PORA_PYRFU
ID PORA_PYRFU Reviewed; 396 AA.
AC Q51804;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2002, sequence version 2.
DT 25-MAY-2022, entry version 123.
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=PF0966;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 5-15.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=8550425; DOI=10.1128/jb.178.1.248-257.1996;
RA Kletzin A., Adams M.W.W.;
RT "Molecular and phylogenetic characterization of pyruvate and 2-
RT ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and
RT pyruvate ferredoxin oxidoreductase from Thermotoga maritima.";
RL J. Bacteriol. 178:248-257(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3]
RP PROTEIN SEQUENCE OF 2-32.
RX PubMed=8305426; DOI=10.1021/bi00170a019;
RA Blamey J.M., Adams M.W.W.;
RT "Characterization of an ancestral type of pyruvate ferredoxin
RT oxidoreductase from the hyperthermophilic bacterium, Thermotoga maritima.";
RL Biochemistry 33:1000-1007(1994).
RN [4]
RP CHARACTERIZATION.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=8380721; DOI=10.1016/0167-4838(93)90190-3;
RA Blamey J.M., Adams M.W.W.;
RT "Purification and characterization of pyruvate ferredoxin oxidoreductase
RT from the hyperthermophilic archaeon Pyrococcus furiosus.";
RL Biochim. Biophys. Acta 1161:19-27(1993).
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; X85250; CAA59505.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81090.1; -; Genomic_DNA.
DR PIR; T45088; T45088.
DR RefSeq; WP_011012103.1; NZ_CP023154.1.
DR AlphaFoldDB; Q51804; -.
DR SMR; Q51804; -.
DR IntAct; Q51804; 1.
DR STRING; 186497.PF0966; -.
DR EnsemblBacteria; AAL81090; AAL81090; PF0966.
DR GeneID; 41712778; -.
DR KEGG; pfu:PF0966; -.
DR PATRIC; fig|186497.12.peg.1025; -.
DR eggNOG; arCOG01608; Archaea.
DR HOGENOM; CLU_002569_5_0_2; -.
DR OMA; WNDQQDS; -.
DR OrthoDB; 29908at2157; -.
DR PhylomeDB; Q51804; -.
DR BRENDA; 1.2.7.1; 5243.
DR Proteomes; UP000001013; 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 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 Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01855; POR_N; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR SUPFAM; SSF52922; SSF52922; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Oxidoreductase; Reference proteome.
FT CHAIN 1..396
FT /note="Pyruvate synthase subunit PorA"
FT /id="PRO_0000099900"
FT CONFLICT 277
FT /note="K -> N (in Ref. 1; CAA59505)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="L -> H (in Ref. 1; CAA59505)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 44177 MW; 16204779F27B9BC3 CRC64;
MPIRKVMKAN EAAAWAAKLA KPKVIAAFPI TPSTLIPEKI SEFVANGELD AEFIKVESEH
SAISACVGAA AAGVRTFTAT ASQGLALMHE ILFIAAGMRL PIVMAIGNRA LSAPINIWND
WQDTISQRDT GWMQFYAENN QEALDLILIA YKVAEDERVL LPAMVGFDAF ILTHTVEPVE
IPDQEVVDEF LGEYEPKHAY IDPARPITQG SLAFPAHYME SRYTVWEAME RAKKVIDEAF
AEFEKKFGRK YQKIEEYKTE DADIIFVTMG SLAGTLKEWI DKKREEGYKV GAAKITVYRP
FPVEEIRELA KKAKVLAFLE KNITIGLYGA VFTDASAALI NESEKPLMVD FIVGLGGRDV
TFNQLDEALE IAEKALKEGK VENPINWIGL RWELVK