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Conserved domains on  [gi|2096027763|gb|UAX24987|]
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pyruvate flavodoxin/ferrodoxin oxidoreductase, partial [uncultured microorganism]

Protein Classification

thiamine pyrophosphate-dependent enzyme( domain architecture ID 22)

thiamine pyrophosphate (TPP)-dependent enzyme uses thiamine pyrophosphate as a cofactor to catalyze various reactions including reversible decarboxylation

CATH:  3.40.50.1220
Gene Ontology:  GO:0030976|GO:0003824
PubMed:  12735696|15514159
SCOP:  3001790

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TPP_enzymes super family cl01629
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
 1-156 2.10e-90

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.


The actual alignment was detected with superfamily member cd03377:

Pssm-ID: 470272  Cd Length: 365  Bit Score: 267.16  E-value: 2.10e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096027763   1 CGETPYLKLLSQLFGDRSLIANATGCSSIYGGNLPTTPWTKNADGRGPAWSNSLLEDNAEFGLGMRVALDKRVEYAFEIL 80
Cdd:cd03377    12 CGETPYVKLLTQLFGDRMVIANATGCSSIYGGSAPTTPYTTNAKGRGPAWANSLFEDNAEFGLGMRLAVDQRRERARELV 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2096027763  81 KRLAPEIGDDLVADLINADQVDEAGIYQQRERVVLLKTKLEKSSSPEAAHLLSLADVLVKKDVWIVGGDGWAYDIG 156
Cdd:cd03377    92 QKLIEKIGDEELKTLLNAWLATEDDIEESRERVAKLKPLLAAEKDELAKELLSLADYLVKKSVWIIGGDGWAYDIG 167
 
Name Accession Description Interval E-value
TPP_PFOR_PNO cd03377
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ...
 1-156 2.10e-90

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: 267.16  E-value: 2.10e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096027763   1 CGETPYLKLLSQLFGDRSLIANATGCSSIYGGNLPTTPWTKNADGRGPAWSNSLLEDNAEFGLGMRVALDKRVEYAFEIL 80
Cdd:cd03377    12 CGETPYVKLLTQLFGDRMVIANATGCSSIYGGSAPTTPYTTNAKGRGPAWANSLFEDNAEFGLGMRLAVDQRRERARELV 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2096027763  81 KRLAPEIGDDLVADLINADQVDEAGIYQQRERVVLLKTKLEKSSSPEAAHLLSLADVLVKKDVWIVGGDGWAYDIG 156
Cdd:cd03377    92 QKLIEKIGDEELKTLLNAWLATEDDIEESRERVAKLKPLLAAEKDELAKELLSLADYLVKKSVWIIGGDGWAYDIG 167
pyruv_ox_red TIGR02176
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ...
 1-156 1.97e-69

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: 226.57  E-value: 1.97e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096027763    1 CGETPYLKLLSQLFGDRSLIANATGCSSIYGGNLPTTPWTKNADGRGPAWSNSLLEDNAEFGLGMRVALDKRVEYAFEIL 80
Cdd:TIGR02176  811 CGETPYVKLLTQLFGDRMVIANATGCSSIWGASAPSTPYTTNEQGQGPAWSNSLFEDNAEFGYGMRLSMDKRRERLAELA 890

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096027763   81 KR-LAPEIGDDLVADLINADQVDEAGIYQQRERVVLLKTKLEKSSSPEAAHLLSLADVLVKKDVWIVGGDGWAYDIG 156
Cdd:TIGR02176  891 AKaLESDIASGDLKAALNGWLAGKNDIEKSKERVAKLKKLLAGEKDDLLKEIYAVSDLFVKKSVWIIGGDGWAYDIG 967
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 1-156 5.71e-06

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: 44.36  E-value: 5.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096027763   1 CGETPYLKLLSQLF-----GDRSLIANATGCSSIYggnlpTTPWTKNadgrgpaWSNSLLEDNAEFGLGMRVALDKRVey 75
Cdd:COG1013    19 CGHGIILRLLLKALdelldGDKTVVVSGIGCSSVA-----PGYFNVP-------GFHTLHGRAAAVATGIKLANPDLT-- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096027763  76 afeilkrlapeigddlvadlinadqvdeagiyqqrervvllktklekssspeaahllsladvlvkkdVWIVGGDGWAYDI 155
Cdd:COG1013    85 -------------------------------------------------------------------VIVFGGDGDTYDI 97


                  .
gi 2096027763 156 G 156
Cdd:COG1013    98 G 98
PRK11865 PRK11865
pyruvate synthase subunit beta;
1-72 7.69e-05

pyruvate synthase subunit beta;


Pssm-ID: 183346 [Multi-domain]  Cd Length: 299  Bit Score: 41.24  E-value: 7.69e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2096027763   1 CGETPYLKLLSQLFGDRSLIANATGCSSIYGGNLPTTPWtknadgRGPaWSNSLLEDNAEFGLGMRVALDKR 72
Cdd:PRK11865   24 CGAAIAMRLALKALGKNTVIVVATGCLEVITTPYPETAW------NVP-WIHVAFENAAAVASGIERAVKAL 88
 
Name Accession Description Interval E-value
TPP_PFOR_PNO cd03377
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ...
 1-156 2.10e-90

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: 267.16  E-value: 2.10e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096027763   1 CGETPYLKLLSQLFGDRSLIANATGCSSIYGGNLPTTPWTKNADGRGPAWSNSLLEDNAEFGLGMRVALDKRVEYAFEIL 80
Cdd:cd03377    12 CGETPYVKLLTQLFGDRMVIANATGCSSIYGGSAPTTPYTTNAKGRGPAWANSLFEDNAEFGLGMRLAVDQRRERARELV 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2096027763  81 KRLAPEIGDDLVADLINADQVDEAGIYQQRERVVLLKTKLEKSSSPEAAHLLSLADVLVKKDVWIVGGDGWAYDIG 156
Cdd:cd03377    92 QKLIEKIGDEELKTLLNAWLATEDDIEESRERVAKLKPLLAAEKDELAKELLSLADYLVKKSVWIIGGDGWAYDIG 167
pyruv_ox_red TIGR02176
pyruvate:ferredoxin (flavodoxin) oxidoreductase, homodimeric; This model represents a single ...
 1-156 1.97e-69

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: 226.57  E-value: 1.97e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096027763    1 CGETPYLKLLSQLFGDRSLIANATGCSSIYGGNLPTTPWTKNADGRGPAWSNSLLEDNAEFGLGMRVALDKRVEYAFEIL 80
Cdd:TIGR02176  811 CGETPYVKLLTQLFGDRMVIANATGCSSIWGASAPSTPYTTNEQGQGPAWSNSLFEDNAEFGYGMRLSMDKRRERLAELA 890

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096027763   81 KR-LAPEIGDDLVADLINADQVDEAGIYQQRERVVLLKTKLEKSSSPEAAHLLSLADVLVKKDVWIVGGDGWAYDIG 156
Cdd:TIGR02176  891 AKaLESDIASGDLKAALNGWLAGKNDIEKSKERVAKLKKLLAGEKDDLLKEIYAVSDLFVKKSVWIIGGDGWAYDIG 967
TPP_PFOR cd02018
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ...
 1-156 5.47e-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: 72.13  E-value: 5.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096027763   1 CGETPYLKLLSQLFG--DRSLIANATGCSSIYGGNLPTTPWtknadgrGPAWSNSLLEDNAEFGLGMrvaldkrveyaFE 78
Cdd:cd02018    11 CGEVTAVRVVLAALPapEDTVIANSTGCSSVYASTAPFNSW-------AVPWVNSLFEDANAVASGL-----------KR 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2096027763  79 ILKRLAPEigddlvadlinadqvdeagiyqqrervvllktklekssspeaahllsLADVLVKKDVWIVGGDGWAYDIG 156
Cdd:cd02018    73 GLKARFPK-----------------------------------------------DRELDKKKDVVVIGGDGATYDIG 103
TPP_PFOR_porB_like cd03376
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ...
 1-72 5.17e-06

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: 44.54  E-value: 5.17e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2096027763   1 CGETPYLKLLSQLFGDRSLIANATGCSSIYGGNLPTTPWtknadgRGPaWSNSLLEDNAEFGLGMRVALDKR 72
Cdd:cd03376    11 CGAALALRHVLKALGPDTVVVNPTGCLEVITTPYPYTAW------RVP-WIHVAFENAAAVASGIEAALKAL 75
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 1-156 5.71e-06

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: 44.36  E-value: 5.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096027763   1 CGETPYLKLLSQLF-----GDRSLIANATGCSSIYggnlpTTPWTKNadgrgpaWSNSLLEDNAEFGLGMRVALDKRVey 75
Cdd:COG1013    19 CGHGIILRLLLKALdelldGDKTVVVSGIGCSSVA-----PGYFNVP-------GFHTLHGRAAAVATGIKLANPDLT-- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096027763  76 afeilkrlapeigddlvadlinadqvdeagiyqqrervvllktklekssspeaahllsladvlvkkdVWIVGGDGWAYDI 155
Cdd:COG1013    85 -------------------------------------------------------------------VIVFGGDGDTYDI 97


                  .
gi 2096027763 156 G 156
Cdd:COG1013    98 G 98
PRK11865 PRK11865
pyruvate synthase subunit beta;
1-72 7.69e-05

pyruvate synthase subunit beta;


Pssm-ID: 183346 [Multi-domain]  Cd Length: 299  Bit Score: 41.24  E-value: 7.69e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2096027763   1 CGETPYLKLLSQLFGDRSLIANATGCSSIYGGNLPTTPWtknadgRGPaWSNSLLEDNAEFGLGMRVALDKR 72
Cdd:PRK11865   24 CGAAIAMRLALKALGKNTVIVVATGCLEVITTPYPETAW------NVP-WIHVAFENAAAVASGIERAVKAL 88
 
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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