ID   PORB_METBF              Reviewed;         296 AA.
AC   P80522; Q46DS5;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Pyruvate synthase subunit PorB;
DE            EC=1.2.7.1;
DE   AltName: Full=Pyruvate oxidoreductase beta chain;
DE            Short=POR;
DE   AltName: Full=Pyruvic-ferredoxin oxidoreductase subunit beta;
GN   Name=porB; OrderedLocusNames=Mbar_A0999;
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 2-35.
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P94692};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000250|UniProtKB:P94692};
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; AAZ69967.1; -; Genomic_DNA.
DR   PIR; S65417; S65417.
DR   RefSeq; WP_011306016.1; NC_007355.1.
DR   AlphaFoldDB; P80522; -.
DR   SMR; P80522; -.
DR   STRING; 269797.Mbar_A0999; -.
DR   EnsemblBacteria; AAZ69967; AAZ69967; Mbar_A0999.
DR   GeneID; 3626882; -.
DR   KEGG; mba:Mbar_A0999; -.
DR   eggNOG; arCOG01601; Archaea.
DR   HOGENOM; CLU_058423_0_0_2; -.
DR   OMA; ATGCMEV; -.
DR   OrthoDB; 29720at2157; -.
DR   BRENDA; 1.2.7.1; 3250.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR011766; TPP_enzyme-bd_C.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW   Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8620891"
FT   CHAIN           2..296
FT                   /note="Pyruvate synthase subunit PorB"
FT                   /id="PRO_0000097126"
FT   REGION          140..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         17
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         20
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         45
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         210
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
SQ   SEQUENCE   296 AA;  32056 MW;  C040A6216787AC14 CRC64;
     MSKTAPKTYI TSGHSGCAGC CDAFAAKFTL MGAGPNTIVI NPTGCLEVMS TPFPYSSWQV
     PWIHSLFENA GAVASGVEAA LKALGKKDDV KVVSIGGDGS TMDIGLGALS GAFERGHDFT
     YVCMDNEAYM NTGVQRSSGT PFDASTTTTP AGKVSFGNPR PKKNMPAIMA AHGSPYVATT
     SIGFPRDMIR KVKKATEIVG PTYIHAQAPC PTGWGFDTSK TLEIAKLAVE TCLWPMYEME
     NGEITQVRKV KNPRPVEEYL RAQKRFKHLF TMEGGEEEIK KIQAIADWNI KHFELQ