ID I2JY77_DEKBR Unreviewed; 138 AA.
AC I2JY77;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Isocitrate dehydrogenase {ECO:0000313|EMBL:EIF47929.1};
GN ORFNames=AWRI1499_2158 {ECO:0000313|EMBL:EIF47929.1};
OS Brettanomyces bruxellensis AWRI1499.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Brettanomyces.
OX NCBI_TaxID=1124627 {ECO:0000313|EMBL:EIF47929.1, ECO:0000313|Proteomes:UP000004997};
RN [1] {ECO:0000313|EMBL:EIF47929.1, ECO:0000313|Proteomes:UP000004997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1499 {ECO:0000313|EMBL:EIF47929.1,
RC ECO:0000313|Proteomes:UP000004997};
RX PubMed=22470482; DOI=10.1371/journal.pone.0033840;
RA Curtin C.D., Borneman A.R., Chambers P.J., Pretorius I.S.;
RT "De-Novo Assembly and Analysis of the Heterozygous Triploid Genome of the
RT Wine Spoilage Yeast Dekkera bruxellensis AWRI1499.";
RL PLoS ONE 7:E33840-E33840(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH;
CC Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42;
CC Evidence={ECO:0000256|ARBA:ARBA00023554};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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:EIF47929.1}.
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DR EMBL; AHIQ01000120; EIF47929.1; -; Genomic_DNA.
DR Proteomes; UP000004997; Unassembled WGS sequence.
DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006102; P:isocitrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR004790; Isocitrate_DH_NADP.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR PANTHER; PTHR11822:SF21; ISOCITRATE DEHYDROGENASE [NADP], MITOCHONDRIAL; 1.
DR PANTHER; PTHR11822; NADP-SPECIFIC ISOCITRATE DEHYDROGENASE; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000004997}.
FT DOMAIN 8..136
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|Pfam:PF00180"
SQ SEQUENCE 138 AA; 15834 MW; D0D923B029982E1E CRC64;
MPADKIQVKT PIVDMDGDEM TRIIWELIKD KLIFPYLDIK LDYYDLGIEN RDXTNDKVTV
DSALATKKYG VAVKCATITP DEARVKEFGL KKMWMSPNGT IRNILGGTIF REPIVINNIP
RIIPHWEKPI VIGRHCLR
//
