ID IDH_COREF Reviewed; 729 AA. AC Q8RQL9; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 02-SEP-2026, entry version 119. DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000250|UniProtKB:P50216}; DE Short=IDH; DE EC=1.1.1.42 {ECO:0000250|UniProtKB:P50216}; DE AltName: Full=Oxalosuccinate decarboxylase; GN Name=icd {ECO:0000303|Ref.1}; OrderedLocusNames=CE0682; OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 OS / NBRC 100395). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196164; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395; RA Nonaka G., Kimura E., Kawahara Y., Sugimoto S.; RT "Corynebacterium efficiens icd gene for isocitrate dehydrogenase, complete RT cds."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395; RX PubMed=12840036; DOI=10.1101/gr.1285603; RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.; RT "Comparative complete genome sequence analysis of the amino acid RT replacements responsible for the thermostability of Corynebacterium RT efficiens."; RL Genome Res. 13:1572-1579(2003). CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of isocitrate to 2- CC oxoglutarate and carbon dioxide with the concomitant reduction of CC NADP(+). {ECO:0000250|UniProtKB:P50216}. 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 Evidence={ECO:0000250|UniProtKB:P50216}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P50216}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:P50216}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. CC {ECO:0000250|UniProtKB:P50216}; CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P50216}. CC -!- SIMILARITY: Belongs to the monomeric-type IDH family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC17492.1; Type=Erroneous initiation; Evidence={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; AB083179; BAB88832.1; -; Genomic_DNA. DR EMBL; BA000035; BAC17492.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_006769639.1; NC_004369.1. DR AlphaFoldDB; Q8RQL9; -. DR SMR; Q8RQL9; -. DR STRING; 196164.gene:10741084; -. DR KEGG; cef:CE0682; -. DR eggNOG; COG2838; Bacteria. DR HOGENOM; CLU_025308_1_0_11; -. DR OrthoDB; 9807643at2; -. DR Proteomes; UP000001409; Chromosome. DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; ISS:UniProtKB. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR InterPro; IPR004436; Isocitrate_DH_NADP_mono. DR NCBIfam; TIGR00178; monomer_idh; 1. DR PANTHER; PTHR36999:SF1; ISOCITRATE DEHYDROGENASE (NADP(+)); 1. DR PANTHER; PTHR36999; ISOCITRATE DEHYDROGENASE [NADP]; 1. DR Pfam; PF03971; IDH; 1. DR PIRSF; PIRSF009407; IDH_monmr; 1. DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1. PE 3: Inferred from homology; KW Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP; KW Oxidoreductase; Reference proteome; Tricarboxylic acid cycle. FT CHAIN 1..729 FT /note="Isocitrate dehydrogenase [NADP]" FT /id="PRO_0000083594" FT BINDING 83 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 85 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 121 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 124 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 124 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 128 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 134 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 244 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 337 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P50216" FT BINDING 407 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 534 FT /ligand="D-threo-isocitrate" FT /ligand_id="ChEBI:CHEBI:15562" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 535 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P50216" FT BINDING 539 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P50216" FT BINDING 572 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 576 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 587 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 589 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P16100" FT BINDING 636 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250|UniProtKB:P16100" SQ SEQUENCE 729 AA; 79285 MW; 84BCDECA8687627B CRC64; MAKIIWTRTD EAPLLATYSL KPVVEAFAAT AGIEVETRDI SLAGRILAQF ADQLPEEQKV SDALAELGEL AKTPEANIIK LPNISASVPQ LKAAVKELQE QGYDLPEYED AKDRYAAVIG SNVNPVLREG NSDRRAPVAV KNFVKKFPHR MGEWSADSKT NVATMGADDF RSNEKSVIMD EADTVVIKHV AADGTETVLK DSLPLLKGEV IDGTFISAKA LDAFLLDQVK RAKEEGILFS AHMKATMMKV SDPIIFGHIV RAYFADVYAQ YGEQLLAAGL NGENGLAAIY AGLDKLDNGA EIKAAFDKGL EEGPDLAMVN SAKGITNLHV PSDVIIDASM PAMIRTSGKM WNKDDQTQDA LAVIPDSSYA GVYQTVIEDC RKNGAFDPTT MGTVPNVGLM AQKAEEYGSH DKTFRIEADG KVQVVASNGD VLIEHDVEKG DIWRACQTKD APIQDWVKLA VNRARLSGMP AVFWLDPARA HDRNLTTLVE KYLADHDTEG LDIQILSPVE ATQHAIDRIR RGEDTISVTG NVLRDYNTDL FPILELGTSA KMLSVVPLMA GGGLFETGAG GSAPKHVQQV IEENHLRWDS LGEFLALAES FRHELNTRNN TKAGVLADAL DRATEKLLNE EKSPSRKVGE IDNRGSHFWL ATYWADELAN QTEDAELAET FAPVAEALNN QAADIDAALI GEQGKPVDLG GYYAPSDEKT SAIMRPVAAF NEIIDSLKK //