ID A1RRC2_PYRIL Unreviewed; 336 AA.
AC A1RRC2;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=2-oxoacid oxidoreductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012691};
DE EC=1.2.7.11 {ECO:0000256|ARBA:ARBA00012691};
GN OrderedLocusNames=Pisl_0326 {ECO:0000313|EMBL:ABL87504.1};
OS Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=384616 {ECO:0000313|EMBL:ABL87504.1, ECO:0000313|Proteomes:UP000002595};
RN [1] {ECO:0000313|Proteomes:UP000002595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4184 / JCM 9189 / GEO3 {ECO:0000313|Proteomes:UP000002595};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.;
RT "Complete sequence of Pyrobaculum islandicum DSM 4184.";
RL Submitted (DEC-2006) 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; CP000504; ABL87504.1; -; Genomic_DNA.
DR RefSeq; WP_011762081.1; NC_008701.1.
DR AlphaFoldDB; A1RRC2; -.
DR STRING; 384616.Pisl_0326; -.
DR GeneID; 4617309; -.
DR KEGG; pis:Pisl_0326; -.
DR eggNOG; arCOG01601; Archaea.
DR HOGENOM; CLU_058423_0_0_2; -.
DR OrthoDB; 296931at2157; -.
DR Proteomes; UP000002595; 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; PYRUVATE SYNTHASE SUBUNIT PORB; 1.
DR PANTHER; PTHR42897:SF2; 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:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABL87504.1}; Pyruvate {ECO:0000313|EMBL:ABL87504.1}.
FT DOMAIN 63..231
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 336 AA; 37162 MW; 76F457AFB3874A43 CRC64;
MVKTAVKAAE EYEGQYEYAT FELPNEELFL PGHGLCAGCT IGVIARHMLK VFGPDTVIIN
PTGCAEVSTV VYPRTNWAVP WIHVAFGNGG SVASGIEAAI KALKRRGVID PNRRINVVVF
AGDGGTADIG FQALSGMLER GHKVIYVMYD NEGYMNTGIQ RSGTTPFGAS TTTSPAGKVV
PGNIRHKKPM AAIAAAHGIP YVATANPAYV HDMVYKFKKA MEVNGPSFIH ILQSCTPGWR
FEPKYAIRVL ELATETGYWV NYEIENGEFR VTLPVPRRKH VKCFLQLQGR FRHLKPDEIE
YIQKVIDRDV EEINRLMGRE VIGPLDPSLP CLTERK
//
