ID IDH_CORGL Reviewed; 738 AA. AC P50216; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 136. DE RecName: Full=Isocitrate dehydrogenase [NADP]; DE Short=IDH; DE EC=1.1.1.42; DE AltName: Full=Oxalosuccinate decarboxylase; GN Name=icd; OrderedLocusNames=Cgl0664, cg0766; OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / OS JCM 1318 / LMG 3730 / NCIMB 10025). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196627; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / RC NCIMB 10025; RX PubMed=7836312; DOI=10.1128/jb.177.3.774-782.1995; RA Eikmanns B.J., Rittmann D., Sahm H.; RT "Cloning, sequence analysis, expression, and inactivation of the RT Corynebacterium glutamicum icd gene encoding isocitrate dehydrogenase and RT biochemical characterization of the enzyme."; RL J. Bacteriol. 177:774-782(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / RC NCIMB 10025; RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1; RA Ikeda M., Nakagawa S.; RT "The Corynebacterium glutamicum genome: features and impacts on RT biotechnological processes."; RL Appl. Microbiol. Biotechnol. 62:99-109(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / RC NCIMB 10025; RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8; RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.; RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its RT impact on the production of L-aspartate-derived amino acids and vitamins."; RL J. Biotechnol. 104:5-25(2003). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, AND RP SUBUNIT. RX PubMed=16416443; DOI=10.1002/prot.20867; RA Imabayashi F., Aich S., Prasad L., Delbaere L.T.; RT "Substrate-free structure of a monomeric NADP isocitrate dehydrogenase: an RT open conformation phylogenetic relationship of isocitrate dehydrogenase."; RL Proteins 63:100-112(2006). 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; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.; CC -!- ACTIVITY REGULATION: Weakly inhibited by oxaloacetate, 2-oxoglutarate, CC and citrate. Severely inhibited by oxaloacetate plus glyoxylate. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16416443}. CC -!- SIMILARITY: Belongs to the monomeric-type IDH 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; X71489; CAA50590.1; -; Genomic_DNA. DR EMBL; BA000036; BAB98057.1; -; Genomic_DNA. DR EMBL; BX927149; CAF19369.1; -; Genomic_DNA. DR PIR; I40719; I40719. DR RefSeq; NP_599896.1; NC_003450.3. DR RefSeq; WP_011013800.1; NC_006958.1. DR PDB; 2B0T; X-ray; 1.75 A; A=1-738. DR PDB; 3MBC; X-ray; 1.90 A; A/B=1-738. DR PDBsum; 2B0T; -. DR PDBsum; 3MBC; -. DR AlphaFoldDB; P50216; -. DR SMR; P50216; -. DR STRING; 196627.cg0766; -. DR KEGG; cgb:cg0766; -. DR KEGG; cgl:Cgl0664; -. DR PATRIC; fig|196627.13.peg.650; -. DR eggNOG; COG2838; Bacteria. DR HOGENOM; CLU_025308_1_0_11; -. DR OrthoDB; 9807643at2; -. DR BioCyc; CORYNE:G18NG-10226-MONOMER; -. DR BRENDA; 1.1.1.42; 960. DR EvolutionaryTrace; P50216; -. DR Proteomes; UP000000582; Chromosome. DR Proteomes; UP000001009; Chromosome. DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR InterPro; IPR004436; Isocitrate_DH_NADP_mono. DR NCBIfam; TIGR00178; monomer_idh; 1. DR PANTHER; PTHR36999; ISOCITRATE DEHYDROGENASE [NADP]; 1. DR PANTHER; PTHR36999:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 1. DR Pfam; PF03971; IDH; 1. DR PIRSF; PIRSF009407; IDH_monmr; 1. DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP; KW Oxidoreductase; Phosphoprotein; Reference proteome; KW Tricarboxylic acid cycle. FT CHAIN 1..738 FT /note="Isocitrate dehydrogenase [NADP]" FT /id="PRO_0000083595" FT BINDING 80..85 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 130..137 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 133 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 143 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 346 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:16416443" FT BINDING 543 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 544 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:16416443" FT BINDING 548 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:16416443" FT BINDING 580..581 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 585 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 596..598 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 645 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT SITE 253 FT /note="Critical for catalysis" FT /evidence="ECO:0000250" FT SITE 416 FT /note="Critical for catalysis" FT /evidence="ECO:0000250" FT STRAND 3..8 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 11..29 FT /evidence="ECO:0007829|PDB:2B0T" FT TURN 30..32 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 34..39 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 42..47 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 51..53 FT /evidence="ECO:0007829|PDB:2B0T" FT TURN 56..58 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 63..70 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 77..80 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 88..100 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 115..125 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 132..136 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 141..144 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 147..155 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 175..178 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 179..182 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 184..187 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 192..199 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 205..214 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 219..225 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 227..244 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 247..250 FT /evidence="ECO:0007829|PDB:2B0T" FT TURN 254..256 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 260..272 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 274..286 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 294..302 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 308..321 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 327..329 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 330..332 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 345..354 FT /evidence="ECO:0007829|PDB:2B0T" FT TURN 355..357 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 358..360 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 366..372 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 376..392 FT /evidence="ECO:0007829|PDB:2B0T" FT TURN 397..399 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 405..407 FT /evidence="ECO:0007829|PDB:2B0T" FT TURN 410..412 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 414..417 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 419..421 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 422..424 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 427..434 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 440..446 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 451..457 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 459..476 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 480..483 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 489..502 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 512..515 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 517..529 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 535..538 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 540..555 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 558..560 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 562..567 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 572..575 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 583..592 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 600..617 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 620..638 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 652..669 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 674..700 FT /evidence="ECO:0007829|PDB:2B0T" FT STRAND 711..713 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 716..723 FT /evidence="ECO:0007829|PDB:2B0T" FT HELIX 727..735 FT /evidence="ECO:0007829|PDB:2B0T" SQ SEQUENCE 738 AA; 80081 MW; EAC4C5FA38C33F63 CRC64; MAKIIWTRTD EAPLLATYSL KPVVEAFAAT AGIEVETRDI SLAGRILAQF PERLTEDQKV GNALAELGEL AKTPEANIIK LPNISASVPQ LKAAIKELQD QGYDIPELPD NATTDEEKDI LARYNAVKGS AVNPVLREGN SDRRAPIAVK NFVKKFPHRM GEWSADSKTN VATMDANDFR HNEKSIILDA ADEVQIKHIA ADGTETILKD SLKLLEGEVL DGTVLSAKAL DAFLLEQVAR AKAEGILFSA HLKATMMKVS DPIIFGHVVR AYFADVFAQY GEQLLAAGLN GENGLAAILS GLESLDNGEE IKAAFEKGLE DGPDLAMVNS ARGITNLHVP SDVIVDASMP AMIRTSGHMW NKDDQEQDTL AIIPDSSYAG VYQTVIEDCR KNGAFDPTTM GTVPNVGLMA QKAEEYGSHD KTFRIEADGV VQVVSSNGDV LIEHDVEAND IWRACQVKDA PIQDWVKLAV TRSRLSGMPA VFWLDPERAH DRNLASLVEK YLADHDTEGL DIQILSPVEA TQLSIDRIRR GEDTISVTGN VLRDYNTDLF PILELGTSAK MLSVVPLMAG GGLFETGAGG SAPKHVQQVQ EENHLRWDSL GEFLALAESF RHELNNNGNT KAGVLADALD KATEKLLNEE KSPSRKVGEI DNRGSHFWLT KFWADELAAQ TEDADLAATF APVAEALNTG AADIDAALLA VQGGATDLGG YYSPNEEKLT NIMRPVAQFN EIVDALKK //