IDH_STAES
ID IDH_STAES Reviewed; 422 AA.
AC Q8CNX4;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Isocitrate dehydrogenase [NADP];
DE Short=IDH;
DE EC=1.1.1.42;
DE AltName: Full=IDP;
DE AltName: Full=NADP(+)-specific ICDH;
DE AltName: Full=Oxalosuccinate decarboxylase;
GN Name=icd; Synonyms=citC; OrderedLocusNames=SE_1370;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; AE015929; AAO04969.1; -; Genomic_DNA.
DR RefSeq; NP_764925.1; NC_004461.1.
DR RefSeq; WP_001830826.1; NZ_WBME01000042.1.
DR AlphaFoldDB; Q8CNX4; -.
DR SMR; Q8CNX4; -.
DR STRING; 176280.SE_1370; -.
DR EnsemblBacteria; AAO04969; AAO04969; SE_1370.
DR GeneID; 50018516; -.
DR KEGG; sep:SE_1370; -.
DR PATRIC; fig|176280.10.peg.1338; -.
DR eggNOG; COG0538; Bacteria.
DR HOGENOM; CLU_031953_7_1_9; -.
DR OMA; CVRPCRY; -.
DR Proteomes; UP000001411; Chromosome.
DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004439; Isocitrate_DH_NADP_dimer_prok.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR PANTHER; PTHR43504; PTHR43504; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00183; prok_nadp_idh; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 3: Inferred from homology;
KW Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP;
KW Oxidoreductase; Tricarboxylic acid cycle.
FT CHAIN 1..422
FT /note="Isocitrate dehydrogenase [NADP]"
FT /id="PRO_0000083565"
FT BINDING 94
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 344..350
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 396
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 150
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 220
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 422 AA; 46619 MW; 31EA599CF275A83C CRC64;
MSAEKITQSK DGLNVPNEPI IPFIIGDGIG PDIWKAASRV IDAAVEKAYN GEKRIEWKEV
LAGQKAYDET GEWLPQETLE TIKEYLIAVK GPLTTPIGGG IRSLNVALRQ ELDLFTCLRP
VRWFKGVPSP VKRPEDVDMV IFRENTEDIY AGIEFKQGTS EVKKVIDFLQ NEMGATNIRF
PETSGIGIKP VSKEGTERLV RAAIQYALDN NRKSVTLVHK GNIMKFTEGS FKQWGYDLAH
NEFGDKVFTW QQYDEIVEQK GKDAANEAQS KAEQEGKIII KDSIADIFLQ QILTRPAEHD
VVATMNLNGD YISDALAAQV GGIGIAPGAN INYETGHAIF EATHGTAPKY AGLNKVNPSS
EILSSVLMLE HLGWQEAADK ITDSIEATIA SKIVTYDFAR LMDGAKEVST SDFADELIKN
IR
