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}.
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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
//
