|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
1-283 |
0e+00 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 513.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 1 MATFKDFRNNVKPNWCPGCGDFSVQAAIQKAAANIGLEPEEVAIITGIGCSGRLSGYINSYGVHSIHGRALPLAQGVKMA 80
Cdd:PRK11867 5 MLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGLKLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 81 NKDLTVIASGGDGDGYAIGMGHTIHALRRNMNMTYIVMDNQIYGLTKGQTSPSSAVGFVTKTTPKGNIEKNVAPLELALS 160
Cdd:PRK11867 85 NPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVELALG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 161 SGATFVAQGFSSDIKGLTKLIEDAINHDGFSFVNVFSPCVTYNKINTYDWFKEHLTSVDDIENYDSTDKQLATKTVIEHE 240
Cdd:PRK11867 165 AGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFNNVNTFDWFKERLVKVHDAEGYDPTNALAAMKTLEEGD 244
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446112283 241 SLVTGIVYQDkETPSYESQIKELDDTPLAKRDIKITEDTFNAL 283
Cdd:PRK11867 245 PIPTGIFYQV-ERPTYEEAVRAQIEGPLALQDLLMGGDTWTVL 286
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
15-202 |
2.55e-123 |
|
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: 349.90 E-value: 2.55e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 15 WCPGCGDFSVQAAIQKAAANIGLEPEEVAIITGIGCSGRLSGYINSYGVHSIHGRALPLAQGVKMANKDLTVIASGGDGD 94
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 95 GYAIGMGHTIHALRRNMNMTYIVMDNQIYGLTKGQTSPSSAVGFVTKTTPKGNIEKNVAPLELALSSGATFVAQGFSSDI 174
Cdd:cd03375 81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160
|
170 180
....*....|....*....|....*...
gi 446112283 175 KGLTKLIEDAINHDGFSFVNVFSPCVTY 202
Cdd:cd03375 161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
3-263 |
1.02e-119 |
|
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: 343.66 E-value: 1.02e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 3 TFKDFRNNVKPNWCPGCGDFSVQAAIQKAAANIgLEPEEVAIITGIGCSGRLSGYINSYGVHSIHGRALPLAQGVKMANK 82
Cdd:COG1013 3 KKKDLLRTPGHRWCPGCGHGIILRLLLKALDEL-LDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 83 DLTVIASGGDGDGYAIGMGHTIHALRRNMNMTYIVMDNQIYGLTKGQTSPSSAVGFVTKTTPKGNIEKNVAPLELALSSG 162
Cdd:COG1013 82 DLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 163 ATFVAQGFSSDIKGLTKLIEDAINHDGFSFVNVFSPCVTYNKIN---TYDWFKEHLTSVDDIENYDSTdkqlaTKTVIEH 239
Cdd:COG1013 162 ATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRDpskTIEWAKEGMWPLYEYDPGEKL-----RLTYEPK 236
|
250 260
....*....|....*....|....
gi 446112283 240 ESLVTGIVYQDKEtpSYESQIKEL 263
Cdd:COG1013 237 DKIPVGEFLKNQG--RFEELIEEI 258
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
13-285 |
1.65e-117 |
|
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: 339.05 E-value: 1.65e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 13 PNWCPGCGDFSVQAAIQKAAANIGLEPEEVAIITGIGCSGRLSGYINSYGVHSIHGRALPLAQGVKMANKDLTVIASGGD 92
Cdd:TIGR02177 1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 93 GDGYAIGMGHTIHALRRNMNMTYIVMDNQIYGLTKGQTSPSSAVGFVTKTTPKGNIEKNVAPLELALSSGATFVAQGFSS 172
Cdd:TIGR02177 81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 173 DIKGLTKLIEDAINHDGFSFVNVFSPCVTYNKINTYDWFKEHLTSVDDiENYDSTDKQ---------LATKTVIE-HESL 242
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNKINTYEWYRERVYKLDE-EGYDPIVREpeefeekaaAAIKKAMEwGDRI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446112283 243 VTGIVYQDKETPSYESQIKEL----DDTPLAKRDIKIT-EDTFNALTE 285
Cdd:TIGR02177 240 PIGIFYKNENKPTFEERLEKIlpryMSAPPAEQEIKPPiEKPKELLEE 287
|
|
| Oxoac_fdxbeta_Archa |
NF041171 |
2-oxoacid:ferredoxin oxidoreductase subunit beta; |
13-273 |
8.80e-103 |
|
2-oxoacid:ferredoxin oxidoreductase subunit beta;
Pssm-ID: 469082 [Multi-domain] Cd Length: 296 Bit Score: 301.86 E-value: 8.80e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 13 PNWCPGCGDFSVQAAIQKAAANIGLEPEEVAIITGIGCSGRLSGYINSYGVHSIHGRALPLAQGVKMANKDLTVIASGGD 92
Cdd:NF041171 3 VDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 93 GDGYAIGMGHTIHALRRNMNMTYIVMDNQIYGLTKGQTSPSSAVGFVTKTTPKGNIEKNVAPLELALSSGATFVAQGFSS 172
Cdd:NF041171 83 GDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 173 DIKGLTKLIEDAINHDGFSFVNVFSPCVTYNKINTYDWFKEHLTSVDDIENYD------STDKQLATKTVIEH----ESL 242
Cdd:NF041171 163 DVKHLKELIKAAIKHKGLAFIDVLQPCPTYNDINTKEWYDKRVYKLDDEPGWDpvvrspEEADEKMAKAIEKAlewgDRI 242
|
250 260 270
....*....|....*....|....*....|....*.
gi 446112283 243 VTGIVYQDKETPSYESQIKE-----LDDTPlAKRDI 273
Cdd:NF041171 243 PIGIFYQNELVPTFEERIAErlpnyLDNPP-AKQPI 277
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
47-195 |
1.23e-37 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 130.40 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 47 GIGCSG----------RLSGYINSYGvHSIHGRALPLAQGVKMANKDLTVIASGGDGDGYAIGMgHTIHALRRNMNMTYI 116
Cdd:pfam02775 1 DIGCHQmwaaqyyrfrPPRRYLTSGG-LGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQ-ELATAVRYNLPITVV 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446112283 117 VMDNQIYGLTKGQTSPSsavGFVTKTTPKGNIEKNVAPLELALSSGATFVaqgFSSDIKGLTKLIEDAINHDGFSFVNV 195
Cdd:pfam02775 79 VLNNGGYGMTRGQQTPF---GGGRYSGPSGKILPPVDFAKLAEAYGAKGA---RVESPEELEEALKEALEHDGPALIDV 151
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
1-283 |
0e+00 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 513.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 1 MATFKDFRNNVKPNWCPGCGDFSVQAAIQKAAANIGLEPEEVAIITGIGCSGRLSGYINSYGVHSIHGRALPLAQGVKMA 80
Cdd:PRK11867 5 MLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGLKLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 81 NKDLTVIASGGDGDGYAIGMGHTIHALRRNMNMTYIVMDNQIYGLTKGQTSPSSAVGFVTKTTPKGNIEKNVAPLELALS 160
Cdd:PRK11867 85 NPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVELALG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 161 SGATFVAQGFSSDIKGLTKLIEDAINHDGFSFVNVFSPCVTYNKINTYDWFKEHLTSVDDIENYDSTDKQLATKTVIEHE 240
Cdd:PRK11867 165 AGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFNNVNTFDWFKERLVKVHDAEGYDPTNALAAMKTLEEGD 244
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446112283 241 SLVTGIVYQDkETPSYESQIKELDDTPLAKRDIKITEDTFNAL 283
Cdd:PRK11867 245 PIPTGIFYQV-ERPTYEEAVRAQIEGPLALQDLLMGGDTWTVL 286
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
4-281 |
1.74e-132 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 377.30 E-value: 1.74e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 4 FKDFRNNVKPN-WCPGCGDFSVQAAIQKAAANIGLEPEEVAIITGIGCSGRLSGYINSYGVHSIHGRALPLAQGVKMANK 82
Cdd:PRK05778 8 LTYLRYDGLPTtWCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLANP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 83 DLTVIASGGDGDGYAIGMGHTIHALRRNMNMTYIVMDNQIYGLTKGQTSPSSAVGFVTKTTPKGNIEKNVAPLELALSSG 162
Cdd:PRK05778 88 DLEVIVVGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAAG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 163 ATFVAQGFSSDIKGLTKLIEDAINHDGFSFVNVFSPCVTYNKINTYD--------WFKEHLTSVDDIENYDSTDKQLATK 234
Cdd:PRK05778 168 ATFVARSFAGDVKQLVELIKKAISHKGFAFIDVLSPCVTFNGRNTSTkspaymreYYKKRVYKLKLEEDYDPTDRDKAAE 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446112283 235 TVIEHES---LVTGIVYQDkETPSYESQIKELDD-----TPLAKRDIKITEDTFN 281
Cdd:PRK05778 248 KMLEEELggkIPIGVFYKN-ERPTFEERLEKLIEpllelPPAALRPGKEALDTIN 301
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
15-202 |
2.55e-123 |
|
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: 349.90 E-value: 2.55e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 15 WCPGCGDFSVQAAIQKAAANIGLEPEEVAIITGIGCSGRLSGYINSYGVHSIHGRALPLAQGVKMANKDLTVIASGGDGD 94
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 95 GYAIGMGHTIHALRRNMNMTYIVMDNQIYGLTKGQTSPSSAVGFVTKTTPKGNIEKNVAPLELALSSGATFVAQGFSSDI 174
Cdd:cd03375 81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160
|
170 180
....*....|....*....|....*...
gi 446112283 175 KGLTKLIEDAINHDGFSFVNVFSPCVTY 202
Cdd:cd03375 161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
7-269 |
6.13e-120 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 344.82 E-value: 6.13e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 7 FRNNVKPNWCPGCGDFSVQAAIQKAAANIGLEPEEVAIITGIGCSGRLSGYINSYGVHSIHGRALPLAQGVKMANKDLTV 86
Cdd:PRK11866 1 YAVKRPPIWCPGCGNYGILEALRKALAELGIPPENVVVVSGIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 87 IASGGDGDGYAIGMGHTIHALRRNMNMTYIVMDNQIYGLTKGQTSPSSAVGFVTKTTPKGNIEKNVAPLELALSSGATFV 166
Cdd:PRK11866 81 IGYGGDGDGYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 167 AQGFSSDIKGLTKLIEDAINHDGFSFVNVFSPCVTYNKINTYDWFKEHLTSVDDIENyDSTDKQLATKTVIEHESLV-TG 245
Cdd:PRK11866 161 ARGFSGDVKHLKEIIKEAIKHKGFSFIDVLSPCVTFNKLNTYDWFRPRVYKLEETGH-DPTNFEQAYKKALEWGDRIpIG 239
|
250 260
....*....|....*....|....*
gi 446112283 246 IVYqDKETPSYESQIKE-LDDTPLA 269
Cdd:PRK11866 240 VFY-KEEKPTYEEELDEiLKNPPLA 263
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
3-263 |
1.02e-119 |
|
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: 343.66 E-value: 1.02e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 3 TFKDFRNNVKPNWCPGCGDFSVQAAIQKAAANIgLEPEEVAIITGIGCSGRLSGYINSYGVHSIHGRALPLAQGVKMANK 82
Cdd:COG1013 3 KKKDLLRTPGHRWCPGCGHGIILRLLLKALDEL-LDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 83 DLTVIASGGDGDGYAIGMGHTIHALRRNMNMTYIVMDNQIYGLTKGQTSPSSAVGFVTKTTPKGNIEKNVAPLELALSSG 162
Cdd:COG1013 82 DLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 163 ATFVAQGFSSDIKGLTKLIEDAINHDGFSFVNVFSPCVTYNKIN---TYDWFKEHLTSVDDIENYDSTdkqlaTKTVIEH 239
Cdd:COG1013 162 ATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRDpskTIEWAKEGMWPLYEYDPGEKL-----RLTYEPK 236
|
250 260
....*....|....*....|....
gi 446112283 240 ESLVTGIVYQDKEtpSYESQIKEL 263
Cdd:COG1013 237 DKIPVGEFLKNQG--RFEELIEEI 258
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
13-285 |
1.65e-117 |
|
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: 339.05 E-value: 1.65e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 13 PNWCPGCGDFSVQAAIQKAAANIGLEPEEVAIITGIGCSGRLSGYINSYGVHSIHGRALPLAQGVKMANKDLTVIASGGD 92
Cdd:TIGR02177 1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 93 GDGYAIGMGHTIHALRRNMNMTYIVMDNQIYGLTKGQTSPSSAVGFVTKTTPKGNIEKNVAPLELALSSGATFVAQGFSS 172
Cdd:TIGR02177 81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 173 DIKGLTKLIEDAINHDGFSFVNVFSPCVTYNKINTYDWFKEHLTSVDDiENYDSTDKQ---------LATKTVIE-HESL 242
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNKINTYEWYRERVYKLDE-EGYDPIVREpeefeekaaAAIKKAMEwGDRI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446112283 243 VTGIVYQDKETPSYESQIKEL----DDTPLAKRDIKIT-EDTFNALTE 285
Cdd:TIGR02177 240 PIGIFYKNENKPTFEERLEKIlpryMSAPPAEQEIKPPiEKPKELLEE 287
|
|
| Oxoac_fdxbeta_Archa |
NF041171 |
2-oxoacid:ferredoxin oxidoreductase subunit beta; |
13-273 |
8.80e-103 |
|
2-oxoacid:ferredoxin oxidoreductase subunit beta;
Pssm-ID: 469082 [Multi-domain] Cd Length: 296 Bit Score: 301.86 E-value: 8.80e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 13 PNWCPGCGDFSVQAAIQKAAANIGLEPEEVAIITGIGCSGRLSGYINSYGVHSIHGRALPLAQGVKMANKDLTVIASGGD 92
Cdd:NF041171 3 VDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 93 GDGYAIGMGHTIHALRRNMNMTYIVMDNQIYGLTKGQTSPSSAVGFVTKTTPKGNIEKNVAPLELALSSGATFVAQGFSS 172
Cdd:NF041171 83 GDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 173 DIKGLTKLIEDAINHDGFSFVNVFSPCVTYNKINTYDWFKEHLTSVDDIENYD------STDKQLATKTVIEH----ESL 242
Cdd:NF041171 163 DVKHLKELIKAAIKHKGLAFIDVLQPCPTYNDINTKEWYDKRVYKLDDEPGWDpvvrspEEADEKMAKAIEKAlewgDRI 242
|
250 260 270
....*....|....*....|....*....|....*.
gi 446112283 243 VTGIVYQDKETPSYESQIKE-----LDDTPlAKRDI 273
Cdd:NF041171 243 PIGIFYQNELVPTFEERIAErlpnyLDNPP-AKQPI 277
|
|
| PRK11869 |
PRK11869 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
15-277 |
2.18e-96 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183349 [Multi-domain] Cd Length: 280 Bit Score: 285.14 E-value: 2.18e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 15 WCPGCGDFSVQAAIQKAAANIGLEPEEVAIITGIGCSGRLSGYINSYGVHSIHGRALPLAQGVKMANKDLTVIASGGDGD 94
Cdd:PRK11869 10 WCPGCGNFGIRNALMKALSELNLKPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTVIAEGGDGD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 95 GYAIGMGHTIHALRRNMNMTYIVMDNQIYGLTKGQTSPSSAVGFVTKTTPKGNIEKNVAPLELALSSGATFVAQGFSSDI 174
Cdd:PRK11869 90 MYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASFVARTFSGDI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 175 KGLTKLIEDAINHDGFSFVNVFSPCVTYNKINTYDWFKEHLTSVDDienYDSTDKQLATKTVIEHESLVTGIVYQDKEtP 254
Cdd:PRK11869 170 EETKEILKEAIKHKGLAIVDIFQPCVSFNKVNTYQWYRENTYYLKD---HDPTDRELAFKRALETEKLPLGIFYINEK-P 245
|
250 260
....*....|....*....|....*
gi 446112283 255 SYESQIK--ELDDTPLAKRDIKITE 277
Cdd:PRK11869 246 TFEELVPayKGDKTPLWKREPNFEK 270
|
|
| oorB |
PRK09628 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; |
15-275 |
1.49e-66 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
Pssm-ID: 182003 [Multi-domain] Cd Length: 277 Bit Score: 208.82 E-value: 1.49e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 15 WCPGCGDFSVQAAIQKAAANIGLEPEEVAIITGIGCSGRLSGYINSYGVHSIHGRALPLAQGVKMANKDLTVIASGGDGD 94
Cdd:PRK09628 18 WCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGIKLANPDKHVIVVSGDGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 95 GYAIGMGHTIHALRRNMNMTYIVMDNQIYGLTKGQTSPSSAVGFVTKTTPKGNIEKNVAPLELALSSGATFVAQGFSSDI 174
Cdd:PRK09628 98 GLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKLATAAGASFVARESVIDP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 175 KGLTKLIEDAINHDGFSFVNVFSPCVT----YNKIN----TYDWFKEHLTSVDDIENYDSTDKQlatktviehESLVTGI 246
Cdd:PRK09628 178 QKLEKLLVKGFSHKGFSFFDVFSNCHInlgrKNKMGeavqMLKWIESRTVSKRKFDALSPEERV---------GKFPTGI 248
|
250 260
....*....|....*....|....*....
gi 446112283 247 VYQDKETPSYESQIKELDDTPLAKRDIKI 275
Cdd:PRK09628 249 LKHDTDRKEYCEAYEEVIEAAQGKQKVDL 277
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
47-195 |
1.23e-37 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 130.40 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 47 GIGCSG----------RLSGYINSYGvHSIHGRALPLAQGVKMANKDLTVIASGGDGDGYAIGMgHTIHALRRNMNMTYI 116
Cdd:pfam02775 1 DIGCHQmwaaqyyrfrPPRRYLTSGG-LGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQ-ELATAVRYNLPITVV 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446112283 117 VMDNQIYGLTKGQTSPSsavGFVTKTTPKGNIEKNVAPLELALSSGATFVaqgFSSDIKGLTKLIEDAINHDGFSFVNV 195
Cdd:pfam02775 79 VLNNGGYGMTRGQQTPF---GGGRYSGPSGKILPPVDFAKLAEAYGAKGA---RVESPEELEEALKEALEHDGPALIDV 151
|
|
| TPP_PFOR |
cd02018 |
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ... |
16-207 |
3.28e-30 |
|
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: 113.74 E-value: 3.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 16 CPGCGDfsvQAAIQKAAANIGlEPEEVAIITGIGCSGRLSGYI--NSYGVHSIH---GRALPLAQGVKMA-----NKDL- 84
Cdd:cd02018 8 CAGCGE---VTAVRVVLAALP-APEDTVIANSTGCSSVYASTApfNSWAVPWVNslfEDANAVASGLKRGlkarfPKDRe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 85 -----TVIASGGDGDGYAIGMGHTIHALRRNMNMTYIVMDNQIYGLTKGQTSPSSAVGFVTKTTPKGNIEKNVAPLELAL 159
Cdd:cd02018 84 ldkkkDVVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKKDLVLIAA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446112283 160 SSGATFVAQGFSSDIKGLTKLIEDAI-NHDGFSFVNVFSPCVTYNKINT 207
Cdd:cd02018 164 THGCVYVARLSPALKKHFLKVVKEAIsRTDGPTFIHAYTPCITEWGIGS 212
|
|
| PFO_beta_C |
pfam12367 |
Pyruvate ferredoxin oxidoreductase beta subunit C terminal; This domain family is found in ... |
199-262 |
2.72e-22 |
|
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: 87.55 E-value: 2.72e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446112283 199 CVTYNKINTYDWFKEHLTSVDdiENYDSTDKQLATKTVIE-HESLVTGIVYQdKETPSYESQIKE 262
Cdd:pfam12367 1 CVTFNKVNTYDWYKERVYKLD--EDHDPTDREAAMEKALEwGDRIPIGIFYK-EERPTFEERLPV 62
|
|
| TPP_PFOR_porB_like |
cd03376 |
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ... |
16-201 |
1.51e-21 |
|
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: 90.38 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 16 CPGCGDFSVQAAIQKAAAniglepEEVAIITGIGCSGRLSG--YINSYGVHSIH---GRALPLAQGVKMA------NKDL 84
Cdd:cd03376 8 CAGCGAALALRHVLKALG------PDTVVVNPTGCLEVITTpyPYTAWRVPWIHvafENAAAVASGIEAAlkalgrGKDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 85 TVIASGGDGDGYAIGMGHTIHALRRNMNMTYIVMDNQIYGLTKGQTSPSSAVGFVTKTTPKGNIE-------KNVAplEL 157
Cdd:cd03376 82 TVVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTTPVGKVSfgkkqpkKDLP--LI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446112283 158 ALSSGATFVAQGFSSDIKGLTKLIEDAINHDGFSFVNVFSPCVT 201
Cdd:cd03376 160 MAAHNIPYVATASVAYPEDLYKKVKKALSIEGPAYIHILSPCPT 203
|
|
| PRK11865 |
PRK11865 |
pyruvate synthase subunit beta; |
16-201 |
7.09e-21 |
|
pyruvate synthase subunit beta;
Pssm-ID: 183346 [Multi-domain] Cd Length: 299 Bit Score: 90.16 E-value: 7.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 16 CPGCGDFSVQAAIQKAAAniglepEEVAIITGIGCSGRLSGYI--NSYGVHSIH-------GRALPLAQGVKMANKDLTV 86
Cdd:PRK11865 21 CAGCGAAIAMRLALKALG------KNTVIVVATGCLEVITTPYpeTAWNVPWIHvafenaaAVASGIERAVKALGKKVNV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 87 IASGGDGDGYAIGMGHTIHALRRNMNMTYIVMDNQIYGLTKGQTSPSSAVGFVTKTTPKGNI-------EKNVaPLeLAL 159
Cdd:PRK11865 95 VAIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKYsrgedrpKKNM-PL-IMA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446112283 160 SSGATFVAQGFSSDIKGLTKLIEDAINHDGFSFVNVFSPCVT 201
Cdd:PRK11865 173 AHGIPYVATASIGYPEDFMEKVKKAKEVEGPAYIQVLQPCPT 214
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
39-195 |
1.93e-13 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 66.90 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 39 PEEVAIITGIGCSGRLSGYI---------NSYGVHSIHGRALPLAQGVKMANKDLTVIASGGDGdGYAIGMGHTIHALRR 109
Cdd:cd00568 11 PEDAIVVNDAGNSAYWAYRYlplrrgrrfLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDG-GFMMTGQELATAVRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 110 NMNMTYIVMDNQIYGLTKGQTSPSsavgfvTKTTPKGNIEKNVAPLELALSSGATFVAqgfSSDIKGLTKLIEDAINHDG 189
Cdd:cd00568 90 GLPVIVVVFNNGGYGTIRMHQEAF------YGGRVSGTDLSNPDFAALAEAYGAKGVR---VEDPEDLEAALAEALAAGG 160
|
....*.
gi 446112283 190 FSFVNV 195
Cdd:cd00568 161 PALIEV 166
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
13-199 |
1.97e-12 |
|
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: 64.22 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 13 PNWCPGCGDFSVQAAIQKAAANiglepeEVAIITGIGCS--GRLSGYINSYGvhSIH-GRALPLAQGVKMANKDLTVIAS 89
Cdd:cd02008 4 PGLCPGCPHRPSFYALRKAFKK------DSIVSGDIGCYtlGALPPLNAIDT--CTCmGASIGVAIGMAKASEDKKVVAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 90 GGDGDGYAIGMGHTIHALRRNMNMTYIVMDNQIYGLTKGQTSPSSAVGfVTKTTPKGNIEknvaplELALSSGATFVAQG 169
Cdd:cd02008 76 IGDSTFFHSGILGLINAVYNKANITVVILDNRTTAMTGGQPHPGTGKT-LTEPTTVIDIE------ALVRAIGVKRVVVV 148
|
170 180 190
....*....|....*....|....*....|
gi 446112283 170 FSSDIKGLTKLIEDAINHDGFSFVNVFSPC 199
Cdd:cd02008 149 DPYDLKAIREELKEALAVPGVSVIIAKRPC 178
|
|
| PRK11864 |
PRK11864 |
3-methyl-2-oxobutanoate dehydrogenase subunit beta; |
16-201 |
4.09e-10 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
Pssm-ID: 237005 [Multi-domain] Cd Length: 300 Bit Score: 59.33 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 16 CPGCGdfsvqaaiqkaaANIGLE------PEEVAIITGIGCSGRLSGYINSYG-----VHSIHGRALPLAQGVKMA---- 80
Cdd:PRK11864 21 CPGCG------------APLGLRyllkalGEKTVLVIPASCSTVIQGDTPKSPltvpvLHTAFAATAAVASGIEEAlkar 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 81 -NKDLTVIASGGDGDGYAIGMGHTIHALRRNMNMTYIVMDNQIYGLTKGQTSPSSAVGFVTKTTPKGNIE--KNVAplEL 157
Cdd:PRK11864 89 gEKGVIVVGWAGDGGTADIGFQALSGAAERNHDILYIMYDNEAYMNTGIQRSSSTPYGAWTTTTPGGKREhkKPVP--DI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446112283 158 ALSSGATFVAQGFSSDIKGLTKLIEDAINHDGFSFVNVFSPCVT 201
Cdd:PRK11864 167 MAAHKVPYVATASIAYPEDFIRKLKKAKEIRGFKFIHLLAPCPP 210
|
|
| TPP_PFOR_PNO |
cd03377 |
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ... |
79-200 |
4.92e-09 |
|
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: 56.46 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 79 MANKDLTVIAS----GGDGDGYAIGMG---HTIhALRRNMNMtyIVMDNQIYGLTKGQTSPSSAVGFVTK------TTPK 145
Cdd:cd03377 143 LSLADYLVKKSvwiiGGDGWAYDIGYGgldHVL-ASGENVNI--LVLDTEVYSNTGGQASKATPLGAVAKfaaagkRTGK 219
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446112283 146 gnieKNVAplELALSSGATFVAQ-GFSSDIKGLTKLIEDAINHDGFSFVNVFSPCV 200
Cdd:cd03377 220 ----KDLG--MIAMSYGNVYVAQiALGANDNQTLKAFREAEAYDGPSLIIAYSPCI 269
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
41-195 |
5.18e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 54.84 E-value: 5.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 41 EVAIITGIG-------CSGRLSGyiNSYGVHSIhGRALPLAQGVKMANKDLTVIASGGDGDG-YAIGMGHTIhALRRNMN 112
Cdd:PRK06163 29 EEAVIGGIGntnfdlwAAGQRPQ--NFYMLGSM-GLAFPIALGVALAQPKRRVIALEGDGSLlMQLGALGTI-AALAPKN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 113 MTYIVMDNQIYGLTKGQTSPSSAVGFVtkttpkgnieknvapleLALSSGATFVAQGFSSDIKGLTKLIEDAINHDGFSF 192
Cdd:PRK06163 105 LTIIVMDNGVYQITGGQPTLTSQTVDV-----------------VAIARGAGLENSHWAADEAHFEALVDQALSGPGPSF 167
|
...
gi 446112283 193 VNV 195
Cdd:PRK06163 168 IAV 170
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
62-128 |
6.16e-06 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 47.29 E-value: 6.16e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 62 GVHSIH---GRALPLAQGVKMANKDLTVIASGGDGdGYAIGMGHTIHALRRNMNMTYIVMDNQIYGLTKG 128
Cdd:PRK07064 399 NVHALGggiGQGLAMAIGAALAGPGRKTVGLVGDG-GLMLNLGELATAVQENANMVIVLMNDGGYGVIRN 467
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
68-128 |
1.07e-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: 44.89 E-value: 1.07e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446112283 68 GRALPLAQGVKMANKDLTVIASGGDGDG-YAIgmgHTI-HALRRNMNMTYIVMDNQIYGLTKG 128
Cdd:cd02002 52 GWGLPAAVGAALANPDRKVVAIIGDGSFmYTI---QALwTAARYGLPVTVVILNNRGYGALRS 111
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
70-124 |
3.69e-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: 3.69e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 446112283 70 ALPLAQGVKMANKDLTVIASGGDGdgyaiGMGHTIHAL----RRNMNMTYIVMDNQIYG 124
Cdd:COG0028 417 GLPAAIGAKLARPDRPVVAITGDG-----GFQMNLQELatavRYGLPVKVVVLNNGGLG 470
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
26-136 |
9.25e-05 |
|
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: 42.28 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 26 AAIQKAAANIglepEEVAIITGIGCSGRLSGYIN----------SYGVHSIHGRALPLAQgvkmankDLTVIASGGDGdG 95
Cdd:cd03372 3 DAIKTLIADL----KDELVVSNIGFPSKELYAAGdrplnfymlgSMGLASSIGLGLALAQ-------PRKVIVIDGDG-S 70
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446112283 96 YAIGMGH--TIhALRRNMNMTYIVMDNQIYGLTKGQTSPSSAV 136
Cdd:cd03372 71 LLMNLGAlaTI-AAEKPKNLIIVVLDNGAYGSTGNQPTHAGKK 112
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
68-196 |
1.25e-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: 41.91 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 68 GRALPLAQGVKMANKDLTVIASggDGDGYAI-GMGH--TIHALRRNmNMTYIVMDNQIYGLTKGQTSPSSAVGFvtkttp 144
Cdd:cd03371 51 GHASQIALGIALARPDRKVVCI--DGDGAALmHMGGlaTIGGLAPA-NLIHIVLNNGAHDSVGGQPTVSFDVSL------ 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446112283 145 kgnieknvapLELALSSGATFVAQGfsSDIKGLTKLIEDAINHDGFSFVNVF 196
Cdd:cd03371 122 ----------PAIAKACGYRAVYEV--PSLEELVAALAKALAADGPAFIEVK 161
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|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
68-130 |
6.26e-04 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 41.14 E-value: 6.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446112283 68 GRALPLAQGVKMANKDLTVIASGGDGdGYAIGMGHTIH--ALRRNMNMTYIVMDNQIYGLTKGQT 130
Cdd:PRK08327 433 GWALGAALGAKLATPDRLVIATVGDG-SFIFGVPEAAHwvAERYGLPVLVVVFNNGGWLAVKEAV 496
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|
| TPP_Xsc_like |
cd02013 |
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ... |
39-127 |
6.27e-04 |
|
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity.
Pssm-ID: 238971 [Multi-domain] Cd Length: 196 Bit Score: 40.19 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 39 PEEVAIITGIG--CSgrlsgYINSYGVHS------------IHGRALPLAQGVKMANKDLTVIASGGDGdGYAIGMGHTI 104
Cdd:cd02013 18 PEDAIVSTDIGniCS-----VANSYLRFEkprsfiaplsfgNCGYALPAIIGAKAAAPDRPVVAIAGDG-AWGMSMMEIM 91
|
90 100
....*....|....*....|...
gi 446112283 105 HALRRNMNMTYIVMDNQIYGLTK 127
Cdd:cd02013 92 TAVRHKLPVTAVVFRNRQWGAEK 114
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
26-136 |
1.47e-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: 38.24 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446112283 26 AAIQKAAANIGLEPeevaIITGIGCSGRLSGYI-----NSYGVHSIhGRALPLAQGVKMANKDLTVIAsggDGDGyAIGM 100
Cdd:cd02001 3 AAIAEIIEASGDTP----IVSTTGYASRELYDVqdrdgHFYMLGSM-GLAGSIGLGLALGLSRKVIVV---DGDG-SLLM 73
|
90 100 110
....*....|....*....|....*....|....*....
gi 446112283 101 GHTIHALRRNM---NMTYIVMDNQIYGLTKGQTSPSSAV 136
Cdd:cd02001 74 NPGVLLTAGEFtplNLILVVLDNRAYGSTGGQPTPSSNV 112
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
68-127 |
1.48e-03 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 39.74 E-value: 1.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446112283 68 GRALPLAQGVKMANKDLTVIASGGDGdgyaiGMGHTIHAL----RRNMNMTYIVMDNQIYGLTK 127
Cdd:PRK06112 440 GWGVPMAIGAKVARPGAPVICLVGDG-----GFAHVWAELetarRMGVPVTIVVLNNGILGFQK 498
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