ID IDH_THET8 Reviewed; 496 AA. AC P33197; Q5SI45; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2005, sequence version 2. DT 27-MAR-2024, entry version 139. 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=TTHA1535; OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=300852; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1539996; DOI=10.1128/aem.58.1.93-98.1992; RA Miyazaki K., Eguchi H., Yamagishi A., Wakagi T., Oshima T.; RT "Molecular cloning of the isocitrate dehydrogenase gene of an extreme RT thermophile, Thermus thermophilus HB8."; RL Appl. Environ. Microbiol. 58:93-98(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; RT "Complete genome sequence of Thermus thermophilus HB8."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. 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. 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; M94317; AAA27492.1; -; Genomic_DNA. DR EMBL; AP008226; BAD71358.1; -; Genomic_DNA. DR RefSeq; WP_011228743.1; NC_006461.1. DR RefSeq; YP_144801.1; NC_006461.1. DR PDB; 2D1C; X-ray; 1.80 A; A/B=1-496. DR PDBsum; 2D1C; -. DR AlphaFoldDB; P33197; -. DR SMR; P33197; -. DR EnsemblBacteria; BAD71358; BAD71358; BAD71358. DR GeneID; 3168917; -. DR KEGG; ttj:TTHA1535; -. DR PATRIC; fig|300852.9.peg.1509; -. DR eggNOG; COG0473; Bacteria. DR HOGENOM; CLU_031953_1_3_0; -. DR PhylomeDB; P33197; -. DR BRENDA; 1.1.1.42; 2305. DR EvolutionaryTrace; P33197; -. DR Proteomes; UP000000532; 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; 3.30.70.1570; -; 1. DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR040978; Isocitrate_DH_TT1725_C. DR InterPro; IPR046997; Isocitrate_DH_TT1725_C_sf. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1. DR PANTHER; PTHR11835:SF43; ISOCITRATE DEHYDROGENASE [NADP]; 1. DR Pfam; PF00180; Iso_dh; 1. DR Pfam; PF18324; Isocitrate_DH_C_bact; 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; Phosphoprotein; Reference proteome; KW Tricarboxylic acid cycle. FT CHAIN 1..496 FT /note="Isocitrate dehydrogenase [NADP]" FT /id="PRO_0000083571" FT BINDING 104 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 114 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 137 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 224 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 224 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 248 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 252 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT SITE 144 FT /note="Critical for catalysis" FT /evidence="ECO:0000250" FT SITE 191 FT /note="Critical for catalysis" FT /evidence="ECO:0000250" FT MOD_RES 98 FT /note="Phosphoserine" FT /evidence="ECO:0000250" FT CONFLICT 201..202 FT /note="TL -> P (in Ref. 1; AAA27492)" FT /evidence="ECO:0000305" FT STRAND 3..5 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 11..14 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 20..25 FT /evidence="ECO:0007829|PDB:2D1C" FT HELIX 31..44 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 49..53 FT /evidence="ECO:0007829|PDB:2D1C" FT HELIX 58..61 FT /evidence="ECO:0007829|PDB:2D1C" FT TURN 62..64 FT /evidence="ECO:0007829|PDB:2D1C" FT HELIX 71..80 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 82..85 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 92..96 FT /evidence="ECO:0007829|PDB:2D1C" FT HELIX 99..106 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 111..117 FT /evidence="ECO:0007829|PDB:2D1C" FT TURN 125..128 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 132..138 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 140..142 FT /evidence="ECO:0007829|PDB:2D1C" FT HELIX 143..145 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 148..152 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 155..163 FT /evidence="ECO:0007829|PDB:2D1C" FT HELIX 164..180 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 185..190 FT /evidence="ECO:0007829|PDB:2D1C" FT TURN 192..194 FT /evidence="ECO:0007829|PDB:2D1C" FT HELIX 198..210 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 216..222 FT /evidence="ECO:0007829|PDB:2D1C" FT HELIX 223..232 FT /evidence="ECO:0007829|PDB:2D1C" FT HELIX 234..236 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 238..242 FT /evidence="ECO:0007829|PDB:2D1C" FT HELIX 244..255 FT /evidence="ECO:0007829|PDB:2D1C" FT TURN 256..259 FT /evidence="ECO:0007829|PDB:2D1C" FT HELIX 261..263 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 265..269 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 274..280 FT /evidence="ECO:0007829|PDB:2D1C" FT TURN 284..288 FT /evidence="ECO:0007829|PDB:2D1C" FT HELIX 295..307 FT /evidence="ECO:0007829|PDB:2D1C" FT HELIX 311..327 FT /evidence="ECO:0007829|PDB:2D1C" FT HELIX 333..336 FT /evidence="ECO:0007829|PDB:2D1C" FT TURN 338..340 FT /evidence="ECO:0007829|PDB:2D1C" FT HELIX 344..353 FT /evidence="ECO:0007829|PDB:2D1C" FT TURN 354..356 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 360..362 FT /evidence="ECO:0007829|PDB:2D1C" FT HELIX 375..377 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 387..397 FT /evidence="ECO:0007829|PDB:2D1C" FT HELIX 402..413 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 416..425 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 428..432 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 442..450 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 452..454 FT /evidence="ECO:0007829|PDB:2D1C" FT HELIX 458..469 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 472..483 FT /evidence="ECO:0007829|PDB:2D1C" FT STRAND 486..489 FT /evidence="ECO:0007829|PDB:2D1C" SQ SEQUENCE 496 AA; 54439 MW; BF544C3F772E1AE9 CRC64; MPLITTETGK KMHVLEDGRK LITVIPGDGI GPECVEATLK VLEAAKAPLA YEVREAGASV FRRGIASGVP QETIESIRKT RVVLKGPLET PVGYGEKSAN VTLRKLFETY ANVRPVREFP NVPTPYAGRG IDLVVVRENV EDLYAGIEHM QTPSVAQTLK LISWKGSEKI VRFAFELARA EGRKKVHCAT KSNIMKLAEG TLKRAFEQVA QEYPDIEAVH IIVDNAAHQL VKRPEQFEVI VTTNMNGDIL SDLTSGLIGG LGFAPSANIG NEVAIFEAVH GSAPKYAGKN VINPTAVLLS AVMMLRYLEE FATADLIENA LLYTLEEGRV LTGDVVGYDR GAKTTEYTEA IIQNLGKTPR KTQVRGYKPF RLPQVDGAIA PIVPRSRRVV GVDVFVETNL LPEALGKALE DLAAGTPFRL KMISNRGTQV YPPTGGLTDL VDHYRCRFLY TGEGEAKDPE ILDLVSRVAS RFRWMHLEKL QEFDGEPGFT KAQGED //