|
Name |
Accession |
Description |
Interval |
E-value |
| oorB |
PRK09628 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; |
1-275 |
0e+00 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
Pssm-ID: 182003 [Multi-domain] Cd Length: 277 Bit Score: 544.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 1 MAFNYDKYLRLEKMPTLWCWGCGDGVILKAFIRAVDKLGISQDDICVVSGIGCSGRFSSYVDFNTVHTTHGRTVAFATGI 80
Cdd:PRK09628 1 MAFNYDEYLRVDKMPTLWCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 81 KLVHPDKYVVCVAGDGDALAIGGNHTIHGARRNIDITLIIINNFIYGLTNSQTSPTTPQGMWTVSQKAGNIDPTFNACDL 160
Cdd:PRK09628 81 KLANPDKHVIVVSGDGDGLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 161 GIASGASFVARETMLDPKKLEKIFVKALEHRGFSFLDIMSNCHINLGRKNKMQSAMENLEWIDSITMPKKKYDALPEEEK 240
Cdd:PRK09628 161 ATAAGASFVARESVIDPQKLEKLLVKGFSHKGFSFFDVFSNCHINLGRKNKMGEAVQMLKWIESRTVSKRKFDALSPEER 240
|
250 260 270
....*....|....*....|....*....|....*
gi 1917892507 241 LNVFPTGILKEDKEVREYCDMYADIIAVHQGKRKV 275
Cdd:PRK09628 241 VGKFPTGILKHDTDRKEYCEAYEEVIEAAQGKQKV 275
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
4-267 |
1.06e-109 |
|
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: 317.86 E-value: 1.06e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 4 NYDKYLRLEKMPTLWCWGCGDGVILKAFIRAVDKLGIsQDDICVVSGIGCSGRFSSYVDFNTVHTTHGRTVAFATGIKLV 83
Cdd:COG1013 1 VLKKKDLLRTPGHRWCPGCGHGIILRLLLKALDELLD-GDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 84 HPDKYVVCVAGDGDALAIGGNHTIHGARRNIDITLIIINNFIYGLTNSQTSPTTPQGMWTVSQKAGNIDPTFNACDLGIA 163
Cdd:COG1013 80 NPDLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 164 SGASFVARETMLDPKKLEKIFVKALEHRGFSFLDIMSNCHINLGRknkmqSAMENLEWIDSITMPKKKYDALPE----EE 239
Cdd:COG1013 160 HGATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGR-----DPSKTIEWAKEGMWPLYEYDPGEKlrltYE 234
|
250 260
....*....|....*....|....*...
gi 1917892507 240 KLNVFPTGILKeDKEVReYCDMYADIIA 267
Cdd:COG1013 235 PKDKIPVGEFL-KNQGR-FEELIEEIQK 260
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
18-205 |
4.52e-108 |
|
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: 311.38 E-value: 4.52e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 18 WCWGCGDGVILKAFIRAVDKLGISQDDICVVSGIGCSGRFSSYVDFNTVHTTHGRTVAFATGIKLVHPDKYVVCVAGDGD 97
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 98 ALAIGGNHTIHGARRNIDITLIIINNFIYGLTNSQTSPTTPQGMWTVSQKAGNIDPTFNACDLGIASGASFVARETMLDP 177
Cdd:cd03375 81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160
|
170 180
....*....|....*....|....*...
gi 1917892507 178 KKLEKIFVKALEHRGFSFLDIMSNCHIN 205
Cdd:cd03375 161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
18-258 |
3.82e-69 |
|
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: 215.78 E-value: 3.82e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 18 WCWGCGDGVILKAFIRAVDKLGISQDDICVVSGIGCSGRFSSYVDFNTVHTTHGRTVAFATGIKLVHPDKYVVCVAGDGD 97
Cdd:TIGR02177 3 WCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGDGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 98 ALAIGGNHTIHGARRNIDITLIIINNFIYGLTNSQTSPTTPQGMWTVSQKAGNIDPTFNACDLGIASGASFVARETMLDP 177
Cdd:TIGR02177 83 LYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSGDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 178 KKLEKIFVKALEHRGFSFLDIMSNChINLGRKNKMQSAMENLEWIDSITMPKKKYDALPEEEKLNVF-----------PT 246
Cdd:TIGR02177 163 AHLKEIIKEAINHKGYALVDILQPC-VTYNKINTYEWYRERVYKLDEEGYDPIVREPEEFEEKAAAAikkamewgdriPI 241
|
250
....*....|..
gi 1917892507 247 GILKEDKEVREY 258
Cdd:TIGR02177 242 GIFYKNENKPTF 253
|
|
| Oxoac_fdxbeta_Archa |
NF041171 |
2-oxoacid:ferredoxin oxidoreductase subunit beta; |
18-202 |
1.29e-63 |
|
2-oxoacid:ferredoxin oxidoreductase subunit beta;
Pssm-ID: 469082 [Multi-domain] Cd Length: 296 Bit Score: 201.70 E-value: 1.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 18 WCWGCGDGVILKAFIRAVDKLGISQDDICVVSGIGCSGRFSSYVDFNTVHTTHGRTVAFATGIKLVHPDKYVVCVAGDGD 97
Cdd:NF041171 5 WCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGDGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 98 ALAIGGNHTIHGARRNIDITLIIINNFIYGLTNSQTSPTTPQGMWTVSQKAGNIDPTFNACDLGIASGASFVARETMLDP 177
Cdd:NF041171 85 LLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAYDV 164
|
170 180
....*....|....*....|....*
gi 1917892507 178 KKLEKIFVKALEHRGFSFLDIMSNC 202
Cdd:NF041171 165 KHLKELIKAAIKHKGLAFIDVLQPC 189
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
50-198 |
6.33e-36 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 125.78 E-value: 6.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 50 GIGCSGRFSS-YVDFN--------TVHTTHGRTVAFATGIKLVHPDKYVVCVAGDGDALAIgGNHTIHGARRNIDITLII 120
Cdd:pfam02775 1 DIGCHQMWAAqYYRFRpprryltsGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMN-LQELATAVRYNLPITVVV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1917892507 121 INNFIYGLTNSQtspTTPQGMWTVSQKAGNIDPTFNACDLGIASGASfVARETmlDPKKLEKIFVKALEHRGFSFLDI 198
Cdd:pfam02775 80 LNNGGYGMTRGQ---QTPFGGGRYSGPSGKILPPVDFAKLAEAYGAK-GARVE--SPEELEEALKEALEHDGPALIDV 151
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| oorB |
PRK09628 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; |
1-275 |
0e+00 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
Pssm-ID: 182003 [Multi-domain] Cd Length: 277 Bit Score: 544.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 1 MAFNYDKYLRLEKMPTLWCWGCGDGVILKAFIRAVDKLGISQDDICVVSGIGCSGRFSSYVDFNTVHTTHGRTVAFATGI 80
Cdd:PRK09628 1 MAFNYDEYLRVDKMPTLWCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 81 KLVHPDKYVVCVAGDGDALAIGGNHTIHGARRNIDITLIIINNFIYGLTNSQTSPTTPQGMWTVSQKAGNIDPTFNACDL 160
Cdd:PRK09628 81 KLANPDKHVIVVSGDGDGLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 161 GIASGASFVARETMLDPKKLEKIFVKALEHRGFSFLDIMSNCHINLGRKNKMQSAMENLEWIDSITMPKKKYDALPEEEK 240
Cdd:PRK09628 161 ATAAGASFVARESVIDPQKLEKLLVKGFSHKGFSFFDVFSNCHINLGRKNKMGEAVQMLKWIESRTVSKRKFDALSPEER 240
|
250 260 270
....*....|....*....|....*....|....*
gi 1917892507 241 LNVFPTGILKEDKEVREYCDMYADIIAVHQGKRKV 275
Cdd:PRK09628 241 VGKFPTGILKHDTDRKEYCEAYEEVIEAAQGKQKV 275
|
|
| PRK05778 |
PRK05778 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated |
5-283 |
8.87e-115 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
Pssm-ID: 235604 [Multi-domain] Cd Length: 301 Bit Score: 332.23 E-value: 8.87e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 5 YDKYLRLEKMPTLWCWGCGDGVILKAFIRAVDKLGISQDDICVVSGIGCSGRFSSYVDFNTVHTTHGRTVAFATGIKLVH 84
Cdd:PRK05778 7 GLTYLRYDGLPTTWCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLAN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 85 PDKYVVCVAGDGDALAIGGNHTIHGARRNIDITLIIINNFIYGLTNSQTSPTTPQGMWTVSQKAGNIDPTFNACDLGIAS 164
Cdd:PRK05778 87 PDLEVIVVGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 165 GASFVARETMLDPKKLEKIFVKALEHRGFSFLDIMSNCHINLGRKNKMQSAMENLEWIDSITMPKK------------KY 232
Cdd:PRK05778 167 GATFVARSFAGDVKQLVELIKKAISHKGFAFIDVLSPCVTFNGRNTSTKSPAYMREYYKKRVYKLKleedydptdrdkAA 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1917892507 233 DALPEEEKLNVFPTGILKEDkEVREYCDMYADII---AVHQGKRKVITQDDFAK 283
Cdd:PRK05778 247 EKMLEEELGGKIPIGVFYKN-ERPTFEERLEKLIeplLELPPAALRPGKEALDT 299
|
|
| PRK11867 |
PRK11867 |
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed |
1-284 |
2.44e-114 |
|
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
Pssm-ID: 237006 [Multi-domain] Cd Length: 286 Bit Score: 330.65 E-value: 2.44e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 1 MAFNYDKYlRLEKMPTlWCWGCGDGVILKAFIRAVDKLGISQDDICVVSGIGCSGRFSSYVDFNTVHTTHGRTVAFATGI 80
Cdd:PRK11867 4 PMLTAKDF-RNDQEPR-WCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 81 KLVHPDKYVVCVAGDGDALAIGGNHTIHGARRNIDITLIIINNFIYGLTNSQTSPTTPQGMWTVSQKAGNIDPTFNACDL 160
Cdd:PRK11867 82 KLANPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 161 GIASGASFVARETMLDPKKLEKIFVKALEHRGFSFLDIMSNCHInLGRKNKMQSAMENLEWIDSITM--PKKKYDALPEE 238
Cdd:PRK11867 162 ALGAGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPT-FNNVNTFDWFKERLVKVHDAEGydPTNALAAMKTL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1917892507 239 EKLNVFPTGILKeDKEVREYCDMYADIIAVHQGKRKV-ITQDDFAKK 284
Cdd:PRK11867 241 EEGDPIPTGIFY-QVERPTYEEAVRAQIEGPLALQDLlMGGDTWTVL 286
|
|
| PorB |
COG1013 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ... |
4-267 |
1.06e-109 |
|
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: 317.86 E-value: 1.06e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 4 NYDKYLRLEKMPTLWCWGCGDGVILKAFIRAVDKLGIsQDDICVVSGIGCSGRFSSYVDFNTVHTTHGRTVAFATGIKLV 83
Cdd:COG1013 1 VLKKKDLLRTPGHRWCPGCGHGIILRLLLKALDELLD-GDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 84 HPDKYVVCVAGDGDALAIGGNHTIHGARRNIDITLIIINNFIYGLTNSQTSPTTPQGMWTVSQKAGNIDPTFNACDLGIA 163
Cdd:COG1013 80 NPDLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 164 SGASFVARETMLDPKKLEKIFVKALEHRGFSFLDIMSNCHINLGRknkmqSAMENLEWIDSITMPKKKYDALPE----EE 239
Cdd:COG1013 160 HGATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGR-----DPSKTIEWAKEGMWPLYEYDPGEKlrltYE 234
|
250 260
....*....|....*....|....*...
gi 1917892507 240 KLNVFPTGILKeDKEVReYCDMYADIIA 267
Cdd:COG1013 235 PKDKIPVGEFL-KNQGR-FEELIEEIQK 260
|
|
| TPP_OGFOR |
cd03375 |
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ... |
18-205 |
4.52e-108 |
|
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: 311.38 E-value: 4.52e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 18 WCWGCGDGVILKAFIRAVDKLGISQDDICVVSGIGCSGRFSSYVDFNTVHTTHGRTVAFATGIKLVHPDKYVVCVAGDGD 97
Cdd:cd03375 1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 98 ALAIGGNHTIHGARRNIDITLIIINNFIYGLTNSQTSPTTPQGMWTVSQKAGNIDPTFNACDLGIASGASFVARETMLDP 177
Cdd:cd03375 81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160
|
170 180
....*....|....*....|....*...
gi 1917892507 178 KKLEKIFVKALEHRGFSFLDIMSNCHIN 205
Cdd:cd03375 161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
|
|
| PRK11866 |
PRK11866 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
13-202 |
1.93e-73 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183347 [Multi-domain] Cd Length: 279 Bit Score: 226.56 E-value: 1.93e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 13 KMPTLWCWGCGDGVILKAFIRAVDKLGISQDDICVVSGIGCSGRFSSYVDFNTVHTTHGRTVAFATGIKLVHPDKYVVCV 92
Cdd:PRK11866 4 KRPPIWCPGCGNYGILEALRKALAELGIPPENVVVVSGIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLTVIGY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 93 AGDGDALAIGGNHTIHGARRNIDITLIIINNFIYGLTNSQTSPTTPQGMWTVSQKAGNIDPTFNACDLGIASGASFVARE 172
Cdd:PRK11866 84 GGDGDGYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATFVARG 163
|
170 180 190
....*....|....*....|....*....|
gi 1917892507 173 TMLDPKKLEKIFVKALEHRGFSFLDIMSNC 202
Cdd:PRK11866 164 FSGDVKHLKEIIKEAIKHKGFSFIDVLSPC 193
|
|
| PorB_KorB |
TIGR02177 |
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ... |
18-258 |
3.82e-69 |
|
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: 215.78 E-value: 3.82e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 18 WCWGCGDGVILKAFIRAVDKLGISQDDICVVSGIGCSGRFSSYVDFNTVHTTHGRTVAFATGIKLVHPDKYVVCVAGDGD 97
Cdd:TIGR02177 3 WCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGDGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 98 ALAIGGNHTIHGARRNIDITLIIINNFIYGLTNSQTSPTTPQGMWTVSQKAGNIDPTFNACDLGIASGASFVARETMLDP 177
Cdd:TIGR02177 83 LYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSGDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 178 KKLEKIFVKALEHRGFSFLDIMSNChINLGRKNKMQSAMENLEWIDSITMPKKKYDALPEEEKLNVF-----------PT 246
Cdd:TIGR02177 163 AHLKEIIKEAINHKGYALVDILQPC-VTYNKINTYEWYRERVYKLDEEGYDPIVREPEEFEEKAAAAikkamewgdriPI 241
|
250
....*....|..
gi 1917892507 247 GILKEDKEVREY 258
Cdd:TIGR02177 242 GIFYKNENKPTF 253
|
|
| Oxoac_fdxbeta_Archa |
NF041171 |
2-oxoacid:ferredoxin oxidoreductase subunit beta; |
18-202 |
1.29e-63 |
|
2-oxoacid:ferredoxin oxidoreductase subunit beta;
Pssm-ID: 469082 [Multi-domain] Cd Length: 296 Bit Score: 201.70 E-value: 1.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 18 WCWGCGDGVILKAFIRAVDKLGISQDDICVVSGIGCSGRFSSYVDFNTVHTTHGRTVAFATGIKLVHPDKYVVCVAGDGD 97
Cdd:NF041171 5 WCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGDGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 98 ALAIGGNHTIHGARRNIDITLIIINNFIYGLTNSQTSPTTPQGMWTVSQKAGNIDPTFNACDLGIASGASFVARETMLDP 177
Cdd:NF041171 85 LLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAYDV 164
|
170 180
....*....|....*....|....*
gi 1917892507 178 KKLEKIFVKALEHRGFSFLDIMSNC 202
Cdd:NF041171 165 KHLKELIKAAIKHKGLAFIDVLQPC 189
|
|
| PRK11869 |
PRK11869 |
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional |
10-249 |
2.93e-60 |
|
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
Pssm-ID: 183349 [Multi-domain] Cd Length: 280 Bit Score: 192.69 E-value: 2.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 10 RLEKMPTLWCWGCGDGVILKAFIRAVDKLGISQDDICVVSGIGCSGRFSSYVDFNTVHTTHGRTVAFATGIKLVHPDKYV 89
Cdd:PRK11869 2 RPEKYDIAWCPGCGNFGIRNALMKALSELNLKPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 90 VCVAGDGDALAIGGNHTIHGARRNIDITLIIINNFIYGLTNSQTSPTTPQGMWTVSQKAGNIDPTFNACDLGIASGASFV 169
Cdd:PRK11869 82 IAEGGDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASFV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 170 ARETMLDPKKLEKIFVKALEHRGFSFLDIMSNChINLGRKNKMQSAMENLEWIDS--ITMPKKKYDALPEEEKlnvFPTG 247
Cdd:PRK11869 162 ARTFSGDIEETKEILKEAIKHKGLAIVDIFQPC-VSFNKVNTYQWYRENTYYLKDhdPTDRELAFKRALETEK---LPLG 237
|
..
gi 1917892507 248 IL 249
Cdd:PRK11869 238 IF 239
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
50-198 |
6.33e-36 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 125.78 E-value: 6.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 50 GIGCSGRFSS-YVDFN--------TVHTTHGRTVAFATGIKLVHPDKYVVCVAGDGDALAIgGNHTIHGARRNIDITLII 120
Cdd:pfam02775 1 DIGCHQMWAAqYYRFRpprryltsGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMN-LQELATAVRYNLPITVVV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1917892507 121 INNFIYGLTNSQtspTTPQGMWTVSQKAGNIDPTFNACDLGIASGASfVARETmlDPKKLEKIFVKALEHRGFSFLDI 198
Cdd:pfam02775 80 LNNGGYGMTRGQ---QTPFGGGRYSGPSGKILPPVDFAKLAEAYGAK-GARVE--SPEELEEALKEALEHDGPALIDV 151
|
|
| TPP_PFOR |
cd02018 |
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ... |
19-207 |
2.31e-20 |
|
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: 87.16 E-value: 2.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 19 CWGCGDGVILKAFIRAVDklgiSQDDICVVSGIGCSGRFSSYVDFN-----TVHTTHGRTVAFATGIKLV---------- 83
Cdd:cd02018 8 CAGCGEVTAVRVVLAALP----APEDTVIANSTGCSSVYASTAPFNswavpWVNSLFEDANAVASGLKRGlkarfpkdre 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 84 ---HPDkyVVCVAGDGDALAIGGNHTIHGARRNIDITLIIINNFIYGLTNSQTSPTTPQGMWTVSQKAGNIDPTFNACDL 160
Cdd:cd02018 84 ldkKKD--VVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKKDLVLI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1917892507 161 GIASGASFVARETMLDPKKLEKIFVKAL-EHRGFSFLDIMSNCHINLG 207
Cdd:cd02018 162 AATHGCVYVARLSPALKKHFLKVVKEAIsRTDGPTFIHAYTPCITEWG 209
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
30-199 |
3.82e-14 |
|
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: 68.82 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 30 AFIRAVDKLGisQDDICVVSGIGCSGRFS-SYVDF--------NTVHTTHGRTVAFATGIKLVHPDKYVVCVAGDGDALA 100
Cdd:cd00568 1 RVLAALRAAL--PEDAIVVNDAGNSAYWAyRYLPLrrgrrfltSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDGGFMM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 101 iGGNHTIHGARRNIDITLIIINNFIYGLTNSQtspttpQGMWTVSQKAGNIDPTFNACDLGIASGAsFVARETmlDPKKL 180
Cdd:cd00568 79 -TGQELATAVRYGLPVIVVVFNNGGYGTIRMH------QEAFYGGRVSGTDLSNPDFAALAEAYGA-KGVRVE--DPEDL 148
|
170
....*....|....*....
gi 1917892507 181 EKIFVKALEHRGFSFLDIM 199
Cdd:cd00568 149 EAALAEALAAGGPALIEVK 167
|
|
| TPP_PFOR_porB_like |
cd03376 |
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ... |
19-202 |
7.86e-14 |
|
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: 69.19 E-value: 7.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 19 CWGCGDGVILKAFIRAVDKlgisqdDICVVSGIGCSGRFSS-Y----VDFNTVHTTHGRTVAFATGIK-----LVHPDKY 88
Cdd:cd03376 8 CAGCGAALALRHVLKALGP------DTVVVNPTGCLEVITTpYpytaWRVPWIHVAFENAAAVASGIEaalkaLGRGKDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 89 -VVCVAGDGDALAIGGNHTIHGARRNIDITLIIINNFIYGLTNSQTSPTTPQGMWTVSQKAGNIDP--TFNACDLG---I 162
Cdd:cd03376 82 tVVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTTPVGKVSFgkKQPKKDLPlimA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1917892507 163 ASGASFVARETMLDPKKLEKIFVKALEHRGFSFLDIMSNC 202
Cdd:cd03376 162 AHNIPYVATASVAYPEDLYKKVKKALSIEGPAYIHILSPC 201
|
|
| PRK11864 |
PRK11864 |
3-methyl-2-oxobutanoate dehydrogenase subunit beta; |
19-202 |
4.07e-13 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
Pssm-ID: 237005 [Multi-domain] Cd Length: 300 Bit Score: 68.19 E-value: 4.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 19 CWGCGDGVILKAFIRAVDKLGISQDDICVVSGIGCSGRFSSyVDFNTVHTTHGRTVAFATGIK-----LVHPDKYVVCVA 93
Cdd:PRK11864 21 CPGCGAPLGLRYLLKALGEKTVLVIPASCSTVIQGDTPKSP-LTVPVLHTAFAATAAVASGIEealkaRGEKGVIVVGWA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 94 GDGDALAIGGNHTIHGARRNIDITLIIINNFIYGLTNSQTSPTTPQGMWTVSQKAGNIDPTFNACDLGIASGASFVARET 173
Cdd:PRK11864 100 GDGGTADIGFQALSGAAERNHDILYIMYDNEAYMNTGIQRSSSTPYGAWTTTTPGGKREHKKPVPDIMAAHKVPYVATAS 179
|
170 180
....*....|....*....|....*....
gi 1917892507 174 MLDPKKLEKIFVKALEHRGFSFLDIMSNC 202
Cdd:PRK11864 180 IAYPEDFIRKLKKAKEIRGFKFIHLLAPC 208
|
|
| PRK11865 |
PRK11865 |
pyruvate synthase subunit beta; |
19-202 |
3.89e-09 |
|
pyruvate synthase subunit beta;
Pssm-ID: 183346 [Multi-domain] Cd Length: 299 Bit Score: 56.26 E-value: 3.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 19 CWGCGDGVILKAFIRAVDKlgisqdDICVVSGIGCSGRFSSYVDFNT-----VHTTHGRTVAFATGI----KLVHPDKYV 89
Cdd:PRK11865 21 CAGCGAAIAMRLALKALGK------NTVIVVATGCLEVITTPYPETAwnvpwIHVAFENAAAVASGIeravKALGKKVNV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 90 VCVAGDGDALAIGGNHTIHGARRNIDITLIIINNFIYGLTNSQTSPTTPQGMWTVSQKAGNI-----DPTFNACDLGIAS 164
Cdd:PRK11865 95 VAIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKYsrgedRPKKNMPLIMAAH 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1917892507 165 GASFVARETMLDPKKLEKIFVKALEHRGFSFLDIMSNC 202
Cdd:PRK11865 175 GIPYVATASIGYPEDFMEKVKKAKEVEGPAYIQVLQPC 212
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
15-202 |
5.34e-08 |
|
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: 51.51 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 15 PTLwCWGCGDgvilKAFIRAVDKLGisQDDICVVSGIGCSGrFSSYVDFNTVHTT--HGRTVAFATGIKLVHPDKYVVCV 92
Cdd:cd02008 4 PGL-CPGCPH----RPSFYALRKAF--KKDSIVSGDIGCYT-LGALPPLNAIDTCtcMGASIGVAIGMAKASEDKKVVAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 93 AGDGDALAIGGNHTIHGARRNIDITLIIINNFIYGLTNSQTSPTTPqgmWTVSQKAGNIDPTfnacDLGIASGASFVARE 172
Cdd:cd02008 76 IGDSTFFHSGILGLINAVYNKANITVVILDNRTTAMTGGQPHPGTG---KTLTEPTTVIDIE----ALVRAIGVKRVVVV 148
|
170 180 190
....*....|....*....|....*....|
gi 1917892507 173 TMLDPKKLEKIFVKALEHRGFSFLDIMSNC 202
Cdd:cd02008 149 DPYDLKAIREELKEALAVPGVSVIIAKRPC 178
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
77-199 |
2.27e-07 |
|
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: 49.90 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 77 ATGIKLVHPDKYVVCVAGDGDAlaiggNHTIHG----ARRNIDITLIIINNFIYGLTNSQTspttpQGMWTVSQKAGNI- 151
Cdd:cd02002 58 AVGAALANPDRKVVAIIGDGSF-----MYTIQAlwtaARYGLPVTVVILNNRGYGALRSFL-----KRVGPEGPGENAPd 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1917892507 152 -----DPTFNACdlGIASGASFVARETMlDPKKLEKIFVKALEHRGFSFLDIM 199
Cdd:cd02002 128 gldllDPGIDFA--AIAKAFGVEAERVE-TPEELDEALREALAEGGPALIEVV 177
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
30-199 |
7.50e-07 |
|
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: 50.16 E-value: 7.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 30 AFIRAVDKLgISQDDIcVVSGIGCSGRFSS-YVDF---NTVHTTHG-RTVAF----ATGIKLVHPDKYVVCVAGDGD--- 97
Cdd:COG0028 367 RVIAALREA-LPDDAI-VVTDVGQHQMWAArYLRFrrpRRFLTSGGlGTMGYglpaAIGAKLARPDRPVVAITGDGGfqm 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 98 ---ALAiggnhTIhgARRNIDITLIIINNFIYGltnsqtspttpqgmwTVSQKAGNI-DPTFNACDLGiasGASFV--AR 171
Cdd:COG0028 445 nlqELA-----TA--VRYGLPVKVVVLNNGGLG---------------MVRQWQELFyGGRYSGTDLP---NPDFAklAE 499
|
170 180 190
....*....|....*....|....*....|....
gi 1917892507 172 ------ETMLDPKKLEKIFVKALEHRGFSFLDIM 199
Cdd:COG0028 500 afgakgERVETPEELEAALEEALASDGPALIDVR 533
|
|
| TPP_AHAS |
cd02015 |
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ... |
76-199 |
2.24e-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: 47.11 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 76 FATGIKLVHPDKYVVCVAGDGDAL-AIGGNHTIhgARRNIDITLIIINNfiygltNSqtspttpQGM---WTV------- 144
Cdd:cd02015 58 AAIGAKVARPDKTVICIDGDGSFQmNIQELATA--AQYNLPVKIVILNN------GS-------LGMvrqWQElfyegry 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1917892507 145 SQKAGNIDPTFNAcdlgIASGASFVAReTMLDPKKLEKIFVKALEHRGFSFLDIM 199
Cdd:cd02015 123 SHTTLDSNPDFVK----LAEAYGIKGL-RVEKPEELEAALKEALASDGPVLLDVL 172
|
|
| PRK12474 |
PRK12474 |
hypothetical protein; Provisional |
71-199 |
2.86e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 139002 [Multi-domain] Cd Length: 518 Bit Score: 45.25 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 71 GRTVAFATGIKLVHPDKYVVCVAGDGdalaiGGNHTIHG----ARRNIDITLIIINNFIYGLTNSQTSPTTPQGMWTVSQ 146
Cdd:PRK12474 392 GQGLPLAAGAAVAAPDRKVVCPQGDG-----GAAYTMQAlwtmARENLDVTVVIFANRSYAILNGELQRVGAQGAGRNAL 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1917892507 147 KAGNID-PTFN----ACDLGIASGASFVAREtmldpkkLEKIFVKALEHRGFSFLDIM 199
Cdd:PRK12474 467 SMLDLHnPELNwmkiAEGLGVEASRATTAEE-------FSAQYAAAMAQRGPRLIEAM 517
|
|
| TPP_PpyrDC |
cd03371 |
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ... |
77-198 |
3.33e-05 |
|
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: 43.46 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 77 ATGIKLVHPDKYVVCVAGDGDALAIGGNHTIHGARRNIDITLIIINNFIYGLTNSQTspttpqgmwTVSQkagnidpTFN 156
Cdd:cd03371 57 ALGIALARPDRKVVCIDGDGAALMHMGGLATIGGLAPANLIHIVLNNGAHDSVGGQP---------TVSF-------DVS 120
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1917892507 157 ACDLGIASGASFVARETmlDPKKLEKIFVKALEHRGFSFLDI 198
Cdd:cd03371 121 LPAIAKACGYRAVYEVP--SLEELVAALAKALAADGPAFIEV 160
|
|
| PRK08199 |
PRK08199 |
thiamine pyrophosphate protein; Validated |
77-127 |
5.19e-05 |
|
thiamine pyrophosphate protein; Validated
Pssm-ID: 181285 [Multi-domain] Cd Length: 557 Bit Score: 44.48 E-value: 5.19e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1917892507 77 ATGIKLVHPDKYVVCVAGDGDALaIGGNHTIHGARRNIDITLIIINNFIYG 127
Cdd:PRK08199 424 AIAAKLLFPERTVVAFAGDGCFL-MNGQELATAVQYGLPIIVIVVNNGMYG 473
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
76-139 |
9.73e-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: 42.13 E-value: 9.73e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1917892507 76 FATGIKLVHPDKYVVCVAGDGdALAIGGNH--TIhgARRNIDITLIIINNF-IYGLTNSQTSPTTPQ 139
Cdd:cd02004 56 YAIAAALARPDKRVVLVEGDG-AFGFSGMEleTA--VRYNLPIVVVVGNNGgWYQGLDGQQLSYGLG 119
|
|
| TPP_ComE_PpyrDC |
cd02001 |
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ... |
32-166 |
9.89e-05 |
|
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: 41.70 E-value: 9.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 32 IRAVDKLGISQDDICVVSGIGCSGRFSSYVDFNTVH----TTHGRTVAFATGIKLVHPDKyVVCVAGDGDALAIGGNHTI 107
Cdd:cd02001 2 IAAIAEIIEASGDTPIVSTTGYASRELYDVQDRDGHfymlGSMGLAGSIGLGLALGLSRK-VIVVDGDGSLLMNPGVLLT 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1917892507 108 HGARRNIDITLIIINNFIYGLTNSQTSPTTPQGMWTVSQKAGNIdpTFNACDLGIASGA 166
Cdd:cd02001 81 AGEFTPLNLILVVLDNRAYGSTGGQPTPSSNVNLEAWAAACGYL--VLSAPLLGGLGSE 137
|
|
| PRK07092 |
PRK07092 |
benzoylformate decarboxylase; Reviewed |
77-127 |
1.09e-04 |
|
benzoylformate decarboxylase; Reviewed
Pssm-ID: 235931 [Multi-domain] Cd Length: 530 Bit Score: 43.41 E-value: 1.09e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1917892507 77 ATGIKLVHPDKYVVCVAGDGDAL-AIGGNHTihGARRNIDITLIIINNFIYG 127
Cdd:PRK07092 416 AVGVALAQPGRRVIGLIGDGSAMySIQALWS--AAQLKLPVTFVILNNGRYG 465
|
|
| TPP_POX |
cd02014 |
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ... |
77-199 |
1.72e-04 |
|
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; composed of proteins similar to Lactobacillus plantarum POX, which plays a key role in controlling acetate production under aerobic conditions. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. It requires FAD in addition to TPP and a divalent cation as cofactors.
Pssm-ID: 238972 [Multi-domain] Cd Length: 178 Bit Score: 41.36 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1917892507 77 ATGIKLVHPDKYVVCVAGDGdALAIGGNHTIHGARRNIDITLIIINNFIYGL-TNSQTSptTPQGMWTVSQkagnIDPTF 155
Cdd:cd02014 60 AIAAKLAYPDRQVIALSGDG-GFAMLMGDLITAVKYNLPVIVVVFNNSDLGFiKWEQEV--MGQPEFGVDL----PNPDF 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1917892507 156 NAcdlgIASGASFVAReTMLDPKKLEKIFVKALEHRGFSFLDIM 199
Cdd:cd02014 133 AK----IAEAMGIKGI-RVEDPDELEAALDEALAADGPVVIDVV 171
|
|
| PRK06112 |
PRK06112 |
acetolactate synthase catalytic subunit; Validated |
71-127 |
3.73e-04 |
|
acetolactate synthase catalytic subunit; Validated
Pssm-ID: 235700 [Multi-domain] Cd Length: 578 Bit Score: 41.67 E-value: 3.73e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917892507 71 GRTVAFATGIKLVHPDKYVVCVAGDGdalaiGGNHT---IHGARR-NIDITLIIINNFIYG 127
Cdd:PRK06112 440 GWGVPMAIGAKVARPGAPVICLVGDG-----GFAHVwaeLETARRmGVPVTIVVLNNGILG 495
|
|
| PRK06154 |
PRK06154 |
thiamine pyrophosphate-requiring protein; |
68-127 |
2.48e-03 |
|
thiamine pyrophosphate-requiring protein;
Pssm-ID: 235718 [Multi-domain] Cd Length: 565 Bit Score: 39.02 E-value: 2.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1917892507 68 TTH-GRTVAFATGIKLVHPDKYVVCVAGDGdalAIG--GNHTIHGARRNIDITLIIINNFIYG 127
Cdd:PRK06154 430 TTQlGYGLGLAMGAKLARPDALVINLWGDA---AFGmtGMDFETAVRERIPILTILLNNFSMG 489
|
|
| PRK07586 |
PRK07586 |
acetolactate synthase large subunit; |
77-126 |
2.96e-03 |
|
acetolactate synthase large subunit;
Pssm-ID: 236063 [Multi-domain] Cd Length: 514 Bit Score: 38.67 E-value: 2.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1917892507 77 ATGIKLVHPDKYVVCVAGDGDALaiggnHTIHG----ARRNIDITLIIINNFIY 126
Cdd:PRK07586 394 ATGAAVACPDRKVLALQGDGSAM-----YTIQAlwtqARENLDVTTVIFANRAY 442
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
77-127 |
3.88e-03 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 38.44 E-value: 3.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1917892507 77 ATGIKLVHPDKYVVCVAGDGdALAIGGNHTIHGARRNIDITLIIINNFIYG 127
Cdd:PRK07525 444 IIGAKIACPDRPVVGFAGDG-AWGISMNEVMTAVRHNWPVTAVVFRNYQWG 493
|
|
| PRK08322 |
PRK08322 |
acetolactate synthase large subunit; |
75-128 |
9.09e-03 |
|
acetolactate synthase large subunit;
Pssm-ID: 236239 [Multi-domain] Cd Length: 547 Bit Score: 37.50 E-value: 9.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1917892507 75 AFAT-GI--------KLVHPDKYVVCVAGDGDAL--------AIggnhtihgaRRNIDITLIIINNFIYGL 128
Cdd:PRK08322 404 ALATmGAglpsaiaaKLVHPDRKVLAVCGDGGFMmnsqeletAV---------RLGLPLVVLILNDNAYGM 465
|
|
|