ID H6QC12_PYROT Unreviewed; 314 AA.
AC H6QC12;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN OrderedLocusNames=Pogu_2777 {ECO:0000313|EMBL:AFA40804.1};
OS Pyrobaculum oguniense (strain DSM 13380 / JCM 10595 / TE7).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=698757 {ECO:0000313|EMBL:AFA40804.1, ECO:0000313|Proteomes:UP000009062};
RN [1] {ECO:0000313|EMBL:AFA40804.1, 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; AFA40804.1; -; Genomic_DNA.
DR AlphaFoldDB; H6QC12; -.
DR STRING; 698757.Pogu_2777; -.
DR KEGG; pog:Pogu_2777; -.
DR eggNOG; arCOG01051; Archaea.
DR HOGENOM; CLU_009227_1_1_2; -.
DR Proteomes; UP000009062; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0018491; F:2-oxobutyrate synthase activity; IEA:UniProt.
DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProt.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR PANTHER; PTHR43825:SF1; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:AFA40804.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 61..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 7..172
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 314 AA; 34041 MW; A3FEDD7FE0BA5010 CRC64;
MLDIGSLTPR DALGKALADL GDLRKDVVVL VADTGETTRA KFFAERHPER FFNVGIAEQS
LVGIAAGLAL AGFMPYALTF AAFMTRAWEQ ARNSVDRMAL PVRLVGTHAG FADAYDGPSH
QALEDIALFR VLQNFTVLAP ADSCEVYRVV TASAALKGPV YIRVGRDFHI PSTCELYDRF
EVGKAYVVFD GSDVAIFTTG VVLPFAIEAA QLLRDRGISA AVIHFPSVKP LDYAAVEKYA
SATGAVLTVE EHMVYGGFGS AVAEYLSQTR PTKMAIMGLK SYGRTAKSPQ ELYQYFGLTP
ENIAARAEEL VKLK
//
