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Conserved domains on  [gi|1566304881|gb|QAY65666|]
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2-oxoacid:ferredoxin oxidoreductase subunit beta [Paenibacillus protaetiae]

Protein Classification

2-oxoacid:ferredoxin oxidoreductase subunit beta( domain architecture ID 11485631)

2-oxoacid:ferredoxin oxidoreductase subunit beta is a component of KG oxidoreductase (KOR) that catalyzes the CoA-dependent oxidative decarboxylation of 2-oxoglutarate (alpha-ketoglutarate, KG) to succinyl-CoA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 1-283 6.07e-173

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


:

Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 479.34  E-value: 6.07e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881   1 MATFKDFRNNVKPNWCPGCGDFSIQAAIQRAAANVGLEPEQLAVISGIGCSGRISGYINAYGLHGIHGRALPIAQGVKLA 80
Cdd:PRK11867    5 MLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGLKLA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  81 NRELTVIASGGDGDGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQTSPRSAEGFVTKSTPEGSIESTLSPLEIAMS 160
Cdd:PRK11867   85 NPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVELALG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881 161 AGATFVAQSFSSDLKQLTALIEAGIKHEGFSLINVFSPCVTFNKINTYDWFKERVVNLEQFPDYDATNRIAAMNKIMETE 240
Cdd:PRK11867  165 AGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFNNVNTFDWFKERLVKVHDAEGYDPTNALAAMKTLEEGD 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1566304881 241 GMLTGLIYQNtERKSYEDMIPGFQPEALAKQDLALSQDQFDSL 283
Cdd:PRK11867  245 PIPTGIFYQV-ERPTYEEAVRAQIEGPLALQDLLMGGDTWTVL 286
 
Name Accession Description Interval E-value
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 1-283 6.07e-173

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 479.34  E-value: 6.07e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881   1 MATFKDFRNNVKPNWCPGCGDFSIQAAIQRAAANVGLEPEQLAVISGIGCSGRISGYINAYGLHGIHGRALPIAQGVKLA 80
Cdd:PRK11867    5 MLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGLKLA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  81 NRELTVIASGGDGDGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQTSPRSAEGFVTKSTPEGSIESTLSPLEIAMS 160
Cdd:PRK11867   85 NPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVELALG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881 161 AGATFVAQSFSSDLKQLTALIEAGIKHEGFSLINVFSPCVTFNKINTYDWFKERVVNLEQFPDYDATNRIAAMNKIMETE 240
Cdd:PRK11867  165 AGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFNNVNTFDWFKERLVKVHDAEGYDPTNALAAMKTLEEGD 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1566304881 241 GMLTGLIYQNtERKSYEDMIPGFQPEALAKQDLALSQDQFDSL 283
Cdd:PRK11867  245 PIPTGIFYQV-ERPTYEEAVRAQIEGPLALQDLLMGGDTWTVL 286
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 3-267 2.51e-116

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: 334.81  E-value: 2.51e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881   3 TFKDFRNNVKPNWCPGCGDFSIQAAIQRAAANVgLEPEQLAVISGIGCSGRISGYINAYGLHGIHGRALPIAQGVKLANR 82
Cdd:COG1013     3 KKKDLLRTPGHRWCPGCGHGIILRLLLKALDEL-LDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  83 ELTVIASGGDGDGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQTSPRSAEGFVTKSTPEGSIESTLSPLEIAMSAG 162
Cdd:COG1013    82 DLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881 163 ATFVAQSFSSDLKQLTALIEAGIKHEGFSLINVFSPCVTFNKIN---TYDWFKERVVNLEqfpDYDATnriAAMNKIMET 239
Cdd:COG1013   162 ATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRDpskTIEWAKEGMWPLY---EYDPG---EKLRLTYEP 235

                         250       260
                  ....*....|....*....|....*....
gi 1566304881 240 EG-MLTGLIYQNTERksYEDMIPGFQPEA 267
Cdd:COG1013   236 KDkIPVGEFLKNQGR--FEELIEEIQKPV 262
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 15-202 1.02e-114

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: 328.33  E-value: 1.02e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  15 WCPGCGDFSIQAAIQRAAANVGLEPEQLAVISGIGCSGRISGYINAYGLHGIHGRALPIAQGVKLANRELTVIASGGDGD 94
Cdd:cd03375     1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  95 GFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQTSPRSAEGFVTKSTPEGSIESTLSPLEIAMSAGATFVAQSFSSDL 174
Cdd:cd03375    81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160

                         170       180
                  ....*....|....*....|....*...
gi 1566304881 175 KQLTALIEAGIKHEGFSLINVFSPCVTF 202
Cdd:cd03375   161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
PorB_KorB TIGR02177
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ...
 13-286 1.74e-110

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: 320.94  E-value: 1.74e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  13 PNWCPGCGDFSIQAAIQRAAANVGLEPEQLAVISGIGCSGRISGYINAYGLHGIHGRALPIAQGVKLANRELTVIASGGD 92
Cdd:TIGR02177   1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  93 GDGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQTSPRSAEGFVTKSTPEGSIESTLSPLEIAMSAGATFVAQSFSS 172
Cdd:TIGR02177  81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881 173 DLKQLTALIEAGIKHEGFSLINVFSPCVTFNKINTYDWFKERVVNLEQfPDYDATNR---------IAAMNKIMETEGML 243
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNKINTYEWYRERVYKLDE-EGYDPIVRepeefeekaAAAIKKAMEWGDRI 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1566304881 244 -TGLIYQNTERKSYED----MIPGFQPEALAKQDLALSQDQFDSLLAE 286
Cdd:TIGR02177 240 pIGIFYKNENKPTFEErlekILPRYMSAPPAEQEIKPPIEKPKELLEE 287
Oxoac_fdxbeta_Archa NF041171
2-oxoacid:ferredoxin oxidoreductase subunit beta;
13-273 1.30e-98

2-oxoacid:ferredoxin oxidoreductase subunit beta;


Pssm-ID: 469082 [Multi-domain]  Cd Length: 296  Bit Score: 291.07  E-value: 1.30e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  13 PNWCPGCGDFSIQAAIQRAAANVGLEPEQLAVISGIGCSGRISGYINAYGLHGIHGRALPIAQGVKLANRELTVIASGGD 92
Cdd:NF041171    3 VDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  93 GDGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQTSPRSAEGFVTKSTPEGSIESTLSPLEIAMSAGATFVAQSFSS 172
Cdd:NF041171   83 GDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881 173 DLKQLTALIEAGIKHEGFSLINVFSPCVTFNKINTYDWFKERVVNLEQFPDYD--------ATNRIA-AMNKIME-TEGM 242
Cdd:NF041171  163 DVKHLKELIKAAIKHKGLAFIDVLQPCPTYNDINTKEWYDKRVYKLDDEPGWDpvvrspeeADEKMAkAIEKALEwGDRI 242

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1566304881 243 LTGLIYQNTERKSYEDMIPGFQPEAL----AKQDL 273
Cdd:NF041171  243 PIGIFYQNELVPTFEERIAERLPNYLdnppAKQPI 277
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
47-195 2.21e-38

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 132.32  E-value: 2.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  47 GIGCSG----------RISGYINAYGlHGIHGRALPIAQGVKLANRELTVIASGGDGDGFAIGMgHTIHAIRRNLNITYI 116
Cdd:pfam02775   1 DIGCHQmwaaqyyrfrPPRRYLTSGG-LGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQ-ELATAVRYNLPITVV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1566304881 117 VMDNQIYGLTKGQTSPRsaeGFVTKSTPEGSIESTLSPLEIAMSAGATFVaqsFSSDLKQLTALIEAGIKHEGFSLINV 195
Cdd:pfam02775  79 VLNNGGYGMTRGQQTPF---GGGRYSGPSGKILPPVDFAKLAEAYGAKGA---RVESPEELEEALKEALEHDGPALIDV 151
 
Name Accession Description Interval E-value
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 1-283 6.07e-173

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 479.34  E-value: 6.07e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881   1 MATFKDFRNNVKPNWCPGCGDFSIQAAIQRAAANVGLEPEQLAVISGIGCSGRISGYINAYGLHGIHGRALPIAQGVKLA 80
Cdd:PRK11867    5 MLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGLKLA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  81 NRELTVIASGGDGDGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQTSPRSAEGFVTKSTPEGSIESTLSPLEIAMS 160
Cdd:PRK11867   85 NPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVELALG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881 161 AGATFVAQSFSSDLKQLTALIEAGIKHEGFSLINVFSPCVTFNKINTYDWFKERVVNLEQFPDYDATNRIAAMNKIMETE 240
Cdd:PRK11867  165 AGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFNNVNTFDWFKERLVKVHDAEGYDPTNALAAMKTLEEGD 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1566304881 241 GMLTGLIYQNtERKSYEDMIPGFQPEALAKQDLALSQDQFDSL 283
Cdd:PRK11867  245 PIPTGIFYQV-ERPTYEEAVRAQIEGPLALQDLLMGGDTWTVL 286
PRK05778 PRK05778
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
 4-275 1.42e-131

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated


Pssm-ID: 235604 [Multi-domain]  Cd Length: 301  Bit Score: 374.99  E-value: 1.42e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881   4 FKDFRNNVKPN-WCPGCGDFSIQAAIQRAAANVGLEPEQLAVISGIGCSGRISGYINAYGLHGIHGRALPIAQGVKLANR 82
Cdd:PRK05778    8 LTYLRYDGLPTtWCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLANP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  83 ELTVIASGGDGDGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQTSPRSAEGFVTKSTPEGSIESTLSPLEIAMSAG 162
Cdd:PRK05778   88 DLEVIVVGGDGDLASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAAG 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881 163 ATFVAQSFSSDLKQLTALIEAGIKHEGFSLINVFSPCVTFNKINTYD--------WFKERVVNLEQFPDYDATNRIAAMN 234
Cdd:PRK05778  168 ATFVARSFAGDVKQLVELIKKAISHKGFAFIDVLSPCVTFNGRNTSTkspaymreYYKKRVYKLKLEEDYDPTDRDKAAE 247

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1566304881 235 KIMETEG---MLTGLIYQNtERKSYEDMIPGFQPEALAKQDLAL 275
Cdd:PRK05778  248 KMLEEELggkIPIGVFYKN-ERPTFEERLEKLIEPLLELPPAAL 290
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 3-267 2.51e-116

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: 334.81  E-value: 2.51e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881   3 TFKDFRNNVKPNWCPGCGDFSIQAAIQRAAANVgLEPEQLAVISGIGCSGRISGYINAYGLHGIHGRALPIAQGVKLANR 82
Cdd:COG1013     3 KKKDLLRTPGHRWCPGCGHGIILRLLLKALDEL-LDGDKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  83 ELTVIASGGDGDGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQTSPRSAEGFVTKSTPEGSIESTLSPLEIAMSAG 162
Cdd:COG1013    82 DLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881 163 ATFVAQSFSSDLKQLTALIEAGIKHEGFSLINVFSPCVTFNKIN---TYDWFKERVVNLEqfpDYDATnriAAMNKIMET 239
Cdd:COG1013   162 ATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRDpskTIEWAKEGMWPLY---EYDPG---EKLRLTYEP 235

                         250       260
                  ....*....|....*....|....*....
gi 1566304881 240 EG-MLTGLIYQNTERksYEDMIPGFQPEA 267
Cdd:COG1013   236 KDkIPVGEFLKNQGR--FEELIEEIQKPV 262
PRK11866 PRK11866
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 7-273 6.10e-116

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183347 [Multi-domain]  Cd Length: 279  Bit Score: 334.80  E-value: 6.10e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881   7 FRNNVKPNWCPGCGDFSIQAAIQRAAANVGLEPEQLAVISGIGCSGRISGYINAYGLHGIHGRALPIAQGVKLANRELTV 86
Cdd:PRK11866    1 YAVKRPPIWCPGCGNYGILEALRKALAELGIPPENVVVVSGIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  87 IASGGDGDGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQTSPRSAEGFVTKSTPEGSIESTLSPLEIAMSAGATFV 166
Cdd:PRK11866   81 IGYGGDGDGYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATFV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881 167 AQSFSSDLKQLTALIEAGIKHEGFSLINVFSPCVTFNKINTYDWFKERVVNLEQfPDYDATNRIAAMNKIMETEGML-TG 245
Cdd:PRK11866  161 ARGFSGDVKHLKEIIKEAIKHKGFSFIDVLSPCVTFNKLNTYDWFRPRVYKLEE-TGHDPTNFEQAYKKALEWGDRIpIG 239

                         250       260
                  ....*....|....*....|....*....
gi 1566304881 246 LIYQnTERKSYED-MIPGFQPEALAKQDL 273
Cdd:PRK11866  240 VFYK-EEKPTYEEeLDEILKNPPLADQPL 267
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 15-202 1.02e-114

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: 328.33  E-value: 1.02e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  15 WCPGCGDFSIQAAIQRAAANVGLEPEQLAVISGIGCSGRISGYINAYGLHGIHGRALPIAQGVKLANRELTVIASGGDGD 94
Cdd:cd03375     1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  95 GFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQTSPRSAEGFVTKSTPEGSIESTLSPLEIAMSAGATFVAQSFSSDL 174
Cdd:cd03375    81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160

                         170       180
                  ....*....|....*....|....*...
gi 1566304881 175 KQLTALIEAGIKHEGFSLINVFSPCVTF 202
Cdd:cd03375   161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
PorB_KorB TIGR02177
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ...
 13-286 1.74e-110

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: 320.94  E-value: 1.74e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  13 PNWCPGCGDFSIQAAIQRAAANVGLEPEQLAVISGIGCSGRISGYINAYGLHGIHGRALPIAQGVKLANRELTVIASGGD 92
Cdd:TIGR02177   1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  93 GDGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQTSPRSAEGFVTKSTPEGSIESTLSPLEIAMSAGATFVAQSFSS 172
Cdd:TIGR02177  81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881 173 DLKQLTALIEAGIKHEGFSLINVFSPCVTFNKINTYDWFKERVVNLEQfPDYDATNR---------IAAMNKIMETEGML 243
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNKINTYEWYRERVYKLDE-EGYDPIVRepeefeekaAAAIKKAMEWGDRI 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1566304881 244 -TGLIYQNTERKSYED----MIPGFQPEALAKQDLALSQDQFDSLLAE 286
Cdd:TIGR02177 240 pIGIFYKNENKPTFEErlekILPRYMSAPPAEQEIKPPIEKPKELLEE 287
Oxoac_fdxbeta_Archa NF041171
2-oxoacid:ferredoxin oxidoreductase subunit beta;
13-273 1.30e-98

2-oxoacid:ferredoxin oxidoreductase subunit beta;


Pssm-ID: 469082 [Multi-domain]  Cd Length: 296  Bit Score: 291.07  E-value: 1.30e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  13 PNWCPGCGDFSIQAAIQRAAANVGLEPEQLAVISGIGCSGRISGYINAYGLHGIHGRALPIAQGVKLANRELTVIASGGD 92
Cdd:NF041171    3 VDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  93 GDGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQTSPRSAEGFVTKSTPEGSIESTLSPLEIAMSAGATFVAQSFSS 172
Cdd:NF041171   83 GDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881 173 DLKQLTALIEAGIKHEGFSLINVFSPCVTFNKINTYDWFKERVVNLEQFPDYD--------ATNRIA-AMNKIME-TEGM 242
Cdd:NF041171  163 DVKHLKELIKAAIKHKGLAFIDVLQPCPTYNDINTKEWYDKRVYKLDDEPGWDpvvrspeeADEKMAkAIEKALEwGDRI 242

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1566304881 243 LTGLIYQNTERKSYEDMIPGFQPEAL----AKQDL 273
Cdd:NF041171  243 PIGIFYQNELVPTFEERIAERLPNYLdnppAKQPI 277
PRK11869 PRK11869
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 15-267 2.34e-93

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183349 [Multi-domain]  Cd Length: 280  Bit Score: 277.43  E-value: 2.34e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  15 WCPGCGDFSIQAAIQRAAANVGLEPEQLAVISGIGCSGRISGYINAYGLHGIHGRALPIAQGVKLANRELTVIASGGDGD 94
Cdd:PRK11869   10 WCPGCGNFGIRNALMKALSELNLKPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTVIAEGGDGD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  95 GFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQTSPRSAEGFVTKSTPEGSIESTLSPLEIAMSAGATFVAQSFSSDL 174
Cdd:PRK11869   90 MYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASFVARTFSGDI 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881 175 KQLTALIEAGIKHEGFSLINVFSPCVTFNKINTYDWFKERVVNLEqfpDYDATNRIAAMNKIMETEGMLTGLIYQNtERK 254
Cdd:PRK11869  170 EETKEILKEAIKHKGLAIVDIFQPCVSFNKVNTYQWYRENTYYLK---DHDPTDRELAFKRALETEKLPLGIFYIN-EKP 245

                         250
                  ....*....|...
gi 1566304881 255 SYEDMIPGFQPEA 267
Cdd:PRK11869  246 TFEELVPAYKGDK 258
oorB PRK09628
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
15-275 8.27e-64

2-oxoglutarate ferredoxin oxidoreductase subunit beta;


Pssm-ID: 182003 [Multi-domain]  Cd Length: 277  Bit Score: 201.88  E-value: 8.27e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  15 WCPGCGDFSIQAAIQRAAANVGLEPEQLAVISGIGCSGRISGYINAYGLHGIHGRALPIAQGVKLANRELTVIASGGDGD 94
Cdd:PRK09628   18 WCWGCGDGVILKSIIRAIDKLGWNMDDVCVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGIKLANPDKHVIVVSGDGD 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  95 GFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQTSPRSAEGFVTKSTPEGSIESTLSPLEIAMSAGATFVAQSFSSDL 174
Cdd:PRK09628   98 GLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKLATAAGASFVARESVIDP 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881 175 KQLTALIEAGIKHEGFSLINVFSPC-VTFNKIN-------TYDWFKERVVNLEQFPDYDATNRIAAMNkimetegmlTGL 246
Cdd:PRK09628  178 QKLEKLLVKGFSHKGFSFFDVFSNChINLGRKNkmgeavqMLKWIESRTVSKRKFDALSPEERVGKFP---------TGI 248

                         250       260
                  ....*....|....*....|....*....
gi 1566304881 247 IYQNTERKSYEDMIPGFQPEALAKQDLAL 275
Cdd:PRK09628  249 LKHDTDRKEYCEAYEEVIEAAQGKQKVDL 277
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
47-195 2.21e-38

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 132.32  E-value: 2.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  47 GIGCSG----------RISGYINAYGlHGIHGRALPIAQGVKLANRELTVIASGGDGDGFAIGMgHTIHAIRRNLNITYI 116
Cdd:pfam02775   1 DIGCHQmwaaqyyrfrPPRRYLTSGG-LGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNLQ-ELATAVRYNLPITVV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1566304881 117 VMDNQIYGLTKGQTSPRsaeGFVTKSTPEGSIESTLSPLEIAMSAGATFVaqsFSSDLKQLTALIEAGIKHEGFSLINV 195
Cdd:pfam02775  79 VLNNGGYGMTRGQQTPF---GGGRYSGPSGKILPPVDFAKLAEAYGAKGA---RVESPEELEEALKEALEHDGPALIDV 151
PFO_beta_C pfam12367
Pyruvate ferredoxin oxidoreductase beta subunit C terminal; This domain family is found in ...
 199-262 3.57e-27

Pyruvate ferredoxin oxidoreductase beta subunit C terminal; This domain family is found in bacteria and archaea, and is approximately 70 amino acids in length. The family is found in association with pfam02775. There are two completely conserved residues (A and G) that may be functionally important. PFO is involved in carbon dioxide fixation via a reductive TCA cycle. It forms a heterodimer (alpha/beta). The beta subunit has binding motifs for Fe-S clusters and thiamine pyrophosphate.


Pssm-ID: 463551 [Multi-domain]  Cd Length: 62  Bit Score: 100.26  E-value: 3.57e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1566304881 199 CVTFNKINTYDWFKERVVNLEQfpDYDATNRIAAMNKIME-TEGMLTGLIYQNtERKSYEDMIPG 262
Cdd:pfam12367   1 CVTFNKVNTYDWYKERVYKLDE--DHDPTDREAAMEKALEwGDRIPIGIFYKE-ERPTFEERLPV 62
TPP_PFOR cd02018
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ...
 16-207 2.62e-26

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: 103.33  E-value: 2.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  16 CPGCGDFSIQAAIQRAAANvglePEQLAVISGIGCSGRISGYI--NAYGLHGIH---GRALPIAQGVKLA-------NRE 83
Cdd:cd02018     8 CAGCGEVTAVRVVLAALPA----PEDTVIANSTGCSSVYASTApfNSWAVPWVNslfEDANAVASGLKRGlkarfpkDRE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  84 L----TVIASGGDGDGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQTSPRSAEGFVTKSTPEGSIESTLSPLEIAM 159
Cdd:cd02018    84 LdkkkDVVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKKDLVLIAA 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1566304881 160 SAGATFVAQ-SFSSDLKQLTALIEAGIKHEGFSLINVFSPCVTFNKINT 207
Cdd:cd02018   164 THGCVYVARlSPALKKHFLKVVKEAISRTDGPTFIHAYTPCITEWGIGS 212
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 44-195 8.43e-16

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: 73.44  E-value: 8.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  44 VISGIGCSGRISGYI---------NAYGLHGIHGRALPIAQGVKLANRELTVIASGGDGdGFAIGMGHTIHAIRRNLNIT 114
Cdd:cd00568    16 VVNDAGNSAYWAYRYlplrrgrrfLTSTGFGAMGYGLPAAIGAALAAPDRPVVCIAGDG-GFMMTGQELATAVRYGLPVI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881 115 YIVMDNQIYGLTKGQTSPRsaegfvTKSTPEGSIESTLSPLEIAMSAGATFVAqsfSSDLKQLTALIEAGIKHEGFSLIN 194
Cdd:cd00568    95 VVVFNNGGYGTIRMHQEAF------YGGRVSGTDLSNPDFAALAEAYGAKGVR---VEDPEDLEAALAEALAAGGPALIE 165


                  .
gi 1566304881 195 V 195
Cdd:cd00568   166 V 166
TPP_PFOR_porB_like cd03376
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ...
 16-201 5.23e-15

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: 72.66  E-value: 5.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  16 CPGCGDFSIQAAIQRaaanvGLEPEQLAVISGiGCSGRISG--YINAYGLHGIH---GRALPIAQGVKLA------NREL 84
Cdd:cd03376     8 CAGCGAALALRHVLK-----ALGPDTVVVNPT-GCLEVITTpyPYTAWRVPWIHvafENAAAVASGIEAAlkalgrGKDI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  85 TVIASGGDGDGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQtspRSAegfvtkSTPEGSIESTlSP---------- 154
Cdd:cd03376    82 TVVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQ---RSG------STPYGAWTTT-TPvgkvsfgkkq 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1566304881 155 -----LEIAMSAGATFVAQSFSSDLKQLTALIEAGIKHEGFSLINVFSPCVT 201
Cdd:cd03376   152 pkkdlPLIMAAHNIPYVATASVAYPEDLYKKVKKALSIEGPAYIHILSPCPT 203
PRK11865 PRK11865
pyruvate synthase subunit beta;
16-201 3.96e-14

pyruvate synthase subunit beta;


Pssm-ID: 183346 [Multi-domain]  Cd Length: 299  Bit Score: 70.90  E-value: 3.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  16 CPGCGdfsiqaaiqraaANVGLE------PEQLAVISGIGCSGRISGYI--NAYGLHGIH-------GRALPIAQGVKLA 80
Cdd:PRK11865   21 CAGCG------------AAIAMRlalkalGKNTVIVVATGCLEVITTPYpeTAWNVPWIHvafenaaAVASGIERAVKAL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  81 NRELTVIASGGDGDGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQTSPRSAEGFVTKSTPEGSIESTLS------P 154
Cdd:PRK11865   89 GKKVNVVAIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKYSRGEDrpkknmP 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1566304881 155 LeIAMSAGATFVAQSFSSDLKQLTALIEAGIKHEGFSLINVFSPCVT 201
Cdd:PRK11865  169 L-IMAAHGIPYVATASIGYPEDFMEKVKKAKEVEGPAYIQVLQPCPT 214
PRK06163 PRK06163
hypothetical protein; Provisional
 43-195 8.22e-11

hypothetical protein; Provisional


Pssm-ID: 235721 [Multi-domain]  Cd Length: 202  Bit Score: 60.23  E-value: 8.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  43 AVISGIG-------CSGRISGyiNAYGLhGIHGRALPIAQGVKLANRELTVIASGGDGDGF-AIGMGHTIhAIRRNLNIT 114
Cdd:PRK06163   31 AVIGGIGntnfdlwAAGQRPQ--NFYML-GSMGLAFPIALGVALAQPKRRVIALEGDGSLLmQLGALGTI-AALAPKNLT 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881 115 YIVMDNQIYGLTKGQTSPRSAEGFVtkstpegsiestlspleIAMSAGATFVAQSFSSDLKQLTALIEAGIKHEGFSLIN 194
Cdd:PRK06163  107 IIVMDNGVYQITGGQPTLTSQTVDV-----------------VAIARGAGLENSHWAADEAHFEALVDQALSGPGPSFIA 169


                  .
gi 1566304881 195 V 195
Cdd:PRK06163  170 V 170
TPP_PFOR_PNO cd03377
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ...
 79-200 4.91e-10

Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of proteins similar to the single subunit pyruvate ferredoxin oxidoreductase (PFOR) of Desulfovibrio Africanus, present in bacteria and amitochondriate eukaryotes. This subfamily also includes proteins characterized as pyruvate NADP+ oxidoreductase (PNO). These enzymes are dependent on TPP and a divalent metal cation as cofactors. PFOR and PNO catalyze the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. The PFOR from cyanobacterium Anabaena (NifJ) is required for the transfer of electrons from pyruvate to flavodoxin, which reduces nitrogenase. The facultative anaerobic mitochondrion of the photosynthetic protist Euglena gracilis oxidizes pyruvate with PNO.


Pssm-ID: 239472  Cd Length: 365  Bit Score: 59.54  E-value: 4.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  79 LANRELTVIAS----GGDGDGFAIGMG---HTIhAIRRNLNItyIVMDNQIYGLTKGQTSprsaegfvtKSTPEGSI--- 148
Cdd:cd03377   143 LSLADYLVKKSvwiiGGDGWAYDIGYGgldHVL-ASGENVNI--LVLDTEVYSNTGGQAS---------KATPLGAVakf 210

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1566304881 149 --------ESTLSplEIAMSAGATFVAQ-SFSSDLKQ-LTALIEAgIKHEGFSLINVFSPCV 200
Cdd:cd03377   211 aaagkrtgKKDLG--MIAMSYGNVYVAQiALGANDNQtLKAFREA-EAYDGPSLIIAYSPCI 269
TPP_IOR_alpha cd02008
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ...
 13-199 4.41e-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: 51.89  E-value: 4.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  13 PNWCPGC---GDFSIQAaiqraaanvGLEPEQLAVISGIGCSGRisGYinAYGLHGIH-----GRALPIAQGVKLANREL 84
Cdd:cd02008     4 PGLCPGCphrPSFYALR---------KAFKKDSIVSGDIGCYTL--GA--LPPLNAIDtctcmGASIGVAIGMAKASEDK 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  85 TVIASGGDGDGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQTSPRSAEGfVTKSTPEGSIEstlsplEIAMSAGAT 164
Cdd:cd02008    71 KVVAVIGDSTFFHSGILGLINAVYNKANITVVILDNRTTAMTGGQPHPGTGKT-LTEPTTVIDIE------ALVRAIGVK 143

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1566304881 165 FVAQSFSSDLKQLTALIEAGIKHEGFSLINVFSPC 199
Cdd:cd02008   144 RVVVVDPYDLKAIREELKEALAVPGVSVIIAKRPC 178
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
 70-195 4.15e-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: 50.93  E-value: 4.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  70 ALPIAQGVKLANRELTVIASGGDGdGFAIGMG--HTihAIRRNLNITYIVMDNQIYGLTKgqtspRSAEGFvtksTPEGS 147
Cdd:COG0028   417 GLPAAIGAKLARPDRPVVAITGDG-GFQMNLQelAT--AVRYGLPVKVVVLNNGGLGMVR-----QWQELF----YGGRY 484

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1566304881 148 IESTLSPLEIAMsagatfVAQSFS------SDLKQLTALIEAGIKHEGFSLINV 195
Cdd:COG0028   485 SGTDLPNPDFAK------LAEAFGakgervETPEELEAALEEALASDGPALIDV 532
PRK11864 PRK11864
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
74-201 1.06e-06

3-methyl-2-oxobutanoate dehydrogenase subunit beta;


Pssm-ID: 237005 [Multi-domain]  Cd Length: 300  Bit Score: 48.93  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  74 AQGVKLANreltVIASGGDGDGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQTSPRSAEGFVTKSTPEGSIESTLS 153
Cdd:PRK11864   87 ARGEKGVI----VVGWAGDGGTADIGFQALSGAAERNHDILYIMYDNEAYMNTGIQRSSSTPYGAWTTTTPGGKREHKKP 162

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1566304881 154 PLEIAMSAGATFVA-------QSFSSDLKQLTALieagikhEGFSLINVFSPCVT 201
Cdd:PRK11864  163 VPDIMAAHKVPYVAtasiaypEDFIRKLKKAKEI-------RGFKFIHLLAPCPP 210
TPP_BFDC cd02002
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ...
 68-195 1.31e-06

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: 47.59  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  68 GRALPIAQGVKLANRELTVIASGGDGDG-FAIgmgHTI-HAIRRNLNITYIVMDNQIYGLTKgqtsprsaeGFVTKSTPE 145
Cdd:cd02002    52 GWGLPAAVGAALANPDRKVVAIIGDGSFmYTI---QALwTAARYGLPVTVVILNNRGYGALR---------SFLKRVGPE 119

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1566304881 146 GSIESTLSPL----------EIAMSAG--ATFVaqsfsSDLKQLTALIEAGIKHEGFSLINV 195
Cdd:cd02002   120 GPGENAPDGLdlldpgidfaAIAKAFGveAERV-----ETPEELDEALREALAEGGPALIEV 176
PRK08327 PRK08327
thiamine pyrophosphate-requiring protein;
68-130 4.16e-06

thiamine pyrophosphate-requiring protein;


Pssm-ID: 236243 [Multi-domain]  Cd Length: 569  Bit Score: 47.69  E-value: 4.16e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1566304881  68 GRALPIAQGVKLANRELTVIASGGDGdGFAIGMGHTIHAI--RRNLNITYIVMDNQIYGLTKGQT 130
Cdd:PRK08327  433 GWALGAALGAKLATPDRLVIATVGDG-SFIFGVPEAAHWVaeRYGLPVLVVVFNNGGWLAVKEAV 496
PRK07064 PRK07064
thiamine pyrophosphate-binding protein;
63-128 8.43e-06

thiamine pyrophosphate-binding protein;


Pssm-ID: 180820 [Multi-domain]  Cd Length: 544  Bit Score: 46.91  E-value: 8.43e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1566304881  63 LHGIH------GRALPIAQGVKLANRELTVIASGGDGdGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKG 128
Cdd:PRK07064  397 RANVHalgggiGQGLAMAIGAALAGPGRKTVGLVGDG-GLMLNLGELATAVQENANMVIVLMNDGGYGVIRN 467
TPP_POX cd02014
Thiamine pyrophosphate (TPP) family, Pyruvate oxidase (POX) subfamily, TPP-binding module; ...
 62-127 8.48e-06

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: 45.21  E-value: 8.48e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1566304881  62 GLHGIHGRALPIAQGVKLANRELTVIASGGDGdGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTK 127
Cdd:cd02014    48 GLLATMGNGLPGAIAAKLAYPDRQVIALSGDG-GFAMLMGDLITAVKYNLPVIVVVFNNSDLGFIK 112
PRK07525 PRK07525
sulfoacetaldehyde acetyltransferase; Validated
 39-163 1.81e-05

sulfoacetaldehyde acetyltransferase; Validated


Pssm-ID: 236042 [Multi-domain]  Cd Length: 588  Bit Score: 45.76  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  39 PEQLAVISGIGcsgRISGYINAY------------GLHGIHGRALPIAQGVKLANRELTVIASGGDGdGFAIGMGHTIHA 106
Cdd:PRK07525  400 PEDAIVSTDIG---NNCSIANSYlrfekgrkylapGSFGNCGYAFPAIIGAKIACPDRPVVGFAGDG-AWGISMNEVMTA 475

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1566304881 107 IRRNLNITYIVMDNQIYGLTKGQTSPRSAEGFVTkstpeGSIESTLSPLEIAMSAGA 163
Cdd:PRK07525  476 VRHNWPVTAVVFRNYQWGAEKKNQVDFYNNRFVG-----TELDNNVSYAGIAEAMGA 527
TPP_ComE cd03372
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ...
 40-132 4.82e-05

Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins similar to Methanococcus jannaschii sulfopyruvate decarboxylase beta subunit (ComE). M. jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits, which catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. ComDE requires TPP and divalent metal cation cofactors.


Pssm-ID: 239469 [Multi-domain]  Cd Length: 179  Bit Score: 43.05  E-value: 4.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  40 EQLAVISGIGCSGRISGYI-----NAYGLhGIHGRALPIAQGVKLAnRELTVIASGGDGdGFAIGMGH--TIHAIR-RNL 111
Cdd:cd03372    13 KDELVVSNIGFPSKELYAAgdrplNFYML-GSMGLASSIGLGLALA-QPRKVIVIDGDG-SLLMNLGAlaTIAAEKpKNL 89

                          90       100
                  ....*....|....*....|.
gi 1566304881 112 NItyIVMDNQIYGLTKGQTSP 132
Cdd:cd03372    90 II--VVLDNGAYGSTGNQPTH 108
PRK06546 PRK06546
pyruvate dehydrogenase; Provisional
 57-127 5.95e-05

pyruvate dehydrogenase; Provisional


Pssm-ID: 180614 [Multi-domain]  Cd Length: 578  Bit Score: 44.21  E-value: 5.95e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1566304881  57 YINAYG--------LHGIHGRALPIAQGVKLANRELTVIASGGDGdGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTK 127
Cdd:PRK06546  392 YITPNGrrrvigsfRHGSMANALPHAIGAQLADPGRQVISMSGDG-GLSMLLGELLTVKLYDLPVKVVVFNNSTLGMVK 469
TPP_Xsc_like cd02013
Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of ...
 65-127 9.90e-05

Thiamine pyrophosphate (TPP) family, Xsc-like subfamily, TPP-binding module; composed of proteins similar to Alcaligenes defragrans sulfoacetaldehyde acetyltransferase (Xsc). Xsc plays a key role in the degradation of taurine, catalyzing the desulfonation of 2-sulfoacetaldehyde into sulfite and acetyl phosphate. This enzyme requires TPP and divalent metal ions for activity.


Pssm-ID: 238971 [Multi-domain]  Cd Length: 196  Bit Score: 42.50  E-value: 9.90e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1566304881  65 GIHGRALPIAQGVKLANRELTVIASGGDGdGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTK 127
Cdd:cd02013    53 GNCGYALPAIIGAKAAAPDRPVVAIAGDG-AWGMSMMEIMTAVRHKLPVTAVVFRNRQWGAEK 114
PRK06112 PRK06112
acetolactate synthase catalytic subunit; Validated
 62-127 1.81e-04

acetolactate synthase catalytic subunit; Validated


Pssm-ID: 235700 [Multi-domain]  Cd Length: 578  Bit Score: 42.83  E-value: 1.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1566304881  62 GLHGIhGRALPIAQGVKLANRELTVIASGGDGdGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTK 127
Cdd:PRK06112  435 GLAGL-GWGVPMAIGAKVARPGAPVICLVGDG-GFAHVWAELETARRMGVPVTIVVLNNGILGFQK 498
PRK08266 PRK08266
hypothetical protein; Provisional
 62-124 4.64e-04

hypothetical protein; Provisional


Pssm-ID: 181337 [Multi-domain]  Cd Length: 542  Bit Score: 41.54  E-value: 4.64e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1566304881  62 GLHGIHGRALPIAQGVKLANRELTVIASGGDGdGFAIGMGHTIHAIRRNLNITYIVMDNQIYG 124
Cdd:PRK08266  399 GYQGTLGYGFPTALGAKVANPDRPVVSITGDG-GFMFGVQELATAVQHNIGVVTVVFNNNAYG 460
TPP_AHAS cd02015
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ...
 68-125 1.37e-03

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: 39.02  E-value: 1.37e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1566304881  68 GRALPIAQGVKLANRELTVIASGGDGdGFaiGMghTIH----AIRRNLNITYIVMDNQIYGL 125
Cdd:cd02015    53 GFGLPAAIGAKVARPDKTVICIDGDG-SF--QM--NIQelatAAQYNLPVKIVILNNGSLGM 109
PRK09124 PRK09124
ubiquinone-dependent pyruvate dehydrogenase;
64-124 1.54e-03

ubiquinone-dependent pyruvate dehydrogenase;


Pssm-ID: 181661 [Multi-domain]  Cd Length: 574  Bit Score: 39.97  E-value: 1.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1566304881  64 HGIHGRALPIAQGVKLANRELTVIASGGDGdGFAIGMGHTIHAIRRNLNITYIVMDNQIYG 124
Cdd:PRK09124  407 HGSMANAMPQALGAQAAHPGRQVVALSGDG-GFSMLMGDFLSLVQLKLPVKIVVFNNSVLG 466
PRK12474 PRK12474
hypothetical protein; Provisional
 68-185 2.30e-03

hypothetical protein; Provisional


Pssm-ID: 139002 [Multi-domain]  Cd Length: 518  Bit Score: 39.09  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  68 GRALPIAQGVKLANRELTVIASGGDGDGFAIGMGHTIHAiRRNLNITYIVMDNQIYGLTKG-------QTSPRSAEGFVT 140
Cdd:PRK12474  392 GQGLPLAAGAAVAAPDRKVVCPQGDGGAAYTMQALWTMA-RENLDVTVVIFANRSYAILNGelqrvgaQGAGRNALSMLD 470

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1566304881 141 KSTPEGSIESTLSPLEIAMSAGAT---FVAQSFSSDLKQLTALIEAGI 185
Cdd:PRK12474  471 LHNPELNWMKIAEGLGVEASRATTaeeFSAQYAAAMAQRGPRLIEAMI 518
PRK08155 PRK08155
acetolactate synthase large subunit;
62-131 2.86e-03

acetolactate synthase large subunit;


Pssm-ID: 181257 [Multi-domain]  Cd Length: 564  Bit Score: 38.92  E-value: 2.86e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  62 GLhGIHGRALPIAQGVKLANRELTVIASGGDGDgFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTKGQTS 131
Cdd:PRK08155  417 GL-GTMGFGLPAAIGAALANPERKVLCFSGDGS-LMMNIQEMATAAENQLDVKIILMNNEALGLVHQQQS 484
TPP_IolD cd02003
Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins ...
 68-195 4.35e-03

Thiamine pyrophosphate (TPP) family, IolD subfamily, TPP-binding module; composed of proteins similar to Rhizobium leguminosarum bv. viciae IolD. IolD plays an important role in myo-inositol catabolism.


Pssm-ID: 238961 [Multi-domain]  Cd Length: 205  Bit Score: 37.67  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  68 GRALPIAQGVKLANRELTVIASGGDGDGFaigMGHT--IHAIRRNLNITYIVMDNQIYG----LTKGQTSPRSAEGFVTK 141
Cdd:cd02003    51 GYEIAAGLGAKLAKPDREVYVLVGDGSYL---MLHSeiVTAVQEGLKIIIVLFDNHGFGcinnLQESTGSGSFGTEFRDR 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1566304881 142 STPEGSIESTLSPLEIAMSAGATFVAQSFSSDLKQLTALIEAGIKHEGFSLINV 195
Cdd:cd02003   128 DQESGQLDGALLPVDFAANARSLGARVEKVKTIEELKAALAKAKASDRTTVIVI 181
TPP_ComE_PpyrDC cd02001
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ...
 40-135 5.59e-03

Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed of proteins similar to sulfopyruvate decarboxylase beta subunit (ComE) and phosphonopyruvate decarboxylase (Ppyr decarboxylase). Methanococcus jannaschii sulfopyruvate decarboxylase (ComDE) is a dodecamer of six alpha (D) subunits and six (E) beta subunits which, catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway. Ppyr decarboxylase is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. Ppyr decarboxylase and ComDE require TPP and divalent metal cation cofactors.


Pssm-ID: 238959 [Multi-domain]  Cd Length: 157  Bit Score: 36.70  E-value: 5.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  40 EQLAVISGIGCSGRISGYI-----NAYGLhGIHGRALPIAQGVKL-ANRELTVIasggDGDG---FAIGMGHTIHAIRrN 110
Cdd:cd02001    13 GDTPIVSTTGYASRELYDVqdrdgHFYML-GSMGLAGSIGLGLALgLSRKVIVV----DGDGsllMNPGVLLTAGEFT-P 86

                          90       100
                  ....*....|....*....|....*
gi 1566304881 111 LNITYIVMDNQIYGLTKGQTSPRSA 135
Cdd:cd02001    87 LNLILVVLDNRAYGSTGGQPTPSSN 111
TPP_ALS cd02010
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ...
 68-127 7.17e-03

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: 36.50  E-value: 7.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1566304881  68 GRALPIAQGVKLANRELTVIASGGDGdGFAIGMGHTIHAIRRNLNITYIVMDNQIYGLTK 127
Cdd:cd02010    51 GVALPGAIGAKLVYPDRKVVAVSGDG-GFMMNSQELETAVRLKIPLVVLIWNDNGYGLIK 109
 
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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