ID   PORC_METBF              Reviewed;         182 AA.
AC   P80523; Q46DS2;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Pyruvate synthase subunit PorC;
DE            EC=1.2.7.1;
DE   AltName: Full=Pyruvate oxidoreductase gamma chain;
DE            Short=POR;
DE   AltName: Full=Pyruvic-ferredoxin oxidoreductase subunit gamma;
GN   Name=porC; OrderedLocusNames=Mbar_A1002;
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 1-31.
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; AAZ69970.1; -; Genomic_DNA.
DR   PIR; S65418; S65418.
DR   RefSeq; WP_011306019.1; NC_007355.1.
DR   AlphaFoldDB; P80523; -.
DR   SMR; P80523; -.
DR   STRING; 269797.Mbar_A1002; -.
DR   EnsemblBacteria; AAZ69970; AAZ69970; Mbar_A1002.
DR   GeneID; 3626885; -.
DR   KEGG; mba:Mbar_A1002; -.
DR   eggNOG; arCOG01603; Archaea.
DR   HOGENOM; CLU_087284_2_0_2; -.
DR   OMA; PDYVIVQ; -.
DR   OrthoDB; 95610at2157; -.
DR   BRENDA; 1.2.7.1; 3250.
DR   GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.920.10; -; 1.
DR   InterPro; IPR011894; PorC_KorC.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   Pfam; PF01558; POR; 1.
DR   SUPFAM; SSF53323; SSF53323; 1.
DR   TIGRFAMs; TIGR02175; PorC_KorC; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Oxidoreductase.
FT   CHAIN           1..182
FT                   /note="Pyruvate synthase subunit PorC"
FT                   /id="PRO_0000097128"
SQ   SEQUENCE   182 AA;  19526 MW;  12FF67E4BBB4DFFB CRC64;
     MKEIRIHGRG GQGSVTAAEM LSVAAFEDGK FSQAFPAFGV ERRGAPVQAF TRINNNPIRL
     RSQVYTPDYV IVQDATLLET VDVASGVKDD GIIIVNTTEN PESLKLNTKA RVMTVDATKV
     AMDIIGVPIV NTVLLGAFAG ATGEINVESI QHAIRARFSG KVGEKNANAI QKAYKLIRGE
     EA