|
Name |
Accession |
Description |
Interval |
E-value |
| Oxoac_fdxbeta_Archa |
NF041171 |
2-oxoacid:ferredoxin oxidoreductase subunit beta; |
6-303 |
0e+00 |
|
2-oxoacid:ferredoxin oxidoreductase subunit beta;
Pssm-ID: 469082 [Multi-domain] Cd Length: 296 Bit Score: 608.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 6 VFNDWCPGCGNFGILRAEEMAIQELGVDFKKVVLVSGIGCSGKMPHFVNlpVGGVHTLHGRALAFATGIKLANPSLEVIV 85
Cdd:NF041171 1 EWVDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVN--VSGVHTLHGRAIPFATGIKLANPELEVIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 86 NVGDGDGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKGQAAPTLERGIKTKSLPKPNINDAVNPLAVALSAGYTFIAR 165
Cdd:NF041171 79 NGGDGDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 166 AYAYDVIHLKEVIKRAIKHKGSAIIDVFQPCPTYNDINTKEWYDKRVYKLDKDPTWDPVVRKEEEKQSKFEKALLKSMEF 245
Cdd:NF041171 159 GYAYDVKHLKELIKAAIKHKGLAFIDVLQPCPTYNDINTKEWYDKRVYKLDDEPGWDPVVRSPEEADEKMAKAIEKALEW 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 499598361 246 GEKIPIGVFYENELVPTFEERLESNIPNYREFHPAAQPIEIDGIATTRIDELIKAKRI 303
Cdd:NF041171 239 GDRIPIGIFYQNELVPTFEERIAERLPNYLDNPPAKQPIEKDGKPVTIIEDIFKEKIV 296
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
9-285 |
3.85e-161 |
|
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: 449.98 E-value: 3.85e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 9 DWCPGCGNFGILRAEEMAIQELGVDFKKVVLVSGIGCSGKMPHFVNlpVGGVHTLHGRALAFATGIKLANPSLEVIVNVG 88
Cdd:TIGR02177 2 DWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVN--VNGFHGLHGRALPVATGIKLANPHLKVIVVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 89 DGDGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKGQAAPTLERGIKTKSLPKPNINDAVNPLAVALSAGYTFIARAYA 168
Cdd:TIGR02177 80 DGDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 169 YDVIHLKEVIKRAIKHKGSAIIDVFQPCPTYNDINTKEWYDKRVYKLDkDPTWDPVVRKEEEKQSKFEKALLKSMEFGEK 248
Cdd:TIGR02177 160 GDVAHLKEIIKEAINHKGYALVDILQPCVTYNKINTYEWYRERVYKLD-EEGYDPIVREPEEFEEKAAAAIKKAMEWGDR 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 499598361 249 IPIGVFYENELVPTFEERLESNIPNYREFHPAAQPIE 285
Cdd:TIGR02177 239 IPIGIFYKNENKPTFEERLEKILPRYMSAPPAEQEIK 275
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
1-292 |
3.72e-160 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 448.17 E-value: 3.72e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 1 MERKPVFNDWCPGCGNFGILRAEEMAIQELGVDFKKVVLVSGIGCSGKMPHFVNlpVGGVHTLHGRALAFATGIKLANPS 80
Cdd:PRK05778 11 LRYDGLPTTWCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFL--SHGLHTLHGRAIAFATGAKLANPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 81 LEVIVNVGDGDGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKGQAAPTLERGIKTKSLPKPNINDAVNPLAVALSAGY 160
Cdd:PRK05778 89 LEVIVVGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAAGA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 161 TFIARAYAYDVIHLKEVIKRAIKHKGSAIIDVFQPCPTYNDINTK--------EWYDKRVYKLDKDPTWDPvvrkeeekq 232
Cdd:PRK05778 169 TFVARSFAGDVKQLVELIKKAISHKGFAFIDVLSPCVTFNGRNTStkspaymrEYYKKRVYKLKLEEDYDP--------- 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499598361 233 SKFEKALLKSME--FGEKIPIGVFYENElVPTFEERLESNIPNYREFHPAAQPIEIDGIATT 292
Cdd:PRK05778 240 TDRDKAAEKMLEeeLGGKIPIGVFYKNE-RPTFEERLEKLIEPLLELPPAALRPGKEALDTI 300
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
10-199 |
4.62e-122 |
|
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: 347.21 E-value: 4.62e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 10 WCPGCGNFGILRAEEMAIQELGVDFKKVVLVSGIGCSGKMPHFVNlpVGGVHTLHGRALAFATGIKLANPSLEVIVNVGD 89
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFN--TYGFHTLHGRALAVATGVKLANPDLTVIVVSGD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 90 GDGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKGQAAPTLERGIKTKSLPKPNINDAVNPLAVALSAGYTFIARAYAY 169
Cdd:cd03375 79 GDLAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSG 158
|
170 180 190
....*....|....*....|....*....|
gi 499598361 170 DVIHLKEVIKRAIKHKGSAIIDVFQPCPTY 199
Cdd:cd03375 159 DIKQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
4-268 |
2.47e-118 |
|
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: 340.58 E-value: 2.47e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 4 KPVFNDWCPGCGNFGILRAEEMAIQELGVDfKKVVLVSGIGCSGKMPHFVNLPvgGVHTLHGRALAFATGIKLANPSLEV 83
Cdd:COG1013 9 RTPGHRWCPGCGHGIILRLLLKALDELLDG-DKTVVVSGIGCSSVAPGYFNVP--GFHTLHGRAAAVATGIKLANPDLTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 84 IVNVGDGDGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKGQAAPTLERGIKTKSLPKPNINDAVNPLAVALSAGYTFI 163
Cdd:COG1013 86 IVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHGATYV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 164 ARAYAYDVIHLKEVIKRAIKHKGSAIIDVFQPCPTYNDIN---TKEWYDKRVYKLDKdptWDPvvrkeeekqskfEKALL 240
Cdd:COG1013 166 ARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRDpskTIEWAKEGMWPLYE---YDP------------GEKLR 230
|
250 260
....*....|....*....|....*...
gi 499598361 241 KSMEFGEKIPIGVFYENELVptFEERLE 268
Cdd:COG1013 231 LTYEPKDKIPVGEFLKNQGR--FEELIE 256
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
42-192 |
3.30e-37 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 129.63 E-value: 3.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 42 GIGCSG----------KMPHFVNlpvGGVHTLHGRALAFATGIKLANPSLEVIVNVGDGDGLGIGMgHFVHLGRRNIDIT 111
Cdd:pfam02775 1 DIGCHQmwaaqyyrfrPPRRYLT---SGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQ-ELATAVRYNLPIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 112 LIVHDNGVYGLTKGQAAPtleRGIKTKSLPKPNINDAVNPLAVALSAGYTfIARAYAYDviHLKEVIKRAIKHKGSAIID 191
Cdd:pfam02775 77 VVVLNNGGYGMTRGQQTP---FGGGRYSGPSGKILPPVDFAKLAEAYGAK-GARVESPE--ELEEALKEALEHDGPALID 150
|
.
gi 499598361 192 V 192
Cdd:pfam02775 151 V 151
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Oxoac_fdxbeta_Archa |
NF041171 |
2-oxoacid:ferredoxin oxidoreductase subunit beta; |
6-303 |
0e+00 |
|
2-oxoacid:ferredoxin oxidoreductase subunit beta;
Pssm-ID: 469082 [Multi-domain] Cd Length: 296 Bit Score: 608.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 6 VFNDWCPGCGNFGILRAEEMAIQELGVDFKKVVLVSGIGCSGKMPHFVNlpVGGVHTLHGRALAFATGIKLANPSLEVIV 85
Cdd:NF041171 1 EWVDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVN--VSGVHTLHGRAIPFATGIKLANPELEVIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 86 NVGDGDGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKGQAAPTLERGIKTKSLPKPNINDAVNPLAVALSAGYTFIAR 165
Cdd:NF041171 79 NGGDGDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 166 AYAYDVIHLKEVIKRAIKHKGSAIIDVFQPCPTYNDINTKEWYDKRVYKLDKDPTWDPVVRKEEEKQSKFEKALLKSMEF 245
Cdd:NF041171 159 GYAYDVKHLKELIKAAIKHKGLAFIDVLQPCPTYNDINTKEWYDKRVYKLDDEPGWDPVVRSPEEADEKMAKAIEKALEW 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 499598361 246 GEKIPIGVFYENELVPTFEERLESNIPNYREFHPAAQPIEIDGIATTRIDELIKAKRI 303
Cdd:NF041171 239 GDRIPIGIFYQNELVPTFEERIAERLPNYLDNPPAKQPIEKDGKPVTIIEDIFKEKIV 296
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
9-285 |
3.85e-161 |
|
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: 449.98 E-value: 3.85e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 9 DWCPGCGNFGILRAEEMAIQELGVDFKKVVLVSGIGCSGKMPHFVNlpVGGVHTLHGRALAFATGIKLANPSLEVIVNVG 88
Cdd:TIGR02177 2 DWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVN--VNGFHGLHGRALPVATGIKLANPHLKVIVVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 89 DGDGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKGQAAPTLERGIKTKSLPKPNINDAVNPLAVALSAGYTFIARAYA 168
Cdd:TIGR02177 80 DGDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 169 YDVIHLKEVIKRAIKHKGSAIIDVFQPCPTYNDINTKEWYDKRVYKLDkDPTWDPVVRKEEEKQSKFEKALLKSMEFGEK 248
Cdd:TIGR02177 160 GDVAHLKEIIKEAINHKGYALVDILQPCVTYNKINTYEWYRERVYKLD-EEGYDPIVREPEEFEEKAAAAIKKAMEWGDR 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 499598361 249 IPIGVFYENELVPTFEERLESNIPNYREFHPAAQPIE 285
Cdd:TIGR02177 239 IPIGIFYKNENKPTFEERLEKILPRYMSAPPAEQEIK 275
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
1-292 |
3.72e-160 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 448.17 E-value: 3.72e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 1 MERKPVFNDWCPGCGNFGILRAEEMAIQELGVDFKKVVLVSGIGCSGKMPHFVNlpVGGVHTLHGRALAFATGIKLANPS 80
Cdd:PRK05778 11 LRYDGLPTTWCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFL--SHGLHTLHGRAIAFATGAKLANPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 81 LEVIVNVGDGDGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKGQAAPTLERGIKTKSLPKPNINDAVNPLAVALSAGY 160
Cdd:PRK05778 89 LEVIVVGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAAGA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 161 TFIARAYAYDVIHLKEVIKRAIKHKGSAIIDVFQPCPTYNDINTK--------EWYDKRVYKLDKDPTWDPvvrkeeekq 232
Cdd:PRK05778 169 TFVARSFAGDVKQLVELIKKAISHKGFAFIDVLSPCVTFNGRNTStkspaymrEYYKKRVYKLKLEEDYDP--------- 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499598361 233 SKFEKALLKSME--FGEKIPIGVFYENElVPTFEERLESNIPNYREFHPAAQPIEIDGIATT 292
Cdd:PRK05778 240 TDRDKAAEKMLEeeLGGKIPIGVFYKNE-RPTFEERLEKLIEPLLELPPAALRPGKEALDTI 300
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
1-268 |
1.04e-133 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 380.34 E-value: 1.04e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 1 MERKPvfnDWCPGCGNFGILRAEEMAIQELGVDFKKVVLVSGIGCSGKMPHFVNlpVGGVHTLHGRALAFATGIKLANPS 80
Cdd:PRK11867 13 NDQEP---RWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYIN--TYGFHTIHGRALAIATGLKLANPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 81 LEVIVNVGDGDGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKGQAAPTLERGIKTKSLPKPNINDAVNPLAVALSAGY 160
Cdd:PRK11867 88 LTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVELALGAGA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 161 TFIARAYAYDVIHLKEVIKRAIKHKGSAIIDVFQPCPTYNDINTKEWYDKRVYKLDKDPTWDPvvrkeEEKQskfekALL 240
Cdd:PRK11867 168 TFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFNNVNTFDWFKERLVKVHDAEGYDP-----TNAL-----AAM 237
|
250 260
....*....|....*....|....*...
gi 499598361 241 KSMEFGEKIPIGVFYENELvPTFEERLE 268
Cdd:PRK11867 238 KTLEEGDPIPTGIFYQVER-PTYEEAVR 264
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
3-289 |
1.88e-122 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 351.75 E-value: 1.88e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 3 RKPVfndWCPGCGNFGILRAEEMAIQELGVDFKKVVLVSGIGCSGKMPHFVNlpVGGVHTLHGRALAFATGIKLANPSLE 82
Cdd:PRK11866 5 RPPI---WCPGCGNYGILEALRKALAELGIPPENVVVVSGIGCSSNLPEFLN--TYGIHGIHGRVLPIATGVKWANPKLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 83 VIVNVGDGDGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKGQAAPTLERGIKTKSLPKPNINDAVNPLAVALSAGYTF 162
Cdd:PRK11866 80 VIGYGGDGDGYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 163 IARAYAYDVIHLKEVIKRAIKHKGSAIIDVFQPCPTYNDINTKEWYDKRVYKLDK---DPTwdpvvrkeeekqsKFEKAL 239
Cdd:PRK11866 160 VARGFSGDVKHLKEIIKEAIKHKGFSFIDVLSPCVTFNKLNTYDWFRPRVYKLEEtghDPT-------------NFEQAY 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 499598361 240 LKSMEFGEKIPIGVFYENELvPTFEERLESNIPNYREFHPAAQPIEIDGI 289
Cdd:PRK11866 227 KKALEWGDRIPIGVFYKEEK-PTYEEELDEILKNPPLADQPLQPKPEKDL 275
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
10-199 |
4.62e-122 |
|
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: 347.21 E-value: 4.62e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 10 WCPGCGNFGILRAEEMAIQELGVDFKKVVLVSGIGCSGKMPHFVNlpVGGVHTLHGRALAFATGIKLANPSLEVIVNVGD 89
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFN--TYGFHTLHGRALAVATGVKLANPDLTVIVVSGD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 90 GDGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKGQAAPTLERGIKTKSLPKPNINDAVNPLAVALSAGYTFIARAYAY 169
Cdd:cd03375 79 GDLAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSG 158
|
170 180 190
....*....|....*....|....*....|
gi 499598361 170 DVIHLKEVIKRAIKHKGSAIIDVFQPCPTY 199
Cdd:cd03375 159 DIKQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
4-268 |
2.47e-118 |
|
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: 340.58 E-value: 2.47e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 4 KPVFNDWCPGCGNFGILRAEEMAIQELGVDfKKVVLVSGIGCSGKMPHFVNLPvgGVHTLHGRALAFATGIKLANPSLEV 83
Cdd:COG1013 9 RTPGHRWCPGCGHGIILRLLLKALDELLDG-DKTVVVSGIGCSSVAPGYFNVP--GFHTLHGRAAAVATGIKLANPDLTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 84 IVNVGDGDGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKGQAAPTLERGIKTKSLPKPNINDAVNPLAVALSAGYTFI 163
Cdd:COG1013 86 IVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHGATYV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 164 ARAYAYDVIHLKEVIKRAIKHKGSAIIDVFQPCPTYNDIN---TKEWYDKRVYKLDKdptWDPvvrkeeekqskfEKALL 240
Cdd:COG1013 166 ARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRDpskTIEWAKEGMWPLYE---YDP------------GEKLR 230
|
250 260
....*....|....*....|....*...
gi 499598361 241 KSMEFGEKIPIGVFYENELVptFEERLE 268
Cdd:COG1013 231 LTYEPKDKIPVGEFLKNQGR--FEELIE 256
|
|
| PRK11869 |
PRK11869 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
10-302 |
1.43e-94 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183349 [Multi-domain] Cd Length: 280 Bit Score: 280.90 E-value: 1.43e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 10 WCPGCGNFGILRAEEMAIQELGVDFKKVVLVSGIGCSGKMPHFVNlpVGGVHTLHGRALAFATGIKLANPSLEVIVNVGD 89
Cdd:PRK11869 10 WCPGCGNFGIRNALMKALSELNLKPRQVVIVSGIGQAAKMPHYIN--VNGFHTLHGRAIPAATAVKATNPELTVIAEGGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 90 GDGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKGQAAPTLERGIKTKSLPKPNINDAVNPLAVALSAGYTFIARAYAY 169
Cdd:PRK11869 88 GDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASFVARTFSG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 170 DVIHLKEVIKRAIKHKGSAIIDVFQPCPTYNDINTKEWYDKRVYKL-DKDPTwdpvvrkeeEKQSKFEKALLksmefGEK 248
Cdd:PRK11869 168 DIEETKEILKEAIKHKGLAIVDIFQPCVSFNKVNTYQWYRENTYYLkDHDPT---------DRELAFKRALE-----TEK 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 499598361 249 IPIGVFYENElVPTFEErlesNIPNYrefHPAAQPIEIDGIATTRIDELIKAKR 302
Cdd:PRK11869 234 LPLGIFYINE-KPTFEE----LVPAY---KGDKTPLWKREPNFEKLKELIESKR 279
|
|
| oorB |
PRK09628 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; |
10-241 |
3.88e-61 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
Pssm-ID: 182003 [Multi-domain] Cd Length: 277 Bit Score: 195.72 E-value: 3.88e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 10 WCPGCGNFGILRAEEMAIQELGVDFKKVVLVSGIGCSGKMPHFVNlpVGGVHTLHGRALAFATGIKLANPSLEVIVNVGD 89
Cdd:PRK09628 18 WCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSGIGCSGRFSSYVN--CNTVHTTHGRAVAYATGIKLANPDKHVIVVSGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 90 GDGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKGQAAPTLERGIKTKSLPKPNINDAVNPLAVALSAGYTFIARAYAY 169
Cdd:PRK09628 96 GDGLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKLATAAGASFVARESVI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 170 DVIHLKEVIKRAIKHKGSAIIDVFQPCptynDIN------------TKEWYDKRVYKLDKDPTWDPvvrkeEEKQSKFEK 237
Cdd:PRK09628 176 DPQKLEKLLVKGFSHKGFSFFDVFSNC----HINlgrknkmgeavqMLKWIESRTVSKRKFDALSP-----EERVGKFPT 246
|
....
gi 499598361 238 ALLK 241
Cdd:PRK09628 247 GILK 250
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
42-192 |
3.30e-37 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 129.63 E-value: 3.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 42 GIGCSG----------KMPHFVNlpvGGVHTLHGRALAFATGIKLANPSLEVIVNVGDGDGLGIGMgHFVHLGRRNIDIT 111
Cdd:pfam02775 1 DIGCHQmwaaqyyrfrPPRRYLT---SGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQ-ELATAVRYNLPIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 112 LIVHDNGVYGLTKGQAAPtleRGIKTKSLPKPNINDAVNPLAVALSAGYTfIARAYAYDviHLKEVIKRAIKHKGSAIID 191
Cdd:pfam02775 77 VVVLNNGGYGMTRGQQTP---FGGGRYSGPSGKILPPVDFAKLAEAYGAK-GARVESPE--ELEEALKEALEHDGPALID 150
|
.
gi 499598361 192 V 192
Cdd:pfam02775 151 V 151
|
|
| PFO_beta_C |
pfam12367 |
Pyruvate ferredoxin oxidoreductase beta subunit C terminal; This domain family is found in ... |
196-268 |
4.07e-28 |
|
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: 102.96 E-value: 4.07e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499598361 196 CPTYNDINTKEWYDKRVYKLDKDptWDPVVRkeeekqskfEKALLKSMEFGEKIPIGVFYENElVPTFEERLE 268
Cdd:pfam12367 1 CVTFNKVNTYDWYKERVYKLDED--HDPTDR---------EAAMEKALEWGDRIPIGIFYKEE-RPTFEERLP 61
|
|
| TPP_PFOR |
cd02018 |
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ... |
11-206 |
2.27e-17 |
|
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: 79.45 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 11 CPGCGNFGILRAEEMAIQELGvdfkKVVLVSGIGCSG-KMPHFVNLPVGG--VHTLHGRALAFATGIKLA----NPSLE- 82
Cdd:cd02018 8 CAGCGEVTAVRVVLAALPAPE----DTVIANSTGCSSvYASTAPFNSWAVpwVNSLFEDANAVASGLKRGlkarFPKDRe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 83 ------VIVNVGDGDGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKGQAAPTLERGIKTKSLPKPNINDAVNPLAVAL 156
Cdd:cd02018 84 ldkkkdVVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKKDLVLIAA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 499598361 157 SAGYTFIARAYAYDVIHLKEVIKRAI-KHKGSAIIDVFQPCPTYNDINTKE 206
Cdd:cd02018 164 THGCVYVARLSPALKKHFLKVVKEAIsRTDGPTFIHAYTPCITEWGIGSGK 214
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
37-192 |
2.34e-15 |
|
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: 72.29 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 37 VVLVSGIGCSGKMPHFVNLPVGGVHTLH-------GRALAFATGIKLANPSLEVIVNVGDGdGLGIGMGHFVHLGRRNID 109
Cdd:cd00568 14 AIVVNDAGNSAYWAYRYLPLRRGRRFLTstgfgamGYGLPAAIGAALAAPDRPVVCIAGDG-GFMMTGQELATAVRYGLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 110 ITLIVHDNGVYGLTKGQAAPTLERGIKTKSLPKPNINDavnplavalsagytfIARAYAYDVIH------LKEVIKRAIK 183
Cdd:cd00568 93 VIVVVFNNGGYGTIRMHQEAFYGGRVSGTDLSNPDFAA---------------LAEAYGAKGVRvedpedLEAALAEALA 157
|
....*....
gi 499598361 184 HKGSAIIDV 192
Cdd:cd00568 158 AGGPALIEV 166
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
3-196 |
1.25e-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: 64.99 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 3 RKPVFndwCPGCGNFGILRAEEMAIQelgvdfKKVVLVSGIGCS--GKMPHFvNLPVGGVHTlhGRALAFATGIKLANPS 80
Cdd:cd02008 2 RPPGL---CPGCPHRPSFYALRKAFK------KDSIVSGDIGCYtlGALPPL-NAIDTCTCM--GASIGVAIGMAKASED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 81 LEVIVNVGDGDglgigmghFVH---LGRRNI-----DITLIVHDNGVYGLTKGQAAPTLERGIKTKSlPKPNIndavnpL 152
Cdd:cd02008 70 KKVVAVIGDST--------FFHsgiLGLINAvynkaNITVVILDNRTTAMTGGQPHPGTGKTLTEPT-TVIDI------E 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499598361 153 AVALSAGYTFIARAYAYDVIHLKEVIKRAIKHKGSAIIDVFQPC 196
Cdd:cd02008 135 ALVRAIGVKRVVVVDPYDLKAIREELKEALAVPGVSVIIAKRPC 178
|
|
| TPP_PFOR_porB_like |
cd03376 |
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ... |
11-198 |
1.38e-12 |
|
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of proteins similar to the beta subunit (porB) of the Helicobacter pylori four-subunit pyruvate ferredoxin oxidoreductase (PFOR), which are also found in archaea and some hyperthermophilic bacteria. PFOR catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. The 36-kDa porB subunit contains the binding sites for the cofactors, TPP and a divalent metal cation, which are required for activity.
Pssm-ID: 239471 [Multi-domain] Cd Length: 235 Bit Score: 66.11 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 11 CPGCGNFGILRaeeMAIQELGvdfKKVVLVSGIGC----SGKMPHF-VNLPVggVHTLHGRALAFATGIKLANPSL---- 81
Cdd:cd03376 8 CAGCGAALALR---HVLKALG---PDTVVVNPTGCleviTTPYPYTaWRVPW--IHVAFENAAAVASGIEAALKALgrgk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 82 --EVIVNVGDGDGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKGQAAPTLERGIKTKSLPK--------------PNI 145
Cdd:cd03376 80 diTVVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTTPVgkvsfgkkqpkkdlPLI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499598361 146 NDAVNPLAVA-LSAGYTFiarayayDVIhlkEVIKRAIKHKGSAIIDVFQPCPT 198
Cdd:cd03376 160 MAAHNIPYVAtASVAYPE-------DLY---KKVKKALSIEGPAYIHILSPCPT 203
|
|
| PRK11865 |
PRK11865 |
pyruvate synthase subunit beta; |
11-198 |
7.50e-11 |
|
pyruvate synthase subunit beta;
Pssm-ID: 183346 [Multi-domain] Cd Length: 299 Bit Score: 61.65 E-value: 7.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 11 CPGCGNFGILRaeeMAIQELGvdfKKVVLVSGIGCSGKM----PHFV-NLPVggVHTLHGRALAFATGIKLANPSLEVIV 85
Cdd:PRK11865 21 CAGCGAAIAMR---LALKALG---KNTVIVVATGCLEVIttpyPETAwNVPW--IHVAFENAAAVASGIERAVKALGKKV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 86 NV----GDGDGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKGQAAPTLERGIKTKSLP---------KPNINDAVnpl 152
Cdd:PRK11865 93 NVvaigGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPagkysrgedRPKKNMPL--- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499598361 153 aVALSAGYTFIARA---YAYDVIhlkEVIKRAIKHKGSAIIDVFQPCPT 198
Cdd:PRK11865 170 -IMAAHGIPYVATAsigYPEDFM---EKVKKAKEVEGPAYIQVLQPCPT 214
|
|
| PRK11864 |
PRK11864 |
3-methyl-2-oxobutanoate dehydrogenase subunit beta; |
11-198 |
4.76e-10 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
Pssm-ID: 237005 [Multi-domain] Cd Length: 300 Bit Score: 59.33 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 11 CPGCGNFGILRAEEMAiqeLGvdfKKVVLVSGIGCS----GKMPHF-VNLPVggVHTLHGRALAFATGIKLANPSL---- 81
Cdd:PRK11864 21 CPGCGAPLGLRYLLKA---LG---EKTVLVIPASCStviqGDTPKSpLTVPV--LHTAFAATAAVASGIEEALKARgekg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 82 -EVIVNVGDGDGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKGQAAPTLERGIKTKSLP--KPNINDAVNPLAVALSA 158
Cdd:PRK11864 93 vIVVGWAGDGGTADIGFQALSGAAERNHDILYIMYDNEAYMNTGIQRSSSTPYGAWTTTTPggKREHKKPVPDIMAAHKV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 499598361 159 GYTFIAR-AYAYDVIhlkEVIKRAIKHKGSAIIDVFQPCPT 198
Cdd:PRK11864 173 PYVATASiAYPEDFI---RKLKKAKEIRGFKFIHLLAPCPP 210
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
65-192 |
4.92e-09 |
|
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: 54.91 E-value: 4.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 65 GRALAFATGIKLANPSLEVIVNVGDGDGLgIGMGHFVHLGRRNIDITLIVHDNGVYGLTKGQAAPTLERGIKTKslpKPN 144
Cdd:cd02002 52 GWGLPAAVGAALANPDRKVVAIIGDGSFM-YTIQALWTAARYGLPVTVVILNNRGYGALRSFLKRVGPEGPGEN---APD 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 499598361 145 INDAVNPlavalSAGYTFIARAYAYDVIH------LKEVIKRAIKHKGSAIIDV 192
Cdd:cd02002 128 GLDLLDP-----GIDFAAIAKAFGVEAERvetpeeLDEALREALAEGGPALIEV 176
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
55-193 |
1.48e-07 |
|
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: 50.77 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 55 LPVGGVhtlhGRALAFATGIKLANPSLEVIVNVGDGDGL----------GIGMGHFVHlgrrniditlIVHDNGVYGLTK 124
Cdd:cd03371 45 LTVGSM----GHASQIALGIALARPDRKVVCIDGDGAALmhmgglatigGLAPANLIH----------IVLNNGAHDSVG 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499598361 125 GQaaPTLERgikTKSLPkpnindavnplAVALSAGYTFIARayAYDVIHLKEVIKRAIKHKGSAIIDVF 193
Cdd:cd03371 111 GQ--PTVSF---DVSLP-----------AIAKACGYRAVYE--VPSLEELVAALAKALAADGPAFIEVK 161
|
|
| PRK06163 |
PRK06163 |
hypothetical protein; Provisional |
65-192 |
2.37e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235721 [Multi-domain] Cd Length: 202 Bit Score: 50.21 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 65 GRALAFATGIKLANPSLEVIVNVGDGDGL-GIG-MGHFVHLGRRNIdiTLIVHDNGVYGLTKGQAAPTlergiktkslpk 142
Cdd:PRK06163 60 GLAFPIALGVALAQPKRRVIALEGDGSLLmQLGaLGTIAALAPKNL--TIIVMDNGVYQITGGQPTLT------------ 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 499598361 143 pniNDAVNplAVALSAGYTFIARAYAYDVIHLKEVIKRAIKHKGSAIIDV 192
Cdd:PRK06163 126 ---SQTVD--VVAIARGAGLENSHWAADEAHFEALVDQALSGPGPSFIAV 170
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
67-192 |
1.58e-06 |
|
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: 49.39 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 67 ALAFATGIKLANPSLEVIVNVGDGdglGIGMghfvHLG------RRNIDITLIVHDNGVYGLTK-GQAAPTLERGIKTkS 139
Cdd:COG0028 417 GLPAAIGAKLARPDRPVVAITGDG---GFQM----NLQelatavRYGLPVKVVVLNNGGLGMVRqWQELFYGGRYSGT-D 488
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 499598361 140 LPKPNIndavnplaVALSAGYtfiaRAYAYDVIH---LKEVIKRAIKHKGSAIIDV 192
Cdd:COG0028 489 LPNPDF--------AKLAEAF----GAKGERVETpeeLEAALEEALASDGPALIDV 532
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
58-192 |
8.98e-06 |
|
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: 45.57 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 58 GGVHTLhGRALAFATGIKLANPSLEVIVNVGDGdGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKG-QAAPTLERGIK 136
Cdd:cd02015 47 GGLGTM-GFGLPAAIGAKVARPDKTVICIDGDG-SFQMNIQELATAAQYNLPVKIVILNNGSLGMVRQwQELFYEGRYSH 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499598361 137 TKSLPKPNIndavnplaVAlsagytfIARAY---AYDVI---HLKEVIKRAIKHKGSAIIDV 192
Cdd:cd02015 125 TTLDSNPDF--------VK-------LAEAYgikGLRVEkpeELEAALKEALASDGPVLLDV 171
|
|
| PRK07064 |
PRK07064 |
thiamine pyrophosphate-binding protein; |
56-125 |
1.59e-05 |
|
thiamine pyrophosphate-binding protein;
Pssm-ID: 180820 [Multi-domain] Cd Length: 544 Bit Score: 46.14 E-value: 1.59e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499598361 56 PVGGVHTLH---GRALAFATGIKLANPSLEVIVNVGDGdGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKG 125
Cdd:PRK07064 396 PRANVHALGggiGQGLAMAIGAALAGPGRKTVGLVGDG-GLMLNLGELATAVQENANMVIVLMNDGGYGVIRN 467
|
|
| PRK06546 |
PRK06546 |
pyruvate dehydrogenase; Provisional |
63-192 |
3.07e-05 |
|
pyruvate dehydrogenase; Provisional
Pssm-ID: 180614 [Multi-domain] Cd Length: 578 Bit Score: 45.36 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 63 LHG---RALAFATGIKLANPSLEVIVNVGDGdGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTKgqaaptLE---RGIK 136
Cdd:PRK06546 406 RHGsmaNALPHAIGAQLADPGRQVISMSGDG-GLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVK------LEmlvDGLP 478
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 499598361 137 TKSLPKPNINDAvnplAVALSAGytfiarAYAYDVIHLKEV---IKRAIKHKGSAIIDV 192
Cdd:PRK06546 479 DFGTDHPPVDYA----AIAAALG------IHAVRVEDPKDVrgaLREAFAHPGPALVDV 527
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
51-192 |
6.23e-05 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 44.37 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 51 HFVNLPVGGVHTLHGRALA-------FATGIKLANPSLEVIVNVGDGdglgiGMGH----FVHLGRRNIDITLIVHDNGV 119
Cdd:PRK06112 419 NFLTARRAGMRFLTPRGLAglgwgvpMAIGAKVARPGAPVICLVGDG-----GFAHvwaeLETARRMGVPVTIVVLNNGI 493
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499598361 120 YGLTKGqaAPTLERGIKTkslpkpninDAVNPLAVALSAgytfIARAYAYDVIH------LKEVIKRAIKHKGSAIIDV 192
Cdd:PRK06112 494 LGFQKH--AETVKFGTHT---------DACHFAAVDHAA----IARACGCDGVRvedpaeLAQALAAAMAAPGPTLIEV 557
|
|
| TPP_IolD |
cd02003 |
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ... |
65-192 |
1.83e-04 |
|
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: 41.91 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 65 GRALAFATGIKLANPSLEVIVNVGDGDGLgigMGH--FVHLGRRNIDITLIVHDNGVYG----LTKGQAAPTLERGIKTK 138
Cdd:cd02003 51 GYEIAAGLGAKLAKPDREVYVLVGDGSYL---MLHseIVTAVQEGLKIIIVLFDNHGFGcinnLQESTGSGSFGTEFRDR 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 499598361 139 SLPKPNINDAVNPL---AVALSAGytfiARAY-AYDVIHLKEVIKRAIKHKGSAIIDV 192
Cdd:cd02003 128 DQESGQLDGALLPVdfaANARSLG----ARVEkVKTIEELKAALAKAKASDRTTVIVI 181
|
|
| PRK09124 |
PRK09124 |
ubiquinone-dependent pyruvate dehydrogenase; |
64-192 |
1.89e-04 |
|
ubiquinone-dependent pyruvate dehydrogenase;
Pssm-ID: 181661 [Multi-domain] Cd Length: 574 Bit Score: 42.67 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 64 HG---RALAFATGIKLANPSLEVIVNVGDGdGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLT--KGQAAPTLERGIktk 138
Cdd:PRK09124 407 HGsmaNAMPQALGAQAAHPGRQVVALSGDG-GFSMLMGDFLSLVQLKLPVKIVVFNNSVLGFVamEMKAGGYLTDGT--- 482
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 499598361 139 SLPKPNINdavnplAVALSAGYTFIARAYAYDvihLKEVIKRAIKHKGSAIIDV 192
Cdd:PRK09124 483 DLHNPDFA------AIAEACGITGIRVEKASE---LDGALQRAFAHDGPALVDV 527
|
|
| PRK08327 |
PRK08327 |
thiamine pyrophosphate-requiring protein; |
65-192 |
8.35e-04 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 236243 [Multi-domain] Cd Length: 569 Bit Score: 40.75 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 65 GRALAFATGIKLANPSLEVIVNVGDGDGLgIGMGHFVH--LGRRNIDITLIVHDNGVYGLTKGqaaPTLErgiktkslpk 142
Cdd:PRK08327 433 GWALGAALGAKLATPDRLVIATVGDGSFI-FGVPEAAHwvAERYGLPVLVVVFNNGGWLAVKE---AVLE---------- 498
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499598361 143 pnindaVNPLAVALSAG------------YTFIARA---YAYDVIH---LKEVIKRAIKH----KGSAIIDV 192
Cdd:PRK08327 499 ------VYPEGYAARKGtfpgtdfdprpdFAKIAEAfggYGERVEDpeeLKGALRRALAAvrkgRRSAVLDV 564
|
|
| TPP_ComE |
cd03372 |
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ... |
26-130 |
1.16e-03 |
|
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: 39.19 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 26 AIQELGVDFKKVVLVSGIGCSGKMPHFVnlpvgGVHTLH-------GRALAFATGIKLANPsLEVIVNVGDGDGLGiGMG 98
Cdd:cd03372 4 AIKTLIADLKDELVVSNIGFPSKELYAA-----GDRPLNfymlgsmGLASSIGLGLALAQP-RKVIVIDGDGSLLM-NLG 76
|
90 100 110
....*....|....*....|....*....|...
gi 499598361 99 HFVHLGRRNI-DITLIVHDNGVYGLTKGQAAPT 130
Cdd:cd03372 77 ALATIAAEKPkNLIIVVLDNGAYGSTGNQPTHA 109
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
65-124 |
2.25e-03 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 39.60 E-value: 2.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598361 65 GRALAFATGIKLANPSLEVIVNVGDGdGLGIGMGHFVHLGRRNIDITLIVHDNGVYGLTK 124
Cdd:PRK07525 438 GYAFPAIIGAKIACPDRPVVGFAGDG-AWGISMNEVMTAVRHNWPVTAVVFRNYQWGAEK 496
|
|
| |
