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Conserved domains on  [gi|1917892507|gb|QOP41302|]
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2-oxoglutarate ferredoxin oxidoreductase subunit beta [Sulfurimonas marina]

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: 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
 
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
 
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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