ID A0A0C1UGX0_9CLOT Unreviewed; 98 AA.
AC A0A0C1UGX0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Ketoisovalerate oxidoreductase subunit vorD {ECO:0000313|EMBL:KIE46660.1};
DE EC=1.2.7.7 {ECO:0000313|EMBL:KIE46660.1};
GN Name=vorD {ECO:0000313|EMBL:KIE46660.1};
GN ORFNames=U732_3286 {ECO:0000313|EMBL:KIE46660.1};
OS Clostridium argentinense CDC 2741.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1418104 {ECO:0000313|EMBL:KIE46660.1, ECO:0000313|Proteomes:UP000031366};
RN [1] {ECO:0000313|EMBL:KIE46660.1, ECO:0000313|Proteomes:UP000031366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 2741 {ECO:0000313|EMBL:KIE46660.1,
RC ECO:0000313|Proteomes:UP000031366};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(2014).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIE46660.1}.
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DR EMBL; AYSO01000016; KIE46660.1; -; Genomic_DNA.
DR RefSeq; WP_039632954.1; NZ_AYSO01000016.1.
DR AlphaFoldDB; A0A0C1UGX0; -.
DR STRING; 29341.RSJ17_19510; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000031366; Unassembled WGS sequence.
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 Gene3D; 3.30.70.20; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR011898; PorD_KorD.
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; 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:KIE46660.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031366};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 39..68
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 70..97
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 98 AA; 11327 MW; D19314D39805B625 CRC64;
MNKPRLRQYK KPSHISEYPL GPCYKAGHLV TKNAGWRNEK PIIDHEKCVN CLQCYMYCPD
GVIFKKDNNI DIDYDFCKGC GICAKVCIPK AIKMEREV
//
