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Conserved domains on  [gi|1063808819|gb|AOO65201|]
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2-oxoglutarate oxidoreductase, beta subunit [Sulfurospirillum halorespirans DSM 13726]

Protein Classification

2-oxoglutarate ferredoxin oxidoreductase subunit beta( domain architecture ID 11484422)

2-oxoglutarate ferredoxin oxidoreductase subunit beta (OorB) is a component of 2-oxoglutarate:acceptor oxidoreductase (OOR) that catalyzes the analogous, reversible oxidative decarboxylation of 2-oxoglutarate to form succinyl coenzyme A (succinyl-CoA), a major intermediate of the tricarboxylic acid (TCA) cycle

Graphical summary

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List of domain hits

 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: 577.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819   1 MAFNYDKYLRVDKMPTLWCWGCGDGVILKSVIRAIDKMGWDMNDVCIVSGIGCSGRFSSYIDCNTVHTTHGRAIAYATGI 80
Cdd:PRK09628    1 MAFNYDEYLRVDKMPTLWCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  81 KLANPEKHVIVVTGDGDGLAIGGNHTIHGCRRNIDLNHILINNFIYGLTNSQTSPTTPQGFWTATANYGNVDPTFDAAKL 160
Cdd:PRK09628   81 KLANPDKHVIVVSGDGDGLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819 161 ADAAGATFVARESVLDPQKLEKIFVAGFTHKGYSFFDVFSNCHINLGRKNKMGEAVQNLEWIENRIVGKNKFELLSAEER 240
Cdd:PRK09628  161 ATAAGASFVARESVIDPQKLEKLLVKGFSHKGFSFFDVFSNCHINLGRKNKMGEAVQMLKWIESRTVSKRKFDALSPEER 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1063808819 241 VDKFPTGILKQEEGKLEYCEAYDKVIYAAQNKTTV 275
Cdd:PRK09628  241 VGKFPTGILKHDTDRKEYCEAYEEVIEAAQGKQKV 275
 
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: 577.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819   1 MAFNYDKYLRVDKMPTLWCWGCGDGVILKSVIRAIDKMGWDMNDVCIVSGIGCSGRFSSYIDCNTVHTTHGRAIAYATGI 80
Cdd:PRK09628    1 MAFNYDEYLRVDKMPTLWCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  81 KLANPEKHVIVVTGDGDGLAIGGNHTIHGCRRNIDLNHILINNFIYGLTNSQTSPTTPQGFWTATANYGNVDPTFDAAKL 160
Cdd:PRK09628   81 KLANPDKHVIVVSGDGDGLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819 161 ADAAGATFVARESVLDPQKLEKIFVAGFTHKGYSFFDVFSNCHINLGRKNKMGEAVQNLEWIENRIVGKNKFELLSAEER 240
Cdd:PRK09628  161 ATAAGASFVARESVIDPQKLEKLLVKGFSHKGFSFFDVFSNCHINLGRKNKMGEAVQMLKWIESRTVSKRKFDALSPEER 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1063808819 241 VDKFPTGILKQEEGKLEYCEAYDKVIYAAQNKTTV 275
Cdd:PRK09628  241 VGKFPTGILKHDTDRKEYCEAYEEVIEAAQGKQKV 275
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 13-266 1.91e-105

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: 306.69  E-value: 1.91e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  13 KMPTLWCWGCGDGVILKSVIRAIDKMgWDMNDVCIVSGIGCSGRFSSYIDCNTVHTTHGRAIAYATGIKLANPEKHVIVV 92
Cdd:COG1013    10 TPGHRWCPGCGHGIILRLLLKALDEL-LDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANPDLTVIVF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  93 TGDGDGLAIGGNHTIHGCRRNIDLNHILINNFIYGLTNSQTSPTTPQGFWTATANYGNVDPTFDAAKLADAAGATFVARE 172
Cdd:COG1013    89 GGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHGATYVARA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819 173 SVLDPQKLEKIFVAGFTHKGYSFFDVFSNCHINLGRknkmgEAVQNLEWIENRIV----GKNKFELLSAEERVDKFPTGI 248
Cdd:COG1013   169 SVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGR-----DPSKTIEWAKEGMWplyeYDPGEKLRLTYEPKDKIPVGE 243

                         250
                  ....*....|....*...
gi 1063808819 249 LKQEEGKleYCEAYDKVI 266
Cdd:COG1013   244 FLKNQGR--FEELIEEIQ 259
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 18-205 3.06e-105

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: 303.68  E-value: 3.06e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  18 WCWGCGDGVILKSVIRAIDKMGWDMNDVCIVSGIGCSGRFSSYIDCNTVHTTHGRAIAYATGIKLANPEKHVIVVTGDGD 97
Cdd:cd03375     1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  98 GLAIGGNHTIHGCRRNIDLNHILINNFIYGLTNSQTSPTTPQGFWTATANYGNVDPTFDAAKLADAAGATFVARESVLDP 177
Cdd:cd03375    81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160

                         170       180
                  ....*....|....*....|....*...
gi 1063808819 178 QKLEKIFVAGFTHKGYSFFDVFSNCHIN 205
Cdd:cd03375   161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
PorB_KorB TIGR02177
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ...
 18-202 3.67e-63

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: 199.99  E-value: 3.67e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  18 WCWGCGDGVILKSVIRAIDKMGWDMNDVCIVSGIGCSGRFSSYIDCNTVHTTHGRAIAYATGIKLANPEKHVIVVTGDGD 97
Cdd:TIGR02177   3 WCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGDGD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  98 GLAIGGNHTIHGCRRNIDLNHILINNFIYGLTNSQTSPTTPQGFWTATANYGNVDPTFDAAKLADAAGATFVARESVLDP 177
Cdd:TIGR02177  83 LYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSGDV 162

                         170       180
                  ....*....|....*....|....*
gi 1063808819 178 QKLEKIFVAGFTHKGYSFFDVFSNC 202
Cdd:TIGR02177 163 AHLKEIIKEAINHKGYALVDILQPC 187
Oxoac_fdxbeta_Archa NF041171
2-oxoacid:ferredoxin oxidoreductase subunit beta;
18-253 2.34e-59

2-oxoacid:ferredoxin oxidoreductase subunit beta;


Pssm-ID: 469082 [Multi-domain]  Cd Length: 296  Bit Score: 190.53  E-value: 2.34e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  18 WCWGCGDGVILKSVIRAIDKMGWDMNDVCIVSGIGCSGRFSSYIDCNTVHTTHGRAIAYATGIKLANPEKHVIVVTGDGD 97
Cdd:NF041171    5 WCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGDGD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  98 GLAIGGNHTIHGCRRNIDLNHILINNFIYGLTNSQTSPTTPQGFWTATANYGNVDPTFDAAKLADAAGATFVARESVLDP 177
Cdd:NF041171   85 LLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAYDV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819 178 QKLEKIFVAGFTHKGYSFFDVFSNC----HINlgrknkmgeavqNLEWIENRIVgknKFE--------LLSAEERVDKFP 245
Cdd:NF041171  165 KHLKELIKAAIKHKGLAFIDVLQPCptynDIN------------TKEWYDKRVY---KLDdepgwdpvVRSPEEADEKMA 229


                  ....*...
gi 1063808819 246 TGILKQEE 253
Cdd:NF041171  230 KAIEKALE 237
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
50-198 4.51e-29

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 107.67  E-value: 4.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  50 GIGCSGRFS----------SYIDcNTVHTTHGRAIAYATGIKLANPEKHVIVVTGDGDGLAIgGNHTIHGCRRNIDLNHI 119
Cdd:pfam02775   1 DIGCHQMWAaqyyrfrpprRYLT-SGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMN-LQELATAVRYNLPITVV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819 120 LINNFIYGLTNSQtspTTPQGFWTATANYGNVDPTFDaakladaagatFVA--------RESVLDPQKLEKIFVAGFTHK 191
Cdd:pfam02775  79 VLNNGGYGMTRGQ---QTPFGGGRYSGPSGKILPPVD-----------FAKlaeaygakGARVESPEELEEALKEALEHD 144


                  ....*..
gi 1063808819 192 GYSFFDV 198
Cdd:pfam02775 145 GPALIDV 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: 577.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819   1 MAFNYDKYLRVDKMPTLWCWGCGDGVILKSVIRAIDKMGWDMNDVCIVSGIGCSGRFSSYIDCNTVHTTHGRAIAYATGI 80
Cdd:PRK09628    1 MAFNYDEYLRVDKMPTLWCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  81 KLANPEKHVIVVTGDGDGLAIGGNHTIHGCRRNIDLNHILINNFIYGLTNSQTSPTTPQGFWTATANYGNVDPTFDAAKL 160
Cdd:PRK09628   81 KLANPDKHVIVVSGDGDGLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819 161 ADAAGATFVARESVLDPQKLEKIFVAGFTHKGYSFFDVFSNCHINLGRKNKMGEAVQNLEWIENRIVGKNKFELLSAEER 240
Cdd:PRK09628  161 ATAAGASFVARESVIDPQKLEKLLVKGFSHKGFSFFDVFSNCHINLGRKNKMGEAVQMLKWIESRTVSKRKFDALSPEER 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1063808819 241 VDKFPTGILKQEEGKLEYCEAYDKVIYAAQNKTTV 275
Cdd:PRK09628  241 VGKFPTGILKHDTDRKEYCEAYEEVIEAAQGKQKV 275
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 1-272 7.49e-116

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 334.12  E-value: 7.49e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819   1 MAFNYDKYLRvDKMPTlWCWGCGDGVILKSVIRAIDKMGWDMNDVCIVSGIGCSGRFSSYIDCNTVHTTHGRAIAYATGI 80
Cdd:PRK11867    4 PMLTAKDFRN-DQEPR-WCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  81 KLANPEKHVIVVTGDGDGLAIGGNHTIHGCRRNIDLNHILINNFIYGLTNSQTSPTTPQGFWTATANYGNVDPTFDAAKL 160
Cdd:PRK11867   82 KLANPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVEL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819 161 ADAAGATFVARESVLDPQKLEKIFVAGFTHKGYSFFDVFSNCHI--NLGRKNKMGEAVQNLEWIENRIVgKNKFELLSAE 238
Cdd:PRK11867  162 ALGAGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTfnNVNTFDWFKERLVKVHDAEGYDP-TNALAAMKTL 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1063808819 239 ERVDKFPTGILKQEEgKLEYCEAYDKVIYAAQNK 272
Cdd:PRK11867  241 EEGDPIPTGIFYQVE-RPTYEEAVRAQIEGPLAL 273
PRK05778 PRK05778
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
 5-266 1.26e-108

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated


Pssm-ID: 235604 [Multi-domain]  Cd Length: 301  Bit Score: 316.43  E-value: 1.26e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819   5 YDKYLRVDKMPTLWCWGCGDGVILKSVIRAIDKMGWDMNDVCIVSGIGCSGRFSSYIDCNTVHTTHGRAIAYATGIKLAN 84
Cdd:PRK05778    7 GLTYLRYDGLPTTWCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLAN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  85 PEKHVIVVTGDGDGLAIGGNHTIHGCRRNIDLNHILINNFIYGLTNSQTSPTTPQGFWTATANYGNVDPTFDAAKLADAA 164
Cdd:PRK05778   87 PDLEVIVVGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819 165 GATFVARESVLDPQKLEKIFVAGFTHKGYSFFDVFSNCHINLGRKNKMGEAVQNLEWIENRIV------------GKNKF 232
Cdd:PRK05778  167 GATFVARSFAGDVKQLVELIKKAISHKGFAFIDVLSPCVTFNGRNTSTKSPAYMREYYKKRVYklkleedydptdRDKAA 246

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1063808819 233 ELLSAEERVDKFPTGILKQEEgKLEYCEAYDKVI 266
Cdd:PRK05778  247 EKMLEEELGGKIPIGVFYKNE-RPTFEERLEKLI 279
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 13-266 1.91e-105

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: 306.69  E-value: 1.91e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  13 KMPTLWCWGCGDGVILKSVIRAIDKMgWDMNDVCIVSGIGCSGRFSSYIDCNTVHTTHGRAIAYATGIKLANPEKHVIVV 92
Cdd:COG1013    10 TPGHRWCPGCGHGIILRLLLKALDEL-LDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANPDLTVIVF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  93 TGDGDGLAIGGNHTIHGCRRNIDLNHILINNFIYGLTNSQTSPTTPQGFWTATANYGNVDPTFDAAKLADAAGATFVARE 172
Cdd:COG1013    89 GGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHGATYVARA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819 173 SVLDPQKLEKIFVAGFTHKGYSFFDVFSNCHINLGRknkmgEAVQNLEWIENRIV----GKNKFELLSAEERVDKFPTGI 248
Cdd:COG1013   169 SVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGR-----DPSKTIEWAKEGMWplyeYDPGEKLRLTYEPKDKIPVGE 243

                         250
                  ....*....|....*...
gi 1063808819 249 LKQEEGKleYCEAYDKVI 266
Cdd:COG1013   244 FLKNQGR--FEELIEEIQ 259
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 18-205 3.06e-105

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: 303.68  E-value: 3.06e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  18 WCWGCGDGVILKSVIRAIDKMGWDMNDVCIVSGIGCSGRFSSYIDCNTVHTTHGRAIAYATGIKLANPEKHVIVVTGDGD 97
Cdd:cd03375     1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  98 GLAIGGNHTIHGCRRNIDLNHILINNFIYGLTNSQTSPTTPQGFWTATANYGNVDPTFDAAKLADAAGATFVARESVLDP 177
Cdd:cd03375    81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160

                         170       180
                  ....*....|....*....|....*...
gi 1063808819 178 QKLEKIFVAGFTHKGYSFFDVFSNCHIN 205
Cdd:cd03375   161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
PRK11866 PRK11866
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 13-266 1.94e-64

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183347 [Multi-domain]  Cd Length: 279  Bit Score: 203.06  E-value: 1.94e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  13 KMPTLWCWGCGDGVILKSVIRAIDKMGWDMNDVCIVSGIGCSGRFSSYIDCNTVHTTHGRAIAYATGIKLANPEKHVIVV 92
Cdd:PRK11866    4 KRPPIWCPGCGNYGILEALRKALAELGIPPENVVVVSGIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLTVIGY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  93 TGDGDGLAIGGNHTIHGCRRNIDLNHILINNFIYGLTNSQTSPTTPQGFWTATANYGNVDPTFDAAKLADAAGATFVARE 172
Cdd:PRK11866   84 GGDGDGYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATFVARG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819 173 SVLDPQKLEKIFVAGFTHKGYSFFDVFSNChINLGRKNK---MGEAVQNLEWIENRIvgKNKFELLS-AEERVDKFPTGI 248
Cdd:PRK11866  164 FSGDVKHLKEIIKEAIKHKGFSFIDVLSPC-VTFNKLNTydwFRPRVYKLEETGHDP--TNFEQAYKkALEWGDRIPIGV 240

                         250
                  ....*....|....*...
gi 1063808819 249 LKQEEgKLEYCEAYDKVI 266
Cdd:PRK11866  241 FYKEE-KPTYEEELDEIL 257
PorB_KorB TIGR02177
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ...
 18-202 3.67e-63

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: 199.99  E-value: 3.67e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  18 WCWGCGDGVILKSVIRAIDKMGWDMNDVCIVSGIGCSGRFSSYIDCNTVHTTHGRAIAYATGIKLANPEKHVIVVTGDGD 97
Cdd:TIGR02177   3 WCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGDGD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  98 GLAIGGNHTIHGCRRNIDLNHILINNFIYGLTNSQTSPTTPQGFWTATANYGNVDPTFDAAKLADAAGATFVARESVLDP 177
Cdd:TIGR02177  83 LYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSGDV 162

                         170       180
                  ....*....|....*....|....*
gi 1063808819 178 QKLEKIFVAGFTHKGYSFFDVFSNC 202
Cdd:TIGR02177 163 AHLKEIIKEAINHKGYALVDILQPC 187
Oxoac_fdxbeta_Archa NF041171
2-oxoacid:ferredoxin oxidoreductase subunit beta;
18-253 2.34e-59

2-oxoacid:ferredoxin oxidoreductase subunit beta;


Pssm-ID: 469082 [Multi-domain]  Cd Length: 296  Bit Score: 190.53  E-value: 2.34e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  18 WCWGCGDGVILKSVIRAIDKMGWDMNDVCIVSGIGCSGRFSSYIDCNTVHTTHGRAIAYATGIKLANPEKHVIVVTGDGD 97
Cdd:NF041171    5 WCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGDGD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  98 GLAIGGNHTIHGCRRNIDLNHILINNFIYGLTNSQTSPTTPQGFWTATANYGNVDPTFDAAKLADAAGATFVARESVLDP 177
Cdd:NF041171   85 LLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAYDV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819 178 QKLEKIFVAGFTHKGYSFFDVFSNC----HINlgrknkmgeavqNLEWIENRIVgknKFE--------LLSAEERVDKFP 245
Cdd:NF041171  165 KHLKELIKAAIKHKGLAFIDVLQPCptynDIN------------TKEWYDKRVY---KLDdepgwdpvVRSPEEADEKMA 229


                  ....*...
gi 1063808819 246 TGILKQEE 253
Cdd:NF041171  230 KAIEKALE 237
PRK11869 PRK11869
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 10-249 2.48e-54

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183349 [Multi-domain]  Cd Length: 280  Bit Score: 177.28  E-value: 2.48e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  10 RVDKMPTLWCWGCGDGVILKSVIRAIDKMGWDMNDVCIVSGIGCSGRFSSYIDCNTVHTTHGRAIAYATGIKLANPEKHV 89
Cdd:PRK11869    2 RPEKYDIAWCPGCGNFGIRNALMKALSELNLKPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  90 IVVTGDGDGLAIGGNHTIHGCRRNIDLNHILINNFIYGLTNSQTSPTTPQGFWTATANYGNVDPTFDAAKLADAAGATFV 169
Cdd:PRK11869   82 IAEGGDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASFV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819 170 ARESVLDPQKLEKIFVAGFTHKGYSFFDVFSNChINLGRKNKMGEAVQNLEWIENRIVGKNKFELLSAEErVDKFPTGIL 249
Cdd:PRK11869  162 ARTFSGDIEETKEILKEAIKHKGLAIVDIFQPC-VSFNKVNTYQWYRENTYYLKDHDPTDRELAFKRALE-TEKLPLGIF 239
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
50-198 4.51e-29

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 107.67  E-value: 4.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  50 GIGCSGRFS----------SYIDcNTVHTTHGRAIAYATGIKLANPEKHVIVVTGDGDGLAIgGNHTIHGCRRNIDLNHI 119
Cdd:pfam02775   1 DIGCHQMWAaqyyrfrpprRYLT-SGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMN-LQELATAVRYNLPITVV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819 120 LINNFIYGLTNSQtspTTPQGFWTATANYGNVDPTFDaakladaagatFVA--------RESVLDPQKLEKIFVAGFTHK 191
Cdd:pfam02775  79 VLNNGGYGMTRGQ---QTPFGGGRYSGPSGKILPPVD-----------FAKlaeaygakGARVESPEELEEALKEALEHD 144


                  ....*..
gi 1063808819 192 GYSFFDV 198
Cdd:pfam02775 145 GPALIDV 151
TPP_PFOR cd02018
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ...
 19-207 4.08e-15

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: 72.90  E-value: 4.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  19 CWGCGDGVILKSVIRAIDKMGwdmnDVCIVSGIGCSGRFSSYIDCN-----TVHTTHGRAIAYATGIKLA---------- 83
Cdd:cd02018     8 CAGCGEVTAVRVVLAALPAPE----DTVIANSTGCSSVYASTAPFNswavpWVNSLFEDANAVASGLKRGlkarfpkdre 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  84 -NPEKHVIVVTGDGDGLAIGGNHTIHGCRRNIDLNHILINNFIYGLTNSQTSPTTPQGFWTATANYGNVDPTFDAAKLAD 162
Cdd:cd02018    84 lDKKKDVVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKKDLVLIAA 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1063808819 163 AAGATFVARESVLDPQKLEKIFVAGFT-HKGYSFFDVFSNCHINLG 207
Cdd:cd02018   164 THGCVYVARLSPALKKHFLKVVKEAISrTDGPTFIHAYTPCITEWG 209
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 31-132 3.48e-11

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: 60.35  E-value: 3.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  31 VIRAIDKMGwdMNDVCIVSGIGCSG----RFSSYIDCNTVHT-----THGRAIAYATGIKLANPEKHVIVVTGDGdGLAI 101
Cdd:cd00568     2 VLAALRAAL--PEDAIVVNDAGNSAywayRYLPLRRGRRFLTstgfgAMGYGLPAAIGAALAAPDRPVVCIAGDG-GFMM 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1063808819 102 GGNHTIHGCRRNIDLNHILINNFIYGLTNSQ 132
Cdd:cd00568    79 TGQELATAVRYGLPVIVVVFNNGGYGTIRMH 109
TPP_PFOR_porB_like cd03376
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ...
 19-149 4.29e-09

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: 55.71  E-value: 4.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  19 CWGCGDGVILKSVIRAIDKmgwdmnDVCIVSGIGCSGRFSS-Y----IDCNTVHTTHGRAIAYATGIK-----LANPEK- 87
Cdd:cd03376     8 CAGCGAALALRHVLKALGP------DTVVVNPTGCLEVITTpYpytaWRVPWIHVAFENAAAVASGIEaalkaLGRGKDi 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063808819  88 HVIVVTGDGDGLAIGGNHTIHGCRRNIDLNHILINNFIYGLTNSQTSPTTPQGFWTATANYG 149
Cdd:cd03376    82 TVVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTTPVG 143
PRK11864 PRK11864
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
19-202 1.11e-06

3-methyl-2-oxobutanoate dehydrogenase subunit beta;


Pssm-ID: 237005 [Multi-domain]  Cd Length: 300  Bit Score: 48.93  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  19 CWGCGDGVILKSVIRAIDKmgwdmNDVCIVSGiGCS----GRFS-SYIDCNTVHTTHGRAIAYATGIKLA---NPEKHVI 90
Cdd:PRK11864   21 CPGCGAPLGLRYLLKALGE-----KTVLVIPA-SCStviqGDTPkSPLTVPVLHTAFAATAAVASGIEEAlkaRGEKGVI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  91 VVT--GDGdGLAIGGNHTIHG-CRRNIDLNHILINNFIYGLTNSQTSPTTPQGFWTATANYGNVDPTFDAAKLADAAGAT 167
Cdd:PRK11864   95 VVGwaGDG-GTADIGFQALSGaAERNHDILYIMYDNEAYMNTGIQRSSSTPYGAWTTTTPGGKREHKKPVPDIMAAHKVP 173

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063808819 168 FVARESVLDPQKLEKIFVAGFTHKGYSFFDVFSNC 202
Cdd:PRK11864  174 YVATASIAYPEDFIRKLKKAKEIRGFKFIHLLAPC 208
TPP_ComE_PpyrDC cd02001
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ...
 32-148 4.79e-06

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: 45.56  E-value: 4.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  32 IRAIDKMGWDMNDVCIVSGIGCSGRFSSYIDCNTVH----TTHGRAIAYATGIKLANPEKhVIVVTGDGD------GLAI 101
Cdd:cd02001     2 IAAIAEIIEASGDTPIVSTTGYASRELYDVQDRDGHfymlGSMGLAGSIGLGLALGLSRK-VIVVDGDGSllmnpgVLLT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1063808819 102 GGNHTihgcrrNIDLNHILINNFIYGLTNSQTSPT--TPQGFWTATANY 148
Cdd:cd02001    81 AGEFT------PLNLILVVLDNRAYGSTGGQPTPSsnVNLEAWAAACGY 123
PRK11865 PRK11865
pyruvate synthase subunit beta;
19-151 1.53e-05

pyruvate synthase subunit beta;


Pssm-ID: 183346 [Multi-domain]  Cd Length: 299  Bit Score: 45.47  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  19 CWGCGDGVILKSVIRAIDKmgwdmnDVCIVSGIGCSGRFSSYIDCNT-----VHTTHGRAIAYATGIKLA----NPEKHV 89
Cdd:PRK11865   21 CAGCGAAIAMRLALKALGK------NTVIVVATGCLEVITTPYPETAwnvpwIHVAFENAAAVASGIERAvkalGKKVNV 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063808819  90 IVVTGDGDGLAIGGNHTIHGCRRNIDLNHILINNFIYGLTNSQTSPTTPQGFWTATANYGNV 151
Cdd:PRK11865   95 VAIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKY 156
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
 73-127 3.42e-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: 3.42e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063808819  73 AIAYATGIKLANPEKHVIVVTGDGdGLAIGGN--HTIhgCRRNIDLNHILINNFIYG 127
Cdd:COG0028   417 GLPAAIGAKLARPDRPVVAITGDG-GFQMNLQelATA--VRYGLPVKVVVLNNGGLG 470
TPP_PpyrDC cd03371
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ...
 71-137 5.22e-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: 43.07  E-value: 5.22e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  71 GRAIAYATGIKLANPEKHVIVVtgDGDGLAI---GGNHTIHGCRRNiDLNHILINNFIYGLTNSQtsPTT 137
Cdd:cd03371    51 GHASQIALGIALARPDRKVVCI--DGDGAALmhmGGLATIGGLAPA-NLIHIVLNNGAHDSVGGQ--PTV 115
TPP_ComE cd03372
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ...
 32-147 1.08e-04

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: 41.89  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  32 IRAIDKMGWDMNDVCIVSGIGCSGRFSSYIDCNTVH----TTHGRAIAYATGIKLANPEKhVIVVTGDGDGL-AIGGNHT 106
Cdd:cd03372     2 RDAIKTLIADLKDELVVSNIGFPSKELYAAGDRPLNfymlGSMGLASSIGLGLALAQPRK-VIVIDGDGSLLmNLGALAT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1063808819 107 IhGCRRNIDLNHILINNFIYGLTNSQTSPTTPQGFWTATAN 147
Cdd:cd03372    81 I-AAEKPKNLIIVVLDNGAYGSTGNQPTHAGKKTDLEAVAK 120
PRK06163 PRK06163
hypothetical protein; Provisional
 71-136 1.53e-04

hypothetical protein; Provisional


Pssm-ID: 235721 [Multi-domain]  Cd Length: 202  Bit Score: 41.74  E-value: 1.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063808819  71 GRAIAYATGIKLANPEKHVIVVTGDGDGL-AIGGNHTIHGCRRNiDLNHILINNFIYGLTNSQTSPT 136
Cdd:PRK06163   60 GLAFPIALGVALAQPKRRVIALEGDGSLLmQLGALGTIAALAPK-NLTIIVMDNGVYQITGGQPTLT 125
TPP_BFDC cd02002
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ...
 71-123 2.66e-04

Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.


Pssm-ID: 238960 [Multi-domain]  Cd Length: 178  Bit Score: 40.66  E-value: 2.66e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063808819  71 GRAIAYATGIKLANPEKHVIVVTGDGDglaigGNHTIHG----CRRNIDLNHILINN 123
Cdd:cd02002    52 GWGLPAAVGAALANPDRKVVAIIGDGS-----FMYTIQAlwtaARYGLPVTVVILNN 103
TPP_ALS cd02010
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ...
 67-152 3.31e-04

Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; composed of proteins similar to Klebsiella pneumoniae ALS, a catabolic enzyme required for butanediol fermentation. ALS catalyzes the conversion of 2 molecules of pyruvate to acetolactate and carbon dioxide. ALS does not contain FAD, and requires TPP and a divalent metal cation for activity.


Pssm-ID: 238968 [Multi-domain]  Cd Length: 177  Bit Score: 40.35  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  67 HTTHGRAIAYATGIKLANPEKHVIVVTGDGdGLAIGGNHTIHGCRRNIDLNHILINNFIYGLTNSQTSpttPQGFWTATA 146
Cdd:cd02010    47 LATMGVALPGAIGAKLVYPDRKVVAVSGDG-GFMMNSQELETAVRLKIPLVVLIWNDNGYGLIKWKQE---KEYGRDSGV 122


                  ....*.
gi 1063808819 147 NYGNVD 152
Cdd:cd02010   123 DFGNPD 128
TPP_Gcl cd02006
Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins ...
 44-128 3.54e-04

Thiamine pyrophosphate (TPP) family, Gcl subfamily, TPP-binding module; composed of proteins similar to Escherichia coli glyoxylate carboligase (Gcl). E. coli glyoxylate carboligase, plays a key role in glyoxylate metabolism where it catalyzes the condensation of two molecules of glyoxylate to give tartronic semialdehyde and carbon dioxide. This enzyme requires TPP, magnesium ion and FAD as cofactors.


Pssm-ID: 238964 [Multi-domain]  Cd Length: 202  Bit Score: 40.73  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  44 DVCIVSGIGCSG----------RFSSYIDCNTVHTThGRAIAYATGIKLANPEKHVIVVTGDGD------GLAIGGNHti 107
Cdd:cd02006    24 DVRYVTTIGLSQiagaqmlhvyKPRHWINCGQAGPL-GWTVPAALGVAAADPDRQVVALSGDYDfqfmieELAVGAQH-- 100

                          90       100
                  ....*....|....*....|.
gi 1063808819 108 hgcrrNIDLNHILINNFIYGL 128
Cdd:cd02006   101 -----RIPYIHVLVNNAYLGL 116
TPP_BZL_OCoD_HPCL cd02004
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ...
 76-139 5.24e-04

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: 39.82  E-value: 5.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063808819  76 YATGIKLANPEKHVIVVTGDGdglAIGgnhtIHG------CRRNIDLNHILINNF-IYGLTNSQTSPTTPQ 139
Cdd:cd02004    56 YAIAAALARPDKRVVLVEGDG---AFG----FSGmeletaVRYNLPIVVVVGNNGgWYQGLDGQQLSYGLG 119
TPP_IOR_alpha cd02008
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ...
 15-140 2.26e-03

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: 38.03  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  15 PTLwCWGCGDgvilKSVIRAIDKMGWDmnDVCIVSGIGCSGrFSSYIDCNTVHTT--HGRAIAYATGIKLANPEKHVIVV 92
Cdd:cd02008     4 PGL-CPGCPH----RPSFYALRKAFKK--DSIVSGDIGCYT-LGALPPLNAIDTCtcMGASIGVAIGMAKASEDKKVVAV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063808819  93 TGDG-----------DGLAIGGNHTIhgcrrnidlnhILINNFIYGLTNSQTSPTTPQG 140
Cdd:cd02008    76 IGDStffhsgilgliNAVYNKANITV-----------VILDNRTTAMTGGQPHPGTGKT 123
PRK06965 PRK06965
acetolactate synthase 3 catalytic subunit; Validated
 69-96 4.16e-03

acetolactate synthase 3 catalytic subunit; Validated


Pssm-ID: 180780 [Multi-domain]  Cd Length: 587  Bit Score: 38.25  E-value: 4.16e-03
                          10        20
                  ....*....|....*....|....*...
gi 1063808819  69 THGRAIAYATGIKLANPEKHVIVVTGDG 96
Cdd:PRK06965  438 TMGVGLPYAMGIKMAHPDDDVVCITGEG 465
PRK07282 PRK07282
acetolactate synthase large subunit;
69-96 7.57e-03

acetolactate synthase large subunit;


Pssm-ID: 180919 [Multi-domain]  Cd Length: 566  Bit Score: 37.49  E-value: 7.57e-03
                          10        20
                  ....*....|....*....|....*...
gi 1063808819  69 THGRAIAYATGIKLANPEKHVIVVTGDG 96
Cdd:PRK07282  419 TMGFGIPAAIGAKIANPDKEVILFVGDG 446
PRK06112 PRK06112
acetolactate synthase catalytic subunit; Validated
 71-152 7.86e-03

acetolactate synthase catalytic subunit; Validated


Pssm-ID: 235700 [Multi-domain]  Cd Length: 578  Bit Score: 37.43  E-value: 7.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063808819  71 GRAIAYATGIKLANPEKHVIVVTGDGdglaiGGNHT---IHGCRR-NIDLNHILINNFIYGLtnSQTSPTTPQGFWTATA 146
Cdd:PRK06112  440 GWGVPMAIGAKVARPGAPVICLVGDG-----GFAHVwaeLETARRmGVPVTIVVLNNGILGF--QKHAETVKFGTHTDAC 512


                  ....*.
gi 1063808819 147 NYGNVD 152
Cdd:PRK06112  513 HFAAVD 518
PRK06154 PRK06154
thiamine pyrophosphate-requiring protein;
68-127 9.76e-03

thiamine pyrophosphate-requiring protein;


Pssm-ID: 235718 [Multi-domain]  Cd Length: 565  Bit Score: 37.10  E-value: 9.76e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063808819  68 TTH-GRAIAYATGIKLANPEKHVIVVTGDGdglAIG--GNHTIHGCRRNIDLNHILINNFIYG 127
Cdd:PRK06154  430 TTQlGYGLGLAMGAKLARPDALVINLWGDA---AFGmtGMDFETAVRERIPILTILLNNFSMG 489
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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