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Conserved domains on  [gi|494507727|ref|WP_007297186|]
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MULTISPECIES: 2-oxoacid:ferredoxin oxidoreductase subunit beta [Rhodococcus]

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
 20-354 9.53e-176

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


:

Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 488.97  E-value: 9.53e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  20 TDEPQKAKDFTSDQEVRWCPGCGDYVILATIRSFLPELGLRRENLMFVSGIGCSSRFPYYLDTYGLHSIHGRAPAIATGL 99
Cdd:PRK11867   2 TDPMLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 100 AVTRPDLSVWVVTGDGDALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKSTPLGSVDHPFNTLSL 179
Cdd:PRK11867  82 KLANPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVEL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 180 VLGAEATFAARAMDSDRKGLTEVLRQAAAHRGTSFVEIYQDCPIF-NDGSFDVLRKdgseqRLIPLthgepivfggagey 258
Cdd:PRK11867 162 ALGAGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFnNVNTFDWFKE-----RLVKV-------------- 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 259 cvvrsgfglkvvatadvdrdeivvHDAHTDDPDYASAlSRLSDQDLTHTVTGVFRSVTRDTYDDMVRLQNEiarekdpvD 338
Cdd:PRK11867 223 ------------------------HDAEGYDPTNALA-AMKTLEEGDPIPTGIFYQVERPTYEEAVRAQIE--------G 269

                        330
                 ....*....|....*.
gi 494507727 339 DGSLQRLLTGHDTWTV 354
Cdd:PRK11867 270 PLALQDLLMGGDTWTV 285
 
Name Accession Description Interval E-value
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 20-354 9.53e-176

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 488.97  E-value: 9.53e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  20 TDEPQKAKDFTSDQEVRWCPGCGDYVILATIRSFLPELGLRRENLMFVSGIGCSSRFPYYLDTYGLHSIHGRAPAIATGL 99
Cdd:PRK11867   2 TDPMLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 100 AVTRPDLSVWVVTGDGDALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKSTPLGSVDHPFNTLSL 179
Cdd:PRK11867  82 KLANPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVEL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 180 VLGAEATFAARAMDSDRKGLTEVLRQAAAHRGTSFVEIYQDCPIF-NDGSFDVLRKdgseqRLIPLthgepivfggagey 258
Cdd:PRK11867 162 ALGAGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFnNVNTFDWFKE-----RLVKV-------------- 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 259 cvvrsgfglkvvatadvdrdeivvHDAHTDDPDYASAlSRLSDQDLTHTVTGVFRSVTRDTYDDMVRLQNEiarekdpvD 338
Cdd:PRK11867 223 ------------------------HDAEGYDPTNALA-AMKTLEEGDPIPTGIFYQVERPTYEEAVRAQIE--------G 269

                        330
                 ....*....|....*.
gi 494507727 339 DGSLQRLLTGHDTWTV 354
Cdd:PRK11867 270 PLALQDLLMGGDTWTV 285
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 37-224 4.86e-115

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: 331.80  E-value: 4.86e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  37 WCPGCGDYVILATIRSFLPELGLRRENLMFVSGIGCSSRFPYYLDTYGLHSIHGRAPAIATGLAVTRPDLSVWVVTGDGD 116
Cdd:cd03375    1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 117 ALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKSTPLGSVDHPFNTLSLVLGAEATFAARAMDSDR 196
Cdd:cd03375   81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160

                        170       180
                 ....*....|....*....|....*...
gi 494507727 197 KGLTEVLRQAAAHRGTSFVEIYQDCPIF 224
Cdd:cd03375  161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 25-249 7.18e-104

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: 305.92  E-value: 7.18e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  25 KAKDFTSDQEVRWCPGCGDYVILATIRSFLPELGLRrENLMFVSGIGCSSRFPYYLDTYGLHSIHGRAPAIATGLAVTRP 104
Cdd:COG1013    3 KKKDLLRTPGHRWCPGCGHGIILRLLLKALDELLDG-DKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 105 DLSVWVVTGDGDALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKSTPLGSVDHPFNTLSLVLGAE 184
Cdd:COG1013   82 DLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHG 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494507727 185 ATFAARAMDSDRKGLTEVLRQAAAHRGTSFVEIYQDCPIFNDG----SFDVLRKdgseqRLIPLTHGEP 249
Cdd:COG1013  162 ATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRdpskTIEWAKE-----GMWPLYEYDP 225
PorB_KorB TIGR02177
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ...
 35-226 3.95e-84

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: 256.61  E-value: 3.95e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727   35 VRWCPGCGDYVILATIRSFLPELGLRRENLMFVSGIGCSSRFPYYLDTYGLHSIHGRAPAIATGLAVTRPDLSVWVVTGD 114
Cdd:TIGR02177   1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  115 GDALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKSTPLGSVDHPFNTLSLVLGAEATFAARAMDS 194
Cdd:TIGR02177  81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 494507727  195 DRKGLTEVLRQAAAHRGTSFVEIYQDCPIFND 226
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNK 192
Oxoac_fdxbeta_Archa NF041171
2-oxoacid:ferredoxin oxidoreductase subunit beta;
35-226 4.81e-70

2-oxoacid:ferredoxin oxidoreductase subunit beta;


Pssm-ID: 469082 [Multi-domain]  Cd Length: 296  Bit Score: 220.96  E-value: 4.81e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  35 VRWCPGCGDYVILATIRSFLPELGLRRENLMFVSGIGCSSRFPYYLDTYGLHSIHGRAPAIATGLAVTRPDLSVWVVTGD 114
Cdd:NF041171   3 VDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 115 GDALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKSTPLGSVDHPFNTLSLVLGAEATFAARAMDS 194
Cdd:NF041171  83 GDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAY 162

                        170       180       190
                 ....*....|....*....|....*....|..
gi 494507727 195 DRKGLTEVLRQAAAHRGTSFVEIYQDCPIFND 226
Cdd:NF041171 163 DVKHLKELIKAAIKHKGLAFIDVLQPCPTYND 194
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
69-217 1.03e-33

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 121.92  E-value: 1.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727   69 GIGCSSRF---------PYYLDTYGLHSIHGRAPAIATGLAVTRPDLSVWVVTGDGDALSIGgNHLIHALRRNVNMTILL 139
Cdd:pfam02775   1 DIGCHQMWaaqyyrfrpPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNL-QELATAVRYNLPITVVV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494507727  140 FNNRIYGLTKGQYSPTsevGKITKSTPLGSVDHPFNTLSLVLGAEATfAARAmdSDRKGLTEVLRQAAAHRGTSFVEI 217
Cdd:pfam02775  80 LNNGGYGMTRGQQTPF---GGGRYSGPSGKILPPVDFAKLAEAYGAK-GARV--ESPEELEEALKEALEHDGPALIDV 151
 
Name Accession Description Interval E-value
PRK11867 PRK11867
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed
 20-354 9.53e-176

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Reviewed


Pssm-ID: 237006 [Multi-domain]  Cd Length: 286  Bit Score: 488.97  E-value: 9.53e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  20 TDEPQKAKDFTSDQEVRWCPGCGDYVILATIRSFLPELGLRRENLMFVSGIGCSSRFPYYLDTYGLHSIHGRAPAIATGL 99
Cdd:PRK11867   2 TDPMLTAKDFRNDQEPRWCPGCGDGSILAALQRALAELGLDPENVAVVSGIGCSGRLPGYINTYGFHTIHGRALAIATGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 100 AVTRPDLSVWVVTGDGDALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKSTPLGSVDHPFNTLSL 179
Cdd:PRK11867  82 KLANPDLTVIVVTGDGDALAIGGNHFIHALRRNIDITYILFNNQIYGLTKGQYSPTSPVGFVTKTTPYGSIEPPFNPVEL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 180 VLGAEATFAARAMDSDRKGLTEVLRQAAAHRGTSFVEIYQDCPIF-NDGSFDVLRKdgseqRLIPLthgepivfggagey 258
Cdd:PRK11867 162 ALGAGATFVARGFDSDVKQLTELIKAAINHKGFSFVEILQPCPTFnNVNTFDWFKE-----RLVKV-------------- 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 259 cvvrsgfglkvvatadvdrdeivvHDAHTDDPDYASAlSRLSDQDLTHTVTGVFRSVTRDTYDDMVRLQNEiarekdpvD 338
Cdd:PRK11867 223 ------------------------HDAEGYDPTNALA-AMKTLEEGDPIPTGIFYQVERPTYEEAVRAQIE--------G 269

                        330
                 ....*....|....*.
gi 494507727 339 DGSLQRLLTGHDTWTV 354
Cdd:PRK11867 270 PLALQDLLMGGDTWTV 285
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 37-224 4.86e-115

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: 331.80  E-value: 4.86e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  37 WCPGCGDYVILATIRSFLPELGLRRENLMFVSGIGCSSRFPYYLDTYGLHSIHGRAPAIATGLAVTRPDLSVWVVTGDGD 116
Cdd:cd03375    1 WCPGCGDGSILKALAKALAELGIDPEKVVVVSGIGCSSRLPYYFNTYGFHTLHGRALAVATGVKLANPDLTVIVVSGDGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 117 ALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKSTPLGSVDHPFNTLSLVLGAEATFAARAMDSDR 196
Cdd:cd03375   81 LAAIGGNHFIHAARRNIDITVIVHNNQIYGLTKGQASPTTPEGFKTKTTPYGNIEEPFNPLALALAAGATFVARGFSGDI 160

                        170       180
                 ....*....|....*....|....*...
gi 494507727 197 KGLTEVLRQAAAHRGTSFVEIYQDCPIF 224
Cdd:cd03375  161 KQLKEIIKKAIQHKGFSFVEVLSPCPTF 188
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 25-249 7.18e-104

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: 305.92  E-value: 7.18e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  25 KAKDFTSDQEVRWCPGCGDYVILATIRSFLPELGLRrENLMFVSGIGCSSRFPYYLDTYGLHSIHGRAPAIATGLAVTRP 104
Cdd:COG1013    3 KKKDLLRTPGHRWCPGCGHGIILRLLLKALDELLDG-DKTVVVSGIGCSSVAPGYFNVPGFHTLHGRAAAVATGIKLANP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 105 DLSVWVVTGDGDALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKSTPLGSVDHPFNTLSLVLGAE 184
Cdd:COG1013   82 DLTVIVFGGDGDTYDIGGNHLIHAARRNEDITYIVYDNEIYGNTGGQRSPTTPLGAKTTTTPYGKPEPPKDPAEIAAAHG 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494507727 185 ATFAARAMDSDRKGLTEVLRQAAAHRGTSFVEIYQDCPIFNDG----SFDVLRKdgseqRLIPLTHGEP 249
Cdd:COG1013  162 ATYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRdpskTIEWAKE-----GMWPLYEYDP 225
PRK05778 PRK05778
2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated
 37-322 9.43e-99

2-oxoglutarate ferredoxin oxidoreductase subunit beta; Validated


Pssm-ID: 235604 [Multi-domain]  Cd Length: 301  Bit Score: 294.48  E-value: 9.43e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  37 WCPGCGDYVILATIRSFLPELGLRRENLMFVSGIGCSSRFPYYLDTYGLHSIHGRAPAIATGLAVTRPDLSVWVVTGDGD 116
Cdd:PRK05778  20 WCPGCGNFGILNAIIQALAELGLDPDKVVVVSGIGCSSKIPGYFLSHGLHTLHGRAIAFATGAKLANPDLEVIVVGGDGD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 117 ALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKSTPLGSVDHPFNTLSLVLGAEATFAARAMDSDR 196
Cdd:PRK05778 100 LASIGGGHFIHAGRRNIDITVIVENNGIYGLTKGQASPTTPEGSKTKTAPYGNIEPPIDPCALALAAGATFVARSFAGDV 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 197 KGLTEVLRQAAAHRGTSFVEIYQDCPIFNDgsfdvlrkdgseqrliplthgepiVFGGAGEYCVVRsgfglkvvataDVD 276
Cdd:PRK05778 180 KQLVELIKKAISHKGFAFIDVLSPCVTFNG------------------------RNTSTKSPAYMR-----------EYY 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 494507727 277 RDEIV-VHDAHTDDP-DYASALSRLSDQDLT-HTVTGVFRSVTRDTYDD 322
Cdd:PRK05778 225 KKRVYkLKLEEDYDPtDRDKAAEKMLEEELGgKIPIGVFYKNERPTFEE 273
PorB_KorB TIGR02177
2-oxoacid:acceptor oxidoreductase, beta subunit, pyruvate/2-ketoisovalerate family; A number ...
 35-226 3.95e-84

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: 256.61  E-value: 3.95e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727   35 VRWCPGCGDYVILATIRSFLPELGLRRENLMFVSGIGCSSRFPYYLDTYGLHSIHGRAPAIATGLAVTRPDLSVWVVTGD 114
Cdd:TIGR02177   1 PDWCPGCGDFGILSALQRALAELNLDPEQVVVVSGIGCSAKTPHYVNVNGFHGLHGRALPVATGIKLANPHLKVIVVGGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  115 GDALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKSTPLGSVDHPFNTLSLVLGAEATFAARAMDS 194
Cdd:TIGR02177  81 GDLYGIGGNHFVAAGRRNVDITVIVHDNQVYGLTKGQASPTLLKGVKTKSLPYPNIQDPVNPLLLAIALGYTFVARGFSG 160

                         170       180       190
                  ....*....|....*....|....*....|..
gi 494507727  195 DRKGLTEVLRQAAAHRGTSFVEIYQDCPIFND 226
Cdd:TIGR02177 161 DVAHLKEIIKEAINHKGYALVDILQPCVTYNK 192
PRK11866 PRK11866
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 37-233 5.69e-80

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183347 [Multi-domain]  Cd Length: 279  Bit Score: 245.82  E-value: 5.69e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  37 WCPGCGDYVILATIRSFLPELGLRRENLMFVSGIGCSSRFPYYLDTYGLHSIHGRAPAIATGLAVTRPDLSVWVVTGDGD 116
Cdd:PRK11866   9 WCPGCGNYGILEALRKALAELGIPPENVVVVSGIGCSSNLPEFLNTYGIHGIHGRVLPIATGVKWANPKLTVIGYGGDGD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 117 ALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKSTPLGSVDHPFNTLSLVLGAEATFAARAMDSDR 196
Cdd:PRK11866  89 GYGIGLGHLPHAARRNVDITYIVSNNQVYGLTTGQASPTTPRGVKTKTTPDGNIEEPFNPIALALAAGATFVARGFSGDV 168

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 494507727 197 KGLTEVLRQAAAHRGTSFVEIYQDCPIFND-GSFDVLR 233
Cdd:PRK11866 169 KHLKEIIKEAIKHKGFSFIDVLSPCVTFNKlNTYDWFR 206
Oxoac_fdxbeta_Archa NF041171
2-oxoacid:ferredoxin oxidoreductase subunit beta;
35-226 4.81e-70

2-oxoacid:ferredoxin oxidoreductase subunit beta;


Pssm-ID: 469082 [Multi-domain]  Cd Length: 296  Bit Score: 220.96  E-value: 4.81e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  35 VRWCPGCGDYVILATIRSFLPELGLRRENLMFVSGIGCSSRFPYYLDTYGLHSIHGRAPAIATGLAVTRPDLSVWVVTGD 114
Cdd:NF041171   3 VDWCPGCGNFGILTAEQQALAELGLDPKKVVIVSGIGCSGKTPHFVNVSGVHTLHGRAIPFATGIKLANPELEVIVNGGD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 115 GDALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKSTPLGSVDHPFNTLSLVLGAEATFAARAMDS 194
Cdd:NF041171  83 GDLLGIGAGHFVALGRRNVDITVILHDNGVYGLTKGQASPTLPRGVKTKSLPKPNIQDAVNPIALALASGYTFVARGYAY 162

                        170       180       190
                 ....*....|....*....|....*....|..
gi 494507727 195 DRKGLTEVLRQAAAHRGTSFVEIYQDCPIFND 226
Cdd:NF041171 163 DVKHLKELIKAAIKHKGLAFIDVLQPCPTYND 194
PRK11869 PRK11869
2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional
 30-225 2.99e-67

2-oxoacid ferredoxin oxidoreductase subunit beta; Provisional


Pssm-ID: 183349 [Multi-domain]  Cd Length: 280  Bit Score: 213.10  E-value: 2.99e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  30 TSDQEVRWCPGCGDYVILATIRSFLPELGLRRENLMFVSGIGCSSRFPYYLDTYGLHSIHGRAPAIATGLAVTRPDLSVW 109
Cdd:PRK11869   3 PEKYDIAWCPGCGNFGIRNALMKALSELNLKPRQVVIVSGIGQAAKMPHYINVNGFHTLHGRAIPAATAVKATNPELTVI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 110 VVTGDGDALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKSTPLGSVDHPFNTLSLVLGAEATFAA 189
Cdd:PRK11869  83 AEGGDGDMYAEGGNHLIHAIRRNPDITVLVHNNQVYGLTKGQASPTTLKGFKTPTQPWGVFEEPFNPIALAIALDASFVA 162

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 494507727 190 RAMDSDRKGLTEVLRQAAAHRGTSFVEIYQDCPIFN 225
Cdd:PRK11869 163 RTFSGDIEETKEILKEAIKHKGLAIVDIFQPCVSFN 198
oorB PRK09628
2-oxoglutarate ferredoxin oxidoreductase subunit beta;
37-223 1.41e-59

2-oxoglutarate ferredoxin oxidoreductase subunit beta;


Pssm-ID: 182003 [Multi-domain]  Cd Length: 277  Bit Score: 193.41  E-value: 1.41e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  37 WCPGCGDYVIL-ATIRSFlPELGLRRENLMFVSGIGCSSRFPYYLDTYGLHSIHGRAPAIATGLAVTRPDLSVWVVTGDG 115
Cdd:PRK09628  18 WCWGCGDGVILkSIIRAI-DKLGWNMDDVCVVSGIGCSGRFSSYVNCNTVHTTHGRAVAYATGIKLANPDKHVIVVSGDG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 116 DALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKSTPLGSVDHPFNTLSLVLGAEATFAARAMDSD 195
Cdd:PRK09628  97 DGLAIGGNHTIHGCRRNIDLNFILINNFIYGLTNSQTSPTTPKGMWTVTAQYGNIDPTFDACKLATAAGASFVARESVID 176

                        170       180
                 ....*....|....*....|....*...
gi 494507727 196 RKGLTEVLRQAAAHRGTSFVEIYQDCPI 223
Cdd:PRK09628 177 PQKLEKLLVKGFSHKGFSFFDVFSNCHI 204
TPP_enzyme_C pfam02775
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
69-217 1.03e-33

Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;


Pssm-ID: 460689 [Multi-domain]  Cd Length: 151  Bit Score: 121.92  E-value: 1.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727   69 GIGCSSRF---------PYYLDTYGLHSIHGRAPAIATGLAVTRPDLSVWVVTGDGDALSIGgNHLIHALRRNVNMTILL 139
Cdd:pfam02775   1 DIGCHQMWaaqyyrfrpPRRYLTSGGLGTMGYGLPAAIGAKLARPDRPVVAIAGDGGFQMNL-QELATAVRYNLPITVVV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494507727  140 FNNRIYGLTKGQYSPTsevGKITKSTPLGSVDHPFNTLSLVLGAEATfAARAmdSDRKGLTEVLRQAAAHRGTSFVEI 217
Cdd:pfam02775  80 LNNGGYGMTRGQQTPF---GGGRYSGPSGKILPPVDFAKLAEAYGAK-GARV--ESPEELEEALKEALEHDGPALIDV 151
TPP_PFOR cd02018
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ...
 38-234 6.65e-16

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: 75.99  E-value: 6.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  38 CPGCGDYVIlatIRSFLPELGlRRENLMFVSGIGCSS----RFPYylDTYGLHSIH---GRAPAIATG----LAVTRPDL 106
Cdd:cd02018    8 CAGCGEVTA---VRVVLAALP-APEDTVIANSTGCSSvyasTAPF--NSWAVPWVNslfEDANAVASGlkrgLKARFPKD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 107 S-------VWVVTGDGDALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKSTPLGSVDHPFNTLSL 179
Cdd:cd02018   82 ReldkkkdVVVIGGDGATYDIGFGALSHSLFRGEDITVIVLDNEVYSNTGGQRSGATPLGADSKMAPAGKKEDKKDLVLI 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 180 VLGAEATFAARAMDSDRKGLTEVLRQA-AAHRGTSFVEIYQDCPI---FNDG-SFDVLRK 234
Cdd:cd02018  162 AATHGCVYVARLSPALKKHFLKVVKEAiSRTDGPTFIHAYTPCITewgIGSGkSLELARK 221
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 46-217 9.50e-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: 73.83  E-value: 9.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  46 ILATIRSFLPELGlrrenlMFVSGIGCSSRFPYYL------DTYGLHSIHGR---APAIATGLAVTRPDLSVWVVTGDGD 116
Cdd:cd00568    2 VLAALRAALPEDA------IVVNDAGNSAYWAYRYlplrrgRRFLTSTGFGAmgyGLPAAIGAALAAPDRPVVCIAGDGG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 117 ALSiGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKStpLGSVDhpFNTLSLVLGAEatfAARAmdSDR 196
Cdd:cd00568   76 FMM-TGQELATAVRYGLPVIVVVFNNGGYGTIRMHQEAFYGGRVSGTD--LSNPD--FAALAEAYGAK---GVRV--EDP 145

                        170       180
                 ....*....|....*....|.
gi 494507727 197 KGLTEVLRQAAAHRGTSFVEI 217
Cdd:cd00568  146 EDLEAALAEALAAGGPALIEV 166
PRK11865 PRK11865
pyruvate synthase subunit beta;
36-222 9.98e-14

pyruvate synthase subunit beta;


Pssm-ID: 183346 [Multi-domain]  Cd Length: 299  Bit Score: 70.90  E-value: 9.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  36 RWCPGCGDYVILatiRSFLPELGlrrENLMFVSGIGCSS----RFPYylDTYGLHSIH---GRAPAIATGL-----AVTR 103
Cdd:PRK11865  19 RACAGCGAAIAM---RLALKALG---KNTVIVVATGCLEvittPYPE--TAWNVPWIHvafENAAAVASGIeravkALGK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 104 pDLSVWVVTGDGDALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKSTPLGSV----DHPFNTLSL 179
Cdd:PRK11865  91 -KVNVVAIGGDGGTADIGFQSLSGAMERGHNILYLMYDNEAYMNTGIQRSGSTPFGASTTTSPAGKYsrgeDRPKKNMPL 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 494507727 180 VLGAE-ATFAARAMDSDRKGLTEVLRQAAAHRGTSFVEIYQDCP 222
Cdd:PRK11865 170 IMAAHgIPYVATASIGYPEDFMEKVKKAKEVEGPAYIQVLQPCP 213
TPP_PFOR_porB_like cd03376
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ...
 36-222 7.99e-12

Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of proteins similar to the beta subunit (porB) of the Helicobacter pylori four-subunit pyruvate ferredoxin oxidoreductase (PFOR), which are also found in archaea and some hyperthermophilic bacteria. PFOR catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA, a crucial step in many metabolic pathways. Archaea, anaerobic bacteria and eukaryotes that lack mitochondria (and therefore pyruvate dehydrogenase) use PFOR to oxidatively decarboxylate pyruvate, with ferredoxin or flavodoxin as the electron acceptor. The 36-kDa porB subunit contains the binding sites for the cofactors, TPP and a divalent metal cation, which are required for activity.


Pssm-ID: 239471 [Multi-domain]  Cd Length: 235  Bit Score: 64.18  E-value: 7.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  36 RWCPGCGDYVILatiRSFLPELGlrrENLMFVSGIGC----SSRFPYY-LDTYGLHSIHGRAPAIATGL-----AVTRP- 104
Cdd:cd03376    6 RACAGCGAALAL---RHVLKALG---PDTVVVNPTGCleviTTPYPYTaWRVPWIHVAFENAAAVASGIeaalkALGRGk 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 105 DLSVWVVTGDGDALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKSTPLGSVD-----HPFNTLSL 179
Cdd:cd03376   80 DITVVAFAGDGGTADIGFQALSGAAERGHDILYICYDNEAYMNTGIQRSGSTPYGAWTTTTPVGKVSfgkkqPKKDLPLI 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 494507727 180 VLGAEATFAARAMDSDRKGLTEVLRQAAAHRGTSFVEIYQDCP 222
Cdd:cd03376  160 MAAHNIPYVATASVAYPEDLYKKVKKALSIEGPAYIHILSPCP 202
PRK11864 PRK11864
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
38-223 7.60e-09

3-methyl-2-oxobutanoate dehydrogenase subunit beta;


Pssm-ID: 237005 [Multi-domain]  Cd Length: 300  Bit Score: 56.25  E-value: 7.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  38 CPGCGdyvILATIRSFLPELGlrrENLMFVSGIGCSS----RFPYY-LDTYGLHSIHGRAPAIATGLAV---TRPDLSVW 109
Cdd:PRK11864  21 CPGCG---APLGLRYLLKALG---EKTVLVIPASCSTviqgDTPKSpLTVPVLHTAFAATAAVASGIEEalkARGEKGVI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 110 VVT--GDGDALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKSTPLGSVDHPFNTLSLVLGAEATF 187
Cdd:PRK11864  95 VVGwaGDGGTADIGFQALSGAAERNHDILYIMYDNEAYMNTGIQRSSSTPYGAWTTTTPGGKREHKKPVPDIMAAHKVPY 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 494507727 188 AARA-----MDSDRKgltevLRQAAAHRGTSFVEIYQDCPI 223
Cdd:PRK11864 175 VATAsiaypEDFIRK-----LKKAKEIRGFKFIHLLAPCPP 210
TPP_PpyrDC cd03371
Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of ...
 62-217 2.48e-07

Thiamine pyrophosphate (TPP) family, PpyrDC subfamily, TPP-binding module; composed of proteins similar to phosphonopyruvate decarboxylase (PpyrDC) proteins. PpyrDC is a homotrimeric enzyme which functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. These proteins require TPP and divalent metal cation cofactors.


Pssm-ID: 239468 [Multi-domain]  Cd Length: 188  Bit Score: 50.39  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  62 ENLMFVSGIGCSSRFPYYL-DTYGLHSIH--------GRAPAIATGLAVTRPDLSVWVVTGDGDAL-SIGGNHLIHALRR 131
Cdd:cd03371   14 ATAAVVSTTGMTSRELFELrDRPGGGHAQdfltvgsmGHASQIALGIALARPDRKVVCIDGDGAALmHMGGLATIGGLAP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 132 NvNMTILLFNNRIYGLTKGQysPTSevgkitkstplgSVDHPFNTLSLVLGAEATFAAramdSDRKGLTEVLRQAAAHRG 211
Cdd:cd03371   94 A-NLIHIVLNNGAHDSVGGQ--PTV------------SFDVSLPAIAKACGYRAVYEV----PSLEELVAALAKALAADG 154


                 ....*.
gi 494507727 212 TSFVEI 217
Cdd:cd03371  155 PAFIEV 160
TPP_PFOR_PNO cd03377
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ...
 107-170 2.71e-07

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: 51.84  E-value: 2.71e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 494507727 107 SVWVVTGDGDALSIGGNHLIH--ALRRNVNmtILLFNNRIYGLTKGQYSptsevgkitKSTPLGSV 170
Cdd:cd03377  153 SVWIIGGDGWAYDIGYGGLDHvlASGENVN--ILVLDTEVYSNTGGQAS---------KATPLGAV 207
TPP_IOR_alpha cd02008
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ...
 38-221 3.83e-07

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: 49.58  E-value: 3.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  38 CPGCGDYVILATIRsflpelGLRRENLMFVSGIGCSSR---FPY-YLDTyglhSIH-GRAPAIATGLAVTRPDLSVWVVT 112
Cdd:cd02008    7 CPGCPHRPSFYALR------KAFKKDSIVSGDIGCYTLgalPPLnAIDT----CTCmGASIGVAIGMAKASEDKKVVAVI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727 113 GDGDALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKITKSTPlgsvdHPFNTLSLVLGAEAtfaARAM 192
Cdd:cd02008   77 GDSTFFHSGILGLINAVYNKANITVVILDNRTTAMTGGQPHPGTGKTLTEPTTV-----IDIEALVRAIGVKR---VVVV 148

                        170       180       190
                 ....*....|....*....|....*....|
gi 494507727 193 DS-DRKGLTEVLRQAAAHRGTSFVEIYQDC 221
Cdd:cd02008  149 DPyDLKAIREELKEALAVPGVSVIIAKRPC 178
TPP_ComE_PpyrDC cd02001
Thiamine pyrophosphate (TPP) family, ComE and PpyrDC subfamily, TPP-binding module; composed ...
 62-158 1.08e-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: 45.17  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  62 ENLMFVSGIGCSSRFPYYLDT-----YGLHSIhGRAPAIATGLAVTRPDlSVWVVTGDGDALSIGGNHLIHALRRNVNMT 136
Cdd:cd02001   13 GDTPIVSTTGYASRELYDVQDrdghfYMLGSM-GLAGSIGLGLALGLSR-KVIVVDGDGSLLMNPGVLLTAGEFTPLNLI 90

                         90       100
                 ....*....|....*....|..
gi 494507727 137 ILLFNNRIYGLTKGQYSPTSEV 158
Cdd:cd02001   91 LVVLDNRAYGSTGGQPTPSSNV 112
PRK06163 PRK06163
hypothetical protein; Provisional
 83-161 1.30e-05

hypothetical protein; Provisional


Pssm-ID: 235721 [Multi-domain]  Cd Length: 202  Bit Score: 45.59  E-value: 1.30e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 494507727  83 YGLHSIhGRAPAIATGLAVTRPDLSVWVVTGDGDALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYSPTSEVGKI 161
Cdd:PRK06163  54 YMLGSM-GLAFPIALGVALAQPKRRVIALEGDGSLLMQLGALGTIAALAPKNLTIIVMDNGVYQITGGQPTLTSQTVDV 131
pyruv_ox_red TIGR02176
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ...
 107-221 2.20e-05

pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single chain form of pyruvate:ferredoxin (or flavodoxin) oxidoreductase. This enzyme may transfer electrons to nitrogenase in nitrogen-fixing species. Portions of this protein are homologous to gamma subunit of the four subunit pyruvate:ferredoxin (flavodoxin) oxidoreductase.


Pssm-ID: 131231 [Multi-domain]  Cd Length: 1165  Bit Score: 46.30  E-value: 2.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727   107 SVWVVTGDGDALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQYS---PTSEV------GKITKSTPLGsvdhpfnTL 177
Cdd:TIGR02176  953 SVWIIGGDGWAYDIGYGGLDHVLASGKDVNVLVMDTEVYSNTGGQSSkatPTGAIakfaaaGKRTSKKDLG-------MM 1025

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 494507727   178 SLVLGaEATFAARAMDSDRKGLTEVLRQAAAHRGTSFVEIYQDC 221
Cdd:TIGR02176 1026 AMTYG-YVYVAQVSMGANMQQTLKAFREAEAYDGPSIVIAYSPC 1068
TPP_ComE cd03372
Thiamine pyrophosphate (TPP) family, ComE subfamily, TPP-binding module; composed of proteins ...
 61-158 3.95e-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: 43.82  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  61 RENLMFVSGIGCSSRFPYYLDT-----YGLHSIhGRAPAIATGLAVTRPDlSVWVVTGDGDALSIGGNHLIHALRRNVNM 135
Cdd:cd03372   12 LKDELVVSNIGFPSKELYAAGDrplnfYMLGSM-GLASSIGLGLALAQPR-KVIVIDGDGSLLMNLGALATIAAEKPKNL 89

                         90       100
                 ....*....|....*....|...
gi 494507727 136 TILLFNNRIYGLTKGQYSPTSEV 158
Cdd:cd03372   90 IIVVLDNGAYGSTGNQPTHAGKK 112
IlvB COG0028
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ...
 93-217 4.79e-05

Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439799 [Multi-domain]  Cd Length: 548  Bit Score: 45.15  E-value: 4.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  93 PAiATGLAVTRPDLSVWVVTGDGdALSIGGNHLIHALRRNVNMTILLFNNRIYGLTK--------GQYSPTSevgkitks 164
Cdd:COG0028  419 PA-AIGAKLARPDRPVVAITGDG-GFQMNLQELATAVRYGLPVKVVVLNNGGLGMVRqwqelfygGRYSGTD-------- 488

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 494507727 165 tpLGSVDhpFNTLslvlgAEAtFAARAMD-SDRKGLTEVLRQAAAHRGTSFVEI 217
Cdd:COG0028  489 --LPNPD--FAKL-----AEA-FGAKGERvETPEELEAALEEALASDGPALIDV 532
TPP_AHAS cd02015
Thiamine pyrophosphate (TPP) family, Acetohydroxyacid synthase (AHAS) subfamily, TPP-binding ...
 83-217 4.97e-05

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: 43.64  E-value: 4.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  83 YGLhsihgraPAiATGLAVTRPDLSVWVVTGDGdalSIGGNhlIHAL----RRNVNMTILLFNNRIYGLT--------KG 150
Cdd:cd02015   54 FGL-------PA-AIGAKVARPDKTVICIDGDG---SFQMN--IQELataaQYNLPVKIVILNNGSLGMVrqwqelfyEG 120

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494507727 151 QYSPTsevgkitksTPLGSVDhpFNTLslvlgAEAtFAARAMD-SDRKGLTEVLRQAAAHRGTSFVEI 217
Cdd:cd02015  121 RYSHT---------TLDSNPD--FVKL-----AEA-YGIKGLRvEKPEELEAALKEALASDGPVLLDV 171
PRK07092 PRK07092
benzoylformate decarboxylase; Reviewed
 93-217 2.83e-04

benzoylformate decarboxylase; Reviewed


Pssm-ID: 235931 [Multi-domain]  Cd Length: 530  Bit Score: 42.63  E-value: 2.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  93 PAiATGLAVTRPDLSVWVVTGDGDAlsiggNHLIHAL----RRNVNMTILLFNNRIYGLTKGqYSPTSEVGKiTKSTPLG 168
Cdd:PRK07092 414 PA-AVGVALAQPGRRVIGLIGDGSA-----MYSIQALwsaaQLKLPVTFVILNNGRYGALRW-FAPVFGVRD-VPGLDLP 485

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 494507727 169 SVDhpFNTLSLVLGAEATFAARAMDsdrkgLTEVLRQAAAHRGTSFVEI 217
Cdd:PRK07092 486 GLD--FVALARGYGCEAVRVSDAAE-----LADALARALAADGPVLVEV 527
PRK07064 PRK07064
thiamine pyrophosphate-binding protein;
85-217 3.50e-04

thiamine pyrophosphate-binding protein;


Pssm-ID: 180820 [Multi-domain]  Cd Length: 544  Bit Score: 42.28  E-value: 3.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  85 LHSIHGRAPAIATGL------AVTRPDLSVWVVTGDGdALSIGGNHLIHALRRNVNMTILLFNNRIYGLTKG----QYsp 154
Cdd:PRK07064 397 RANVHALGGGIGQGLamaigaALAGPGRKTVGLVGDG-GLMLNLGELATAVQENANMVIVLMNDGGYGVIRNiqdaQY-- 473

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494507727 155 tsevGKITKSTPLGSVDhpFNTLSLVLGAEATFAARAMDSDRkglteVLRQAAAHRGTSFVEI 217
Cdd:PRK07064 474 ----GGRRYYVELHTPD--FALLAASLGLPHWRVTSADDFEA-----VLREALAKEGPVLVEV 525
PRK07586 PRK07586
acetolactate synthase large subunit;
96-216 9.62e-04

acetolactate synthase large subunit;


Pssm-ID: 236063 [Multi-domain]  Cd Length: 514  Bit Score: 40.98  E-value: 9.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  96 ATGLAVTRPDLSVWVVTGDGDALsiggnHLIHAL----RRNVNMTILLFNNRIYGLTKGQYSPT--SEVGKITKStpLGS 169
Cdd:PRK07586 394 ATGAAVACPDRKVLALQGDGSAM-----YTIQALwtqaRENLDVTTVIFANRAYAILRGELARVgaGNPGPRALD--MLD 466

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 494507727 170 VDHP---FNTLSLVLGAEATFAARAMDsdrkgLTEVLRQAAAHRGTSFVE 216
Cdd:PRK07586 467 LDDPdldWVALAEGMGVPARRVTTAEE-----FADALAAALAEPGPHLIE 511
PRK06112 PRK06112
acetolactate synthase catalytic subunit; Validated
 95-220 9.77e-04

acetolactate synthase catalytic subunit; Validated


Pssm-ID: 235700 [Multi-domain]  Cd Length: 578  Bit Score: 40.90  E-value: 9.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  95 IATGLAVTRPDLSVWVVTGDGdalsiGGNH----LIHALRRNVNMTILLFNNRIYGLTKgqYSPTSEVGKITKSTPLGSV 170
Cdd:PRK06112 445 MAIGAKVARPGAPVICLVGDG-----GFAHvwaeLETARRMGVPVTIVVLNNGILGFQK--HAETVKFGTHTDACHFAAV 517

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 494507727 171 DHpfntlslVLGAEATFAARAMDSDRKGLTEVLRQAAAHRGTSFVEIYQD 220
Cdd:PRK06112 518 DH-------AAIARACGCDGVRVEDPAELAQALAAAMAAPGPTLIEVITD 560
TPP_ALS cd02010
Thiamine pyrophosphate (TPP) family, Acetolactate synthase (ALS) subfamily, TPP-binding module; ...
 94-223 6.99e-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: 36.88  E-value: 6.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  94 AIATGLAvtRPDLSVWVVTGDGDALsIGGNHLIHALRRNVNMTILLFNNRIYGLTKGQ----YSPTSEVgkitkstPLGS 169
Cdd:cd02010   57 AIGAKLV--YPDRKVVAVSGDGGFM-MNSQELETAVRLKIPLVVLIWNDNGYGLIKWKqekeYGRDSGV-------DFGN 126

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 494507727 170 VDhpfntlsLVLGAEAtFAARAMD-SDRKGLTEVLRQAAAHRGTSFVeiyqDCPI 223
Cdd:cd02010  127 PD-------FVKYAES-FGAKGYRiESADDLLPVLERALAADGVHVI----DCPV 169
TPP_BZL_OCoD_HPCL cd02004
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ...
 96-217 9.28e-03

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: 36.74  E-value: 9.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494507727  96 ATGLAVTRPDLSVWVVTGDGdALSIGGNHLIHALRRNVNMTILLFNN-RIYGLTKGQysPTSEVGKITKSTPLGSVDHpf 174
Cdd:cd02004   57 AIAAALARPDKRVVLVEGDG-AFGFSGMELETAVRYNLPIVVVVGNNgGWYQGLDGQ--QLSYGLGLPVTTLLPDTRY-- 131

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 494507727 175 ntlSLV---LGAEATFAARAMDsdrkgLTEVLRQAAAHRGTSFVEI 217
Cdd:cd02004  132 ---DLVaeaFGGKGELVTTPEE-----LKPALKRALASGKPALINV 169
 
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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