ID A5UKN5_METS3 Unreviewed; 80 AA.
AC A5UKN5;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Pyruvate:ferredoxin oxidoreductase, delta subunit, PorD {ECO:0000313|EMBL:ABQ86763.1};
DE EC=1.2.7.1 {ECO:0000313|EMBL:ABQ86763.1};
GN OrderedLocusNames=Msm_0558 {ECO:0000313|EMBL:ABQ86763.1};
OS Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=420247 {ECO:0000313|EMBL:ABQ86763.1, ECO:0000313|Proteomes:UP000001992};
RN [1] {ECO:0000313|EMBL:ABQ86763.1, ECO:0000313|Proteomes:UP000001992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS
RC {ECO:0000313|Proteomes:UP000001992};
RX PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT human gut.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP000678; ABQ86763.1; -; Genomic_DNA.
DR RefSeq; WP_004032311.1; NZ_CP117965.1.
DR AlphaFoldDB; A5UKN5; -.
DR STRING; 420247.Msm_0558; -.
DR EnsemblBacteria; ABQ86763; ABQ86763; Msm_0558.
DR GeneID; 78817185; -.
DR KEGG; msi:Msm_0558; -.
DR PATRIC; fig|420247.28.peg.556; -.
DR eggNOG; arCOG01605; Archaea.
DR HOGENOM; CLU_139698_1_1_2; -.
DR BioCyc; MSMI420247:GHWZ-567-MONOMER; -.
DR Proteomes; UP000001992; Chromosome.
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 Gene3D; 3.30.70.20; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR011898; PorD_KorD.
DR NCBIfam; NF040684; PorD_Arch; 1.
DR NCBIfam; TIGR02179; PorD_KorD; 1.
DR PANTHER; PTHR43724; PYRUVATE SYNTHASE SUBUNIT PORD; 1.
DR PANTHER; PTHR43724:SF1; PYRUVATE SYNTHASE SUBUNIT PORD; 1.
DR Pfam; PF14697; Fer4_21; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:ABQ86763.1};
KW Pyruvate {ECO:0000313|EMBL:ABQ86763.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 25..50
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 51..80
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 80 AA; 8875 MW; 723A35437C52D504 CRC64;
MVAIGCVIKT PGSSKNNKTG SWRTFKPILD KEKCIDCDNC IIFCPDSSVN KQHDINYDYC
KGCGICAHEC PSDAIEMIKE
//