ID IDH_MYCBO Reviewed; 409 AA. AC P65098; A0A1R3Y3W8; O53389; X2BNC7; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 105. 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=BQ2027_MB3371C; OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=233413; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=12788972; DOI=10.1073/pnas.1130426100; RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J., RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.; RT "The complete genome sequence of Mycobacterium bovis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=28385856; DOI=10.1128/genomea.00157-17; RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R., RA Robbe-Austerman S., Gordon S.V.; RT "Updated reference genome sequence and annotation of Mycobacterium bovis RT AF2122/97."; RL Genome Announc. 5:E00157-E00157(2017). 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 -!- 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; LT708304; SIU02000.1; -; Genomic_DNA. DR RefSeq; NP_857016.1; NC_002945.3. DR RefSeq; WP_003417452.1; NC_002945.4. DR AlphaFoldDB; P65098; -. DR SMR; P65098; -. DR PATRIC; fig|233413.5.peg.3703; -. DR SABIO-RK; P65098; -. DR Proteomes; UP000001419; 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:0006102; P:isocitrate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR004790; Isocitrate_DH_NADP. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR NCBIfam; TIGR00127; nadp_idh_euk; 1. DR PANTHER; PTHR11822:SF21; ISOCITRATE DEHYDROGENASE [NADP], MITOCHONDRIAL; 1. DR PANTHER; PTHR11822; NADP-SPECIFIC ISOCITRATE DEHYDROGENASE; 1. DR Pfam; PF00180; Iso_dh; 1. DR PIRSF; PIRSF000108; IDH_NADP; 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..409 FT /note="Isocitrate dehydrogenase [NADP]" FT /id="PRO_0000083554" FT BINDING 78..80 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 80 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 85 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 97..103 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 112 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 135 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 255 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 263 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 278 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 313..318 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 331 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT SITE 142 FT /note="Critical for catalysis" FT /evidence="ECO:0000250" FT SITE 215 FT /note="Critical for catalysis" FT /evidence="ECO:0000250" FT MOD_RES 97 FT /note="Phosphoserine" FT /evidence="ECO:0000250" SQ SEQUENCE 409 AA; 45514 MW; FDBC1989DF42383A CRC64; MSNAPKIKVS GPVVELDGDE MTRVIWKLIK DMLILPYLDI RLDYYDLGIE HRDATDDQVT IDAAYAIKKH GVGVKCATIT PDEARVEEFN LKKMWLSPNG TIRNILGGTI FREPIVISNV PRLVPGWTKP IVIGRHAFGD QYRATNFKVD QPGTVTLTFT PADGSAPIVH EMVSIPEDGG VVLGMYNFKE SIRDFARASF SYGLNAKWPV YLSTKNTILK AYDGMFKDEF ERVYEEEFKA QFEAAGLTYE HRLIDDMVAA CLKWEGGYVW ACKNYDGDVQ SDTVAQGYGS LGLMTSVLMT ADGKTVEAEA AHGTVTRHYR QYQAGKPTST NPIASIFAWT RGLQHRGKLD GTPEVIDFAH KLESVVIATV ESGKMTKDLA ILIGPEQDWL NSEEFLDAIA DNLEKELAN //