ID   PORD_METBF              Reviewed;          95 AA.
AC   P80524; Q46DS3;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Pyruvate synthase subunit PorD;
DE   AltName: Full=Pyruvate oxidoreductase delta chain;
DE            Short=POR;
DE   AltName: Full=Pyruvic-ferredoxin oxidoreductase subunit delta;
GN   Name=porD; OrderedLocusNames=Mbar_A1001;
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 1-30.
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P94692};
CC       Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250|UniProtKB:P94692};
CC   -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one gamma
CC       chain.
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DR   EMBL; CP000099; AAZ69969.1; -; Genomic_DNA.
DR   PIR; S65419; S65419.
DR   RefSeq; WP_011306018.1; NC_007355.1.
DR   AlphaFoldDB; P80524; -.
DR   SMR; P80524; -.
DR   STRING; 269797.Mbar_A1001; -.
DR   EnsemblBacteria; AAZ69969; AAZ69969; Mbar_A1001.
DR   GeneID; 3626884; -.
DR   KEGG; mba:Mbar_A1001; -.
DR   eggNOG; arCOG01605; Archaea.
DR   HOGENOM; CLU_139698_1_1_2; -.
DR   OMA; HDDRCIR; -.
DR   OrthoDB; 125632at2157; -.
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:0016625; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor; IEA:InterPro.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR011898; PorD_KorD.
DR   PANTHER; PTHR43724; PTHR43724; 1.
DR   TIGRFAMs; TIGR02179; PorD_KorD; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Repeat; Transport.
FT   CHAIN           1..95
FT                   /note="Pyruvate synthase subunit PorD"
FT                   /id="PRO_0000097127"
FT   DOMAIN          34..63
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          64..93
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         43
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         46
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         49
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         53
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         73
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         76
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         79
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
FT   BINDING         83
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P94692"
SQ   SEQUENCE   95 AA;  10813 MW;  B5339CAD1100C527 CRC64;
     MKNEGEKEGL NISRCRVCKP GSTLINKTGG WRNFRPVYIY EKCTKCGICH IVCPDMSVKP
     RENGFFEYDY DYCKGCGICA NECPADAIEM ILEEK