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 27-MAR-2024, entry version 125. 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; Cyanobacteriota; Cyanophyceae; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.gene:10493845; -. DR KEGG; ana:alr1827; -. DR eggNOG; COG0538; Bacteria. DR OrthoDB; 9806254at2; -. 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 Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 2. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR004439; Isocitrate_DH_NADP_dimer_prok. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR NCBIfam; TIGR00183; prok_nadp_idh; 1. DR PANTHER; PTHR43504; ISOCITRATE DEHYDROGENASE [NADP]; 1. DR PANTHER; PTHR43504:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 1. DR Pfam; PF00180; Iso_dh; 1. DR SMART; SM01329; Iso_dh; 1. DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 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 //