ID   IDH1_COLMA              Reviewed;         415 AA.
AC   P41560;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] 1;
DE            EC=1.1.1.42;
DE   AltName: Full=IDH-I;
DE   AltName: Full=IDP-1;
DE   AltName: Full=NADP(+)-specific ICDH 1;
DE   AltName: Full=Oxalosuccinate decarboxylase 1;
GN   Name=icdI;
OS   Colwellia maris.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=77524;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8226630; DOI=10.1128/jb.175.21.6873-6880.1993;
RA   Ishii A., Suzuki M., Sahara T., Takada Y., Sasaki S., Fukunaga N.;
RT   "Genes encoding two isocitrate dehydrogenase isozymes of a psychrophilic
RT   bacterium, Vibrio sp. strain ABE-1.";
RL   J. Bacteriol. 175:6873-6880(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-41.
RX   PubMed=1295895; DOI=10.1093/oxfordjournals.jbchem.a123988;
RA   Fukunaga N., Imagawa S., Sahara T., Ishii A., Suzuki M.;
RT   "Purification and characterization of monomeric isocitrate dehydrogenase
RT   with NADP(+)-specificity from Vibrio parahaemolyticus Y-4.";
RL   J. Biochem. 112:849-855(1992).
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.
CC   -!- INDUCTION: By acetate.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000305}.
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DR   EMBL; D14047; BAA03135.1; -; Genomic_DNA.
DR   PIR; B49341; B49341.
DR   AlphaFoldDB; P41560; -.
DR   SMR; P41560; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Glyoxylate bypass; Magnesium; Manganese;
KW   Metal-binding; NADP; Oxidoreductase; Phosphoprotein;
KW   Tricarboxylic acid cycle.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1295895"
FT   CHAIN           2..415
FT                   /note="Isocitrate dehydrogenase [NADP] 1"
FT                   /id="PRO_0000083550"
FT   BINDING         104
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         339..345
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         352
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         390
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         394
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            160
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   SITE            230
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         113
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        26
FT                   /note="N -> G (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   415 AA;  45145 MW;  353EFF202824696E CRC64;
     MTNKIIIPTT GDKITFIDGK LSVPNNPIIP YIEGDGIGVD VTPPMLKVVN AAVAKAYGGD
     RKIEWLEVYA GEKATKMYDS ETWLPEETLN ILQEYKVSIK GPLTTPVGGG MSSLNVAIRQ
     MLDLYVCQRP VQWFTGVPSP VKRPSEVDMV IFRENTEDIY AGIEYKAGSD KAKSVIKFLI
     EEMGASNIRF TENCGIGIKP VSKEGSQRLV RQAIQYAIDN NKDSVTLVHK GNIMKFTEGA
     FKDWGYELAI EEFGASLLHG GPWCSLKNPN TGKEIIIKDV IADAMLQQVL LRPAEYSVIA
     TLNLNGDYLS DALAAQVGGI GIAPGANLGD EVAVFEATHG TAPKYAGKNK VNPGSVILSA
     EMMLRHMGWL EADLLLKGMS GAIQAKTVTY DFERLMDDAT LVSCSAFGDC IIDHM