ID IDH_BACSU Reviewed; 423 AA. AC P39126; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 170. 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; Synonyms=citC; OrderedLocusNames=BSU29130; OS Bacillus subtilis (strain 168). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=224308; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168 / SMY; RX PubMed=8045898; DOI=10.1128/jb.176.15.4669-4679.1994; RA Jin S., Sonenshein A.L.; RT "Identification of two distinct Bacillus subtilis citrate synthase genes."; RL J. Bacteriol. 176:4669-4679(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431; RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.; RT "Sequencing and functional annotation of the Bacillus subtilis genes in the RT 200 kb rrnB-dnaB region."; RL Microbiology 143:3431-3441(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). RN [4] RP PHOSPHORYLATION. RX PubMed=11751849; DOI=10.1074/jbc.m107908200; RA Singh S.K., Miller S.P., Dean A., Banaszak L.J., LaPorte D.C.; RT "Bacillus subtilis isocitrate dehydrogenase. A substrate analogue for RT Escherichia coli isocitrate dehydrogenase kinase/phosphatase."; RL J. Biol. Chem. 277:7567-7573(2002). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH CITRATE, AND RP SUBUNIT. RX PubMed=11290745; DOI=10.1074/jbc.m101191200; RA Singh S.K., Matsuno K., LaPorte D.C., Banaszak L.J.; RT "Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 A. RT Insights into the nature of substrate specificity exhibited by Escherichia RT coli isocitrate dehydrogenase kinase/phosphatase."; RL J. Biol. Chem. 276:26154-26163(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:0000269|PubMed:11290745}. CC -!- INTERACTION: CC P39126; P49814: mdh; NbExp=3; IntAct=EBI-7829570, EBI-7827708; CC -!- MISCELLANEOUS: The enzyme can be phosphorylated in vitro by the E.coli CC isocitrate dehydrogenase kinase/phosphatase, but B.subtilis lacks such CC an enzyme. 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; U05257; AAA96342.1; -; Genomic_DNA. DR EMBL; AF008220; AAC00346.1; -; Genomic_DNA. DR EMBL; AL009126; CAB14873.1; -; Genomic_DNA. DR PIR; I40382; I40382. DR RefSeq; NP_390791.1; NC_000964.3. DR RefSeq; WP_003229433.1; NZ_JNCM01000036.1. DR PDB; 1HQS; X-ray; 1.55 A; A/B=1-423. DR PDBsum; 1HQS; -. DR AlphaFoldDB; P39126; -. DR SMR; P39126; -. DR IntAct; P39126; 2. DR MINT; P39126; -. DR STRING; 224308.BSU29130; -. DR DrugBank; DB02159; (R)-Propylene glycol. DR DrugBank; DB04349; (S)-propane-1,2-diol. DR DrugBank; DB04272; Citric acid. DR DrugBank; DB04530; S,S-(2-Hydroxyethyl)Thiocysteine. DR jPOST; P39126; -. DR PaxDb; 224308-BSU29130; -. DR EnsemblBacteria; CAB14873; CAB14873; BSU_29130. DR GeneID; 83886750; -. DR GeneID; 938183; -. DR KEGG; bsu:BSU29130; -. DR PATRIC; fig|224308.179.peg.3163; -. DR eggNOG; COG0538; Bacteria. DR InParanoid; P39126; -. DR OrthoDB; 9806254at2; -. DR PhylomeDB; P39126; -. DR BioCyc; BSUB:BSU29130-MONOMER; -. DR SABIO-RK; P39126; -. DR EvolutionaryTrace; P39126; -. DR Proteomes; UP000001570; 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; 1. 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 1: Evidence at protein level; KW 3D-structure; Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP; KW Oxidoreductase; Reference proteome; Tricarboxylic acid cycle. FT CHAIN 1..423 FT /note="Isocitrate dehydrogenase [NADP]" FT /id="PRO_0000083549" FT BINDING 95 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 96 FT /ligand="substrate" FT BINDING 104 FT /ligand="substrate" FT BINDING 106 FT /ligand="substrate" FT BINDING 110 FT /ligand="substrate" FT BINDING 120 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 144 FT /ligand="substrate" FT BINDING 311 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 345..351 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 358 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 397 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT BINDING 401 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT SITE 151 FT /note="Critical for catalysis" FT /evidence="ECO:0000250" FT SITE 221 FT /note="Critical for catalysis" FT /evidence="ECO:0000250" FT STRAND 3..5 FT /evidence="ECO:0007829|PDB:1HQS" FT STRAND 8..10 FT /evidence="ECO:0007829|PDB:1HQS" FT STRAND 13..15 FT /evidence="ECO:0007829|PDB:1HQS" FT STRAND 18..25 FT /evidence="ECO:0007829|PDB:1HQS" FT HELIX 31..50 FT /evidence="ECO:0007829|PDB:1HQS" FT STRAND 57..60 FT /evidence="ECO:0007829|PDB:1HQS" FT HELIX 65..71 FT /evidence="ECO:0007829|PDB:1HQS" FT HELIX 77..86 FT /evidence="ECO:0007829|PDB:1HQS" FT STRAND 88..91 FT /evidence="ECO:0007829|PDB:1HQS" FT STRAND 98..102 FT /evidence="ECO:0007829|PDB:1HQS" FT HELIX 105..112 FT /evidence="ECO:0007829|PDB:1HQS" FT STRAND 117..123 FT /evidence="ECO:0007829|PDB:1HQS" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:1HQS" FT HELIX 135..137 FT /evidence="ECO:0007829|PDB:1HQS" FT STRAND 139..145 FT /evidence="ECO:0007829|PDB:1HQS" FT HELIX 149..152 FT /evidence="ECO:0007829|PDB:1HQS" FT HELIX 161..173 FT /evidence="ECO:0007829|PDB:1HQS" FT HELIX 182..184 FT /evidence="ECO:0007829|PDB:1HQS" FT STRAND 185..193 FT /evidence="ECO:0007829|PDB:1HQS" FT HELIX 194..211 FT /evidence="ECO:0007829|PDB:1HQS" FT STRAND 214..220 FT /evidence="ECO:0007829|PDB:1HQS" FT TURN 222..224 FT /evidence="ECO:0007829|PDB:1HQS" FT TURN 226..228 FT /evidence="ECO:0007829|PDB:1HQS" FT HELIX 229..244 FT /evidence="ECO:0007829|PDB:1HQS" FT HELIX 245..247 FT /evidence="ECO:0007829|PDB:1HQS" FT STRAND 248..250 FT /evidence="ECO:0007829|PDB:1HQS" FT HELIX 251..275 FT /evidence="ECO:0007829|PDB:1HQS" FT STRAND 279..285 FT /evidence="ECO:0007829|PDB:1HQS" FT HELIX 286..295 FT /evidence="ECO:0007829|PDB:1HQS" FT HELIX 297..299 FT /evidence="ECO:0007829|PDB:1HQS" FT STRAND 301..305 FT /evidence="ECO:0007829|PDB:1HQS" FT HELIX 307..320 FT /evidence="ECO:0007829|PDB:1HQS" FT TURN 324..326 FT /evidence="ECO:0007829|PDB:1HQS" FT STRAND 328..332 FT /evidence="ECO:0007829|PDB:1HQS" FT TURN 334..336 FT /evidence="ECO:0007829|PDB:1HQS" FT STRAND 339..344 FT /evidence="ECO:0007829|PDB:1HQS" FT HELIX 349..351 FT /evidence="ECO:0007829|PDB:1HQS" FT TURN 352..355 FT /evidence="ECO:0007829|PDB:1HQS" FT HELIX 360..373 FT /evidence="ECO:0007829|PDB:1HQS" FT HELIX 376..391 FT /evidence="ECO:0007829|PDB:1HQS" FT HELIX 397..400 FT /evidence="ECO:0007829|PDB:1HQS" FT STRAND 403..405 FT /evidence="ECO:0007829|PDB:1HQS" FT HELIX 411..420 FT /evidence="ECO:0007829|PDB:1HQS" SQ SEQUENCE 423 AA; 46418 MW; CC69E694EB66D0D8 CRC64; MAQGEKITVS NGVLNVPNNP IIPFIEGDGT GPDIWNAASK VLEAAVEKAY KGEKKITWKE VYAGEKAYNK TGEWLPAETL DVIREYFIAI KGPLTTPVGG GIRSLNVALR QELDLFVCLR PVRYFTGVPS PVKRPEDTDM VIFRENTEDI YAGIEYAKGS EEVQKLISFL QNELNVNKIR FPETSGIGIK PVSEEGTSRL VRAAIDYAIE HGRKSVTLVH KGNIMKFTEG AFKNWGYELA EKEYGDKVFT WAQYDRIAEE QGKDAANKAQ SEAEAAGKII IKDSIADIFL QQILTRPNEF DVVATMNLNG DYISDALAAQ VGGIGIAPGA NINYETGHAI FEATHGTAPK YAGLDKVNPS SVILSGVLLL EHLGWNEAAD LVIKSMEKTI ASKVVTYDFA RLMDGATEVK CSEFGEELIK NMD //