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Conserved domains on  [gi|808215773|gb|AKD27790|]
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pyruvate:ferredoxin oxidoreductase subunit beta, partial [Thermococcus sp. MV12]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11865 super family cl32732
pyruvate synthase subunit beta;
1-84 3.24e-44

pyruvate synthase subunit beta;


The actual alignment was detected with superfamily member PRK11865:

Pssm-ID: 183346 [Multi-domain]  Cd Length: 299  Bit Score: 144.09  E-value: 3.24e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215773   1 PYVATASIADPYDLYRKVKKAAKIDGPAFLQIHGPCVPGWRIPPEKTVEVAKLAIETGVWPLFEIENGDIRnIKFQRFPK 80
Cdd:PRK11865 177 PYVATASIGYPEDFMEKVKKAKEVEGPAYIQVLQPCPTGWGFPPEKTIEIGRLAVETGYWPLFEIENGKFK-ITYEPLHL 255


                 ....
gi 808215773  81 DGKF 84
Cdd:PRK11865 256 DRRT 259
 
Name Accession Description Interval E-value
PRK11865 PRK11865
pyruvate synthase subunit beta;
1-84 3.24e-44

pyruvate synthase subunit beta;


Pssm-ID: 183346 [Multi-domain]  Cd Length: 299  Bit Score: 144.09  E-value: 3.24e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215773   1 PYVATASIADPYDLYRKVKKAAKIDGPAFLQIHGPCVPGWRIPPEKTVEVAKLAIETGVWPLFEIENGDIRnIKFQRFPK 80
Cdd:PRK11865 177 PYVATASIGYPEDFMEKVKKAKEVEGPAYIQVLQPCPTGWGFPPEKTIEIGRLAVETGYWPLFEIENGKFK-ITYEPLHL 255


                 ....
gi 808215773  81 DGKF 84
Cdd:PRK11865 256 DRRT 259
TPP_PFOR_porB_like cd03376
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ...
 1-70 2.24e-41

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: 135.06  E-value: 2.24e-41
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215773   1 PYVATASIADPYDLYRKVKKAAKIDGPAFLQIHGPCVPGWRIPPEKTVEVAKLAIETGVWPLFEIENGDI 70
Cdd:cd03376  166 PYVATASVAYPEDLYKKVKKALSIEGPAYIHILSPCPTGWRFDPSKTIEIARLAVETGFWPLYEYENGKF 235
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 1-69 3.67e-25

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: 93.67  E-value: 3.67e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808215773   1 PYVATASIADPYDLYRKVKKAAKIDGPAFLQIHGPCVPGWRIPPEKTVEVAKlaieTGVWPLFEIENGD 69
Cdd:COG1013  163 TYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRDPSKTIEWAK----EGMWPLYEYDPGE 227
 
Name Accession Description Interval E-value
PRK11865 PRK11865
pyruvate synthase subunit beta;
1-84 3.24e-44

pyruvate synthase subunit beta;


Pssm-ID: 183346 [Multi-domain]  Cd Length: 299  Bit Score: 144.09  E-value: 3.24e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215773   1 PYVATASIADPYDLYRKVKKAAKIDGPAFLQIHGPCVPGWRIPPEKTVEVAKLAIETGVWPLFEIENGDIRnIKFQRFPK 80
Cdd:PRK11865 177 PYVATASIGYPEDFMEKVKKAKEVEGPAYIQVLQPCPTGWGFPPEKTIEIGRLAVETGYWPLFEIENGKFK-ITYEPLHL 255


                 ....
gi 808215773  81 DGKF 84
Cdd:PRK11865 256 DRRT 259
TPP_PFOR_porB_like cd03376
Thiamine pyrophosphate (TPP family), PFOR porB-like subfamily, TPP-binding module; composed of ...
 1-70 2.24e-41

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: 135.06  E-value: 2.24e-41
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215773   1 PYVATASIADPYDLYRKVKKAAKIDGPAFLQIHGPCVPGWRIPPEKTVEVAKLAIETGVWPLFEIENGDI 70
Cdd:cd03376  166 PYVATASVAYPEDLYKKVKKALSIEGPAYIHILSPCPTGWRFDPSKTIEIARLAVETGFWPLYEYENGKF 235
PRK11864 PRK11864
3-methyl-2-oxobutanoate dehydrogenase subunit beta;
1-71 8.49e-39

3-methyl-2-oxobutanoate dehydrogenase subunit beta;


Pssm-ID: 237005 [Multi-domain]  Cd Length: 300  Bit Score: 130.21  E-value: 8.49e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808215773   1 PYVATASIADPYDLYRKVKKAAKIDGPAFLQIHGPCVPGWRIPPEKTVEVAKLAIETGVWPLFEIENGDIR 71
Cdd:PRK11864 173 PYVATASIAYPEDFIRKLKKAKEIRGFKFIHLLAPCPPGWRFDPDKTIEIARLAVETGVWPLFEYENGKFK 243
PorB COG1013
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, beta ...
 1-69 3.67e-25

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: 93.67  E-value: 3.67e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808215773   1 PYVATASIADPYDLYRKVKKAAKIDGPAFLQIHGPCVPGWRIPPEKTVEVAKlaieTGVWPLFEIENGD 69
Cdd:COG1013  163 TYVARASVGDPKDLKKKIKKAIEHKGFSFIEVLSPCPTGWGRDPSKTIEWAK----EGMWPLYEYDPGE 227
TPP_PFOR cd02018
Thiamine pyrophosphate (TPP family), Pyruvate ferredoxin/flavodoxin oxidoreductase (PFOR) ...
 1-68 1.22e-11

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: 57.88  E-value: 1.22e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808215773   1 PYVATASIADPyDLYRKVKKAA--KIDGPAFLQIHGPCVPGWRIPPEKTVEVAKLAIETGVWPLFEIENG 68
Cdd:cd02018  168 VYVARLSPALK-KHFLKVVKEAisRTDGPTFIHAYTPCITEWGIGSGKSLELARKAVKSRMFPLFEYDPR 236
TPP_PFOR_PNO cd03377
Thiamine pyrophosphate (TPP family), PFOR_PNO subfamily, TPP-binding module; composed of ...
 2-63 5.66e-06

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: 42.21  E-value: 5.66e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808215773   2 YVATASI-ADPYDLYRKVKKAAKIDGPAFLQIHGPCVP-GWRIPPEKTVEVAKLAIETGVWPLF 63
Cdd:cd03377  233 YVAQIALgANDNQTLKAFREAEAYDGPSLIIAYSPCIAhGIKGGMTKSQEQQKLAVESGYWPLY 296
TPP_OGFOR cd03375
Thiamine pyrophosphate (TPP family), 2-oxoglutarate ferredoxin oxidoreductase (OGFOR) ...
 2-37 1.53e-03

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: 35.19  E-value: 1.53e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 808215773   2 YVATASIADPYDLYRKVKKAAKIDGPAFLQIHGPCV 37
Cdd:cd03375  151 FVARGFSGDIKQLKEIIKKAIQHKGFSFVEVLSPCP 186
 
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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