PORD_PYRFU
ID PORD_PYRFU Reviewed; 105 AA.
AC Q51803;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 130.
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=PF0967;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-18.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=8550425; DOI=10.1128/jb.178.1.248-257.1996;
RA Kletzin A., Adams M.W.W.;
RT "Molecular and phylogenetic characterization of pyruvate and 2-
RT ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and
RT pyruvate ferredoxin oxidoreductase from Thermotoga maritima.";
RL J. Bacteriol. 178:248-257(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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; X85250; CAA59504.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81091.1; -; Genomic_DNA.
DR PIR; T45087; T45087.
DR RefSeq; WP_011012104.1; NC_018092.1.
DR AlphaFoldDB; Q51803; -.
DR SMR; Q51803; -.
DR STRING; 186497.PF0967; -.
DR EnsemblBacteria; AAL81091; AAL81091; PF0967.
DR GeneID; 41712779; -.
DR KEGG; pfu:PF0967; -.
DR PATRIC; fig|186497.12.peg.1026; -.
DR eggNOG; arCOG01605; Archaea.
DR HOGENOM; CLU_139698_1_1_2; -.
DR OMA; GSWRTFK; -.
DR OrthoDB; 125632at2157; -.
DR PhylomeDB; Q51803; -.
DR BRENDA; 1.2.7.1; 5243.
DR Proteomes; UP000001013; 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: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; Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8550425"
FT CHAIN 2..105
FT /note="Pyruvate synthase subunit PorD"
FT /id="PRO_0000099922"
FT DOMAIN 44..73
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 74..103
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 63
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="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 86
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 89
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P94692"
FT BINDING 93
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P94692"
SQ SEQUENCE 105 AA; 12012 MW; 2A7B549C5CBDD0ED CRC64;
MAESPFKADI ERAQKELSEK MTPGAIVYIP GSSVINKTGS WRVFKPEFNR DKCVRCYLCY
IYCPEPAIYL DEEGYPVFDY DYCKGCGICA NECPTKAIEM VREVK
