ID   PORA_METBF              Reviewed;         402 AA.
AC   P80521; Q46DS4;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   25-MAY-2022, entry version 118.
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=Mbar_A1000;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-38.
RX   PubMed=8620891; DOI=10.1111/j.1432-1033.1996.0035n.x;
RA   Bock A.-K., Kunow J., Glasemacher J., Schoenheit P.;
RT   "Catalytic properties, molecular composition and sequence alignments of
RT   pyruvate: ferredoxin oxidoreductase from the methanogenic archaeon
RT   Methanosarcina barkeri (strain Fusaro).";
RL   Eur. J. Biochem. 237:35-44(1996).
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.
CC   -!- MISCELLANEOUS: It also catalyzes the oxidation of 2-oxobutyrate.
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DR   EMBL; CP000099; AAZ69968.1; -; Genomic_DNA.
DR   PIR; S65416; S65416.
DR   RefSeq; WP_011306017.1; NC_007355.1.
DR   AlphaFoldDB; P80521; -.
DR   SMR; P80521; -.
DR   STRING; 269797.Mbar_A1000; -.
DR   EnsemblBacteria; AAZ69968; AAZ69968; Mbar_A1000.
DR   GeneID; 3626883; -.
DR   KEGG; mba:Mbar_A1000; -.
DR   eggNOG; arCOG01608; Archaea.
DR   HOGENOM; CLU_002569_5_0_2; -.
DR   OMA; YFEHKVQ; -.
DR   OrthoDB; 29908at2157; -.
DR   BRENDA; 1.2.7.1; 3250.
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.
FT   CHAIN           1..402
FT                   /note="Pyruvate synthase subunit PorA"
FT                   /id="PRO_0000097125"
SQ   SEQUENCE   402 AA;  44503 MW;  D7DA8CA3AF2143B6 CRC64;
     MIDPAYRKKM VVVEGSYAVA HSAKVCRPNV ISAYPITPQT HIVEHLSQFM ADGEIPNCEY
     VNVEAEFSAI SALIGASAVG ARTYSATTSQ GLLLMHEALF NTSGMRLPVV MTVANRAVSA
     PINIWNDHQD AIAQRDTGWM QLYVEDVQEA CDTLPQLYKI AEDNEIMVPG MVCMDGFILS
     HVYEPVVLLE QDLTDNFLPP FQPEDILDPE DPKTFGAFAS PDTYEEFRYL HEQAMQKALP
     KIEATAKEFE EVYGRYHGGL IDGYMLDDAE IVVMAMGSIL GTVKDVVDKY RAKGEKIGVL
     KVRSFRPFPK EQICKAVKNA HAVVVLDKNI SIGTNEGALF TETKSCLYNS KVRVPVIGYT
     IGHGGRDIPV ESIAKVIEET KKVAKSGITI ESQFMDLKEE LL