VORD_PYRFU
ID VORD_PYRFU Reviewed; 105 AA.
AC Q51800;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Ketoisovalerate oxidoreductase subunit VorD;
DE Short=VOR;
DE EC=1.2.7.7;
DE AltName: Full=2-oxoisovalerate ferredoxin reductase subunit delta;
DE AltName: Full=2-oxoisovalerate oxidoreductase delta chain;
GN Name=vorD; OrderedLocusNames=PF0970;
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 1-15.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-2-oxobutanoate + CoA + 2 oxidized [2Fe-2S]-
CC [ferredoxin] = 2-methylpropanoyl-CoA + CO2 + H(+) + 2 reduced [2Fe-
CC 2S]-[ferredoxin]; Xref=Rhea:RHEA:11712, Rhea:RHEA-COMP:10000,
CC Rhea:RHEA-COMP:10001, ChEBI:CHEBI:11851, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57338; EC=1.2.7.7;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250};
CC -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one gamma
CC chain.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X85250; CAA59501.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81094.1; -; Genomic_DNA.
DR PIR; T45084; T45084.
DR RefSeq; WP_011012107.1; NC_018092.1.
DR AlphaFoldDB; Q51800; -.
DR SMR; Q51800; -.
DR STRING; 186497.PF0970; -.
DR PRIDE; Q51800; -.
DR EnsemblBacteria; AAL81094; AAL81094; PF0970.
DR GeneID; 41712782; -.
DR KEGG; pfu:PF0970; -.
DR PATRIC; fig|186497.12.peg.1029; -.
DR eggNOG; arCOG01605; Archaea.
DR HOGENOM; CLU_139698_1_1_2; -.
DR OMA; HDDRCIR; -.
DR OrthoDB; 125632at2157; -.
DR PhylomeDB; Q51800; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0043807; F:3-methyl-2-oxobutanoate dehydrogenase (ferredoxin) activity; IEA:UniProtKB-EC.
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 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; Oxidoreductase; Reference proteome; Repeat; Transport.
FT CHAIN 1..105
FT /note="Ketoisovalerate oxidoreductase subunit VorD"
FT /id="PRO_0000099962"
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:0000255"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 63
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 83
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 86
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 89
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 93
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
SQ SEQUENCE 105 AA; 11851 MW; F609078E069DB899 CRC64;
MNTLFGKTKE EAKPIVLKSV DEYPEAPISL GTTLVNPTGD WRTFKPVVNE EKCVKCYICW
KYCPEPAIYI KPDGYVAIDY DYCKGCGICA NECPTKAITM IKEEK
