ID H6Q762_PYROT Unreviewed; 299 AA.
AC H6Q762;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN OrderedLocusNames=Pogu_0429 {ECO:0000313|EMBL:AFA38456.1};
OS Pyrobaculum oguniense (strain DSM 13380 / JCM 10595 / TE7).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=698757 {ECO:0000313|EMBL:AFA38456.1, ECO:0000313|Proteomes:UP000009062};
RN [1] {ECO:0000313|EMBL:AFA38456.1, ECO:0000313|Proteomes:UP000009062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13380 / JCM 10595 / TE7
RC {ECO:0000313|Proteomes:UP000009062};
RX PubMed=23407329; DOI=10.4056/sigs.2645906;
RA Bernick D.L., Karplus K., Lui L.M., Coker J.K., Murphy J.N., Chan P.P.,
RA Cozen A.E., Lowe T.M.;
RT "Complete genome sequence of Pyrobaculum oguniense.";
RL Stand. Genomic Sci. 6:336-345(2012).
RN [2] {ECO:0000313|Proteomes:UP000009062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13380 / JCM 10595 / TE7
RC {ECO:0000313|Proteomes:UP000009062};
RA Bernick D.L., Karplus K., Lui L.M., Coker J.K.C., Murphy J.N., Cozen A.E.,
RA Chan P.P., Lowe T.M.;
RT "Complete genome sequence of Pyrobaculum oguniense.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-oxocarboxylate + CoA + 2 oxidized [2Fe-2S]-[ferredoxin] =
CC an acyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:42316, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:35179, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58342; EC=1.2.7.11;
CC Evidence={ECO:0000256|ARBA:ARBA00000005};
CC -!- SUBUNIT: Heterodimer composed of an alpha and a beta subunit.
CC {ECO:0000256|ARBA:ARBA00011631}.
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DR EMBL; CP003316; AFA38456.1; -; Genomic_DNA.
DR AlphaFoldDB; H6Q762; -.
DR STRING; 698757.Pogu_0429; -.
DR KEGG; pog:Pogu_0429; -.
DR eggNOG; arCOG01601; Archaea.
DR HOGENOM; CLU_058423_0_0_2; -.
DR Proteomes; UP000009062; Chromosome.
DR GO; GO:0018491; F:2-oxobutyrate synthase activity; IEA:UniProt.
DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProt.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd03376; TPP_PFOR_porB_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR42897:SF1; 2-OXOACID OXIDOREDUCTASE (FERREDOXIN); 1.
DR PANTHER; PTHR42897; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:AFA38456.1};
KW Pyruvate {ECO:0000313|EMBL:AFA38456.1}.
FT DOMAIN 69..202
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 299 AA; 32603 MW; 167E679340CEAF40 CRC64;
MSFRLDQLPK KRYVVPGNAA CAGCGMMIGW KILGMALGEE AVLTIPASCA SVVQGLSPKS
GIAMPILNVP FASAAAVATG IAEAFKTLGV KGHAVVWAGD GGTADIGFAT LSGAAERNSN
ILYIMYDNEA YMNTGIQRSS STPRAAWTTT TPMGKRERKK DVALLMAMHG APYVATASIA
YPQDFYRKLK RAAEVEGFKF IHLHTPCPPG WRFDPAKTVE VARLAVETGA WILWEYDNGK
FKLNPPSTIY ADKNKRKPLK EYLKLQGRFA HLTDNDIKNL EEEIDAKWQT ILALAKTFS
//
