ID   IDH_STRMU               Reviewed;         393 AA.
AC   Q59940; Q59927;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 132.
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=idh; OrderedLocusNames=SMU_672;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=JH1005;
RA   Cvitkovitch D.G., Gutierrez J.A., Bleiweis A.S.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-224.
RC   STRAIN=JH1005;
RA   Gutierrez J.A., Crowley P.J., Brown D.P., Hillman J.D., Youngman P.,
RA   Bleiweis A.S.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
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; U62799; AAC44826.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN58406.1; -; Genomic_DNA.
DR   EMBL; U48886; AAC44503.1; -; Genomic_DNA.
DR   RefSeq; NP_721100.1; NC_004350.2.
DR   RefSeq; WP_002261869.1; NC_004350.2.
DR   AlphaFoldDB; Q59940; -.
DR   SMR; Q59940; -.
DR   STRING; 210007.SMU_672; -.
DR   PRIDE; Q59940; -.
DR   EnsemblBacteria; AAN58406; AAN58406; SMU_672.
DR   KEGG; smu:SMU_672; -.
DR   PATRIC; fig|210007.7.peg.597; -.
DR   eggNOG; COG0538; Bacteria.
DR   HOGENOM; CLU_031953_7_1_9; -.
DR   OMA; CVRPCRY; -.
DR   PhylomeDB; Q59940; -.
DR   Proteomes; UP000002512; 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; 2.
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; Phosphoprotein; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..393
FT                   /note="Isocitrate dehydrogenase [NADP]"
FT                   /id="PRO_0000083568"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   SITE            149
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            219
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         102
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        67
FT                   /note="N -> K (in Ref. 1; AAC44826)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        383
FT                   /note="R -> C (in Ref. 1; AAC44826)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   393 AA;  43141 MW;  0F19F22A93D9DCD6 CRC64;
     MAEKVSFEEG KLQVPDKPVI PYIEGDGVGQ DIWKNAQIVF DKAIAKVYGG HKQVIWREVL
     AGKKAYNETG NWLPNETLEI IKTHLLAIKG PLETPVGGGI RSLNVALRQE LDLFACVRPV
     RYFKGVPSPL KHPEKTAITI FRENTEDIYA GIEWNAGTAE VQKVINFLQD DMQVKKIRFP
     KSSSIGIKPI SIEGSQRLIR AAIEYALANN LTKVTLVHKG NIQKFTEGGF RKWGYELAKR
     EYAAELASGQ LVVDDIIADN FLQQILLKPE RFDVVALTNL NGDYASDALA AQVGGIGISP
     GANINYQTGH AIFEATHGTA PDIAGQDLAN PSSVLLSGCM LFDYIGWSKV SDLIMKAVEK
     AIANGQVTID FAKELGVEAL TTRQFSEVLL TYL