YSPTSRVGTNSPSTPF 154
Cdd:cd02004 78 fGFSGMELETA--VRYNLPIVVVVGNNGgWYQGLDGQqlsYGLGLPVTTLLPDTRY 131
|
|
| TPP_PFOR_porB_like |
cd03376 |
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ... |
23-156 |
1.02e-04 |
|
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: 43.00 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 23 RWCPGCGDYAILKAVQRtlpeigAVPESTVFISGIGCSSRF--PYYVESY---GFHTIHGRAPAFATGLKLA------NP 91
Cdd:cd03376 6 RACAGCGAALALRHVLK------ALGPDTVVVNPTGCLEVIttPYPYTAWrvpWIHVAFENAAAVASGIEAAlkalgrGK 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1015414101 92 ELDVWIVTGDGDGLSIGGNHTMHLIRRNLDCQIMLFNNEIYGLTKGQysptsrvgtNSPSTPFGS 156
Cdd:cd03376 80 DITVVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQ---------RSGSTPYGA 135
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
35-204 |
4.44e-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: 40.76 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 35 KAVQRTLPEIgavPESTVFISGIGCSSRFPYYVE-------SYGFHTI--HGRAPAFATGLKLANPELDVWIVTGDG--- 102
Cdd:cd03371 3 DAIEIVLSRA---PATAAVVSTTGMTSRELFELRdrpggghAQDFLTVgsMGHASQIALGIALARPDRKVVCIDGDGaal 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 103 ---DGLSIGGNHTMhlirRNLdcqI-MLFNNEIYGLTKGQysPTSrvgtnSPSTPFGSVdrpaqpcafALGAGARFVARG 178
Cdd:cd03371 80 mhmGGLATIGGLAP----ANL---IhIVLNNGAHDSVGGQ--PTV-----SFDVSLPAI---------AKACGYRAVYEV 136
|
170 180
....*....|....*....|....*.
gi 1015414101 179 FDvSKELPNVLKAAHAHKGAAFIEIF 204
Cdd:cd03371 137 PS-LEELVAALAKALAADGPAFIEVK 161
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
77-189 |
5.81e-04 |
|
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: 40.27 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 77 GRAPAFATGLKLANPELDVWIVTGDGDGL-SIGGNHTMhlIRRNLDCQIMLFNNEIYGLTKgqySPTSRVGTNSPSTPFG 155
Cdd:cd02002 52 GWGLPAAVGAALANPDRKVVAIIGDGSFMyTIQALWTA--ARYGLPVTVVILNNRGYGALR---SFLKRVGPEGPGENAP 126
|
90 100 110
....*....|....*....|....*....|....*...
gi 1015414101 156 SV---DRPA-QPCAFALGAGARfvARGFDVSKELPNVL 189
Cdd:cd02002 127 DGldlLDPGiDFAAIAKAFGVE--AERVETPEELDEAL 162
|
|
| TPP_PFOR_PNO |
cd03377 |
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ... |
95-183 |
9.75e-04 |
|
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: 40.67 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 95 VWIVTGDGDGLSIGGNHTMHLIRRNLDCQIMLFNNEIYGLTKGQysptsrvgtNSPSTPFGSVdrpaqpcafalgagARF 174
Cdd:cd03377 154 VWIIGGDGWAYDIGYGGLDHVLASGENVNILVLDTEVYSNTGGQ---------ASKATPLGAV--------------AKF 210
|
....*....
gi 1015414101 175 VARGFDVSK 183
Cdd:cd03377 211 AAAGKRTGK 219
|
|
| PFO_beta_C |
pfam12367 |
Pyruvate ferredoxin oxidoreductase beta subunit C terminal; This domain family is found in ... |
273-308 |
1.10e-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: 36.70 E-value: 1.10e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1015414101 273 HDVTNRSVAhMLVEMRFGEfPMALGVLYDDPRPTFE 308
Cdd:pfam12367 24 HDPTDREAA-MEKALEWGD-RIPIGIFYKEERPTFE 57
|
|
| PRK08266 |
PRK08266 |
hypothetical protein; Provisional |
32-133 |
2.38e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 181337 [Multi-domain] Cd Length: 542 Bit Score: 39.61 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 32 AILKAVQRTLPEIGAVPEStvfISGIGCSSRFPY-------YVES-------YGFHTihgrapafATGLKLANPELDVWI 97
Cdd:PRK08266 357 SYLRAIREALPDDGIFVDE---LSQVGFASWFAFpvyaprtFVTCgyqgtlgYGFPT--------ALGAKVANPDRPVVS 425
|
90 100 110
....*....|....*....|....*....|....*.
gi 1015414101 98 VTGDGdGLSIGGNHTMHLIRRNLDCQIMLFNNEIYG 133
Cdd:PRK08266 426 ITGDG-GFMFGVQELATAVQHNIGVVTVVFNNNAYG 460
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
82-161 |
2.39e-03 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 39.74 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 82 FATGLKLANPELDVWIVTGDGdglsiGGNHT---MHLIRR-NLDCQIMLFNNEIYGLTKgqYSPTSRVGTNSPSTPFGSV 157
Cdd:PRK06112 445 MAIGAKVARPGAPVICLVGDG-----GFAHVwaeLETARRmGVPVTIVVLNNGILGFQK--HAETVKFGTHTDACHFAAV 517
|
....
gi 1015414101 158 DRPA 161
Cdd:PRK06112 518 DHAA 521
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
27-137 |
4.02e-03 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 38.82 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015414101 27 GCGDYAIL-KAVQRTLPEIGAVPEStVFISGIGCSSR-FPYYVESYGFHTIH---GRAPAFATGLKLANPELDVWIVTGD 101
Cdd:PRK07064 354 GLGPYAKLvDALRAALPRDGNWVRD-VTISNSTWGNRlLPIFEPRANVHALGggiGQGLAMAIGAALAGPGRKTVGLVGD 432
|
90 100 110
....*....|....*....|....*....|....*.
gi 1015414101 102 GdGLSIGGNHTMHLIRRNLDCQIMLFNNEIYGLTKG 137
Cdd:PRK07064 433 G-GLMLNLGELATAVQENANMVIVLMNDGGYGVIRN 467
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
80-134 |
8.15e-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: 36.71 E-value: 8.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1015414101 80 PAfATGLKLANPELDVWIVTGDGdglSIGGN-HTMHLIRR-NLDCQIMLFNNEIYGL 134
Cdd:cd02015 57 PA-AIGAKVARPDKTVICIDGDG---SFQMNiQELATAAQyNLPVKIVILNNGSLGM 109
|
|
| |
