IDH1_COLMA
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