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Database: UniProt/SWISS-PROT
Entry: PORA_PYRAB
LinkDB: PORA_PYRAB
Original site: PORA_PYRAB 
ID   PORA_PYRAB              Reviewed;         395 AA.
AC   Q9UYZ4; G8ZHG9;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 107.
DE   RecName: Full=Pyruvate synthase subunit PorA;
DE            EC=1.2.7.1;
DE   AltName: Full=Pyruvate oxidoreductase alpha chain;
DE            Short=POR;
DE   AltName: Full=Pyruvic-ferredoxin oxidoreductase subunit alpha;
GN   Name=porA; OrderedLocusNames=PYRAB13630; ORFNames=PAB1475;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + 2 oxidized [2Fe-2S]-[ferredoxin] + pyruvate = acetyl-CoA
CC         + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:12765,
CC         Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=1.2.7.1;
CC   -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one gamma
CC       chain.
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DR   EMBL; AJ248287; CAB50268.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE70806.1; -; Genomic_DNA.
DR   PIR; G75046; G75046.
DR   RefSeq; WP_010868478.1; NC_000868.1.
DR   AlphaFoldDB; Q9UYZ4; -.
DR   SMR; Q9UYZ4; -.
DR   STRING; 272844.PAB1475; -.
DR   GeneID; 1496752; -.
DR   KEGG; pab:PAB1475; -.
DR   PATRIC; fig|272844.11.peg.1449; -.
DR   eggNOG; arCOG01608; Archaea.
DR   HOGENOM; CLU_002569_5_0_2; -.
DR   OMA; WNDQQDS; -.
DR   OrthoDB; 372068at2157; -.
DR   PhylomeDB; Q9UYZ4; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   NCBIfam; NF040682; PorA_Arch; 1.
DR   PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   PANTHER; PTHR32154:SF0; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase.
FT   CHAIN           1..395
FT                   /note="Pyruvate synthase subunit PorA"
FT                   /id="PRO_0000099899"
SQ   SEQUENCE   395 AA;  44045 MW;  E8E09713008A8083 CRC64;
     MPIRTVMKAN EAAAWAAKLA KPKVIAAFPI TPSTLVPEKI SEFVANGELD AEFIKVESEH
     SAISALVGAS AAGVRTFTAT ASQGLALMHE VLFIAAGMRL PIVMAIGNRA LSAPINIWND
     WQDTISQRDT GWIQFYAENN QEALDLILLA YKVAEDERVL LPAMVGFDAF ILTHTVEPVE
     IPDQEVVDEF LGEYEPKHAY LDPKRPITQG TLAFPAHYME ARYLVWEAME NARKVIDEAF
     AEFEKKFGRK YQKIEEYRTD DAEIIFVTMG SLAGTLKDWV DKKREEGYKV GAAKMTVYRP
     FPVEEIRELA KKTKVLAFIE KDISMGLYGA VFTDASAALI NESEKPLMLD FIAGLGGRDV
     TFNQLDEALS IAKEALEKGK VEKPIHWIGL RKELL
//
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