IDH_NOSS1
ID IDH_NOSS1 Reviewed; 473 AA.
AC P50214;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
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; OrderedLocusNames=alr1827;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8169222; DOI=10.1128/jb.176.9.2718-2726.1994;
RA Muro-Pastor M.I., Florencio F.J.;
RT "NADP(+)-isocitrate dehydrogenase from the cyanobacterium Anabaena sp.
RT strain PCC 7120: purification and characterization of the enzyme and
RT cloning, sequencing, and disruption of the icd gene.";
RL J. Bacteriol. 176:2718-2726(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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; X77654; CAA54734.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB73526.1; -; Genomic_DNA.
DR PIR; A55591; A55591.
DR PIR; AE2034; AE2034.
DR RefSeq; WP_010995995.1; NZ_RSCN01000019.1.
DR AlphaFoldDB; P50214; -.
DR SMR; P50214; -.
DR STRING; 103690.17130917; -.
DR EnsemblBacteria; BAB73526; BAB73526; BAB73526.
DR KEGG; ana:alr1827; -.
DR eggNOG; COG0538; Bacteria.
DR OMA; CVRPCRY; -.
DR OrthoDB; 1551125at2; -.
DR Proteomes; UP000002483; 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; Phosphoprotein; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..473
FT /note="Isocitrate dehydrogenase [NADP]"
FT /id="PRO_0000083547"
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 362
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 394..400
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 446
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 450
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 237
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 473 AA; 52228 MW; D30941B992A38AAB CRC64;
MYNKITPPTT GEKITFKNGE PVVPDNPIIP FIRGDGTGID IWPATEKVLD AAVAKAYQGK
RKISWFKVYA GDEACDLYGT YQYLPEDTLT AIREYGVAIK GPLTTPVGGG IRSLNVALRQ
IFDLYACVRP CRYYAGTPSP HKNPEKLDVI VYRENTEDIY LGIEWKQGSE IGDRLISILN
KELIPATPEH GKKQIPLDSG IGIKPISKTG SQRLVRRAIK HALTLPKDKQ QVTLVHKGNI
MKYTEGAFRD WGYELATSEF RQETVTERES WILSNKEKNP NISLEDNARQ IDPGFDALTP
EKKAQIVKEV ETVLNSIWES HGNGKWKEKV LVNDRIADSI FQQIQTRPDE YSILATMNLN
GDYLSDAAAA IVGGLGMGPG ANIGDSCAVF EATHGTAPKH AGLDRINPGS VILSGVMMLE
YMGWQEAADL IKKGLSDAIA NSQVTYDLAR LLEPPVEPLK CSEFADAIIK HFG
