ID IDH_ARCFU Reviewed; 412 AA.
AC O29610; O31221;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 146.
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=AF_0647;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-27, AND
RP CHARACTERIZATION.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9325430; DOI=10.1007/s002030050516;
RA Steen I.H., Lien T., Birkeland N.-K.;
RT "Biochemical and phylogenetic characterization of isocitrate dehydrogenase
RT from a hyperthermophilic archaeon, Archaeoglobus fulgidus.";
RL Arch. Microbiol. 168:412-420(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=118 uM for D,L-isocitrate;
CC KM=30 uM for NADP;
CC KM=5.4 mM for NAD;
CC Vmax=141 umol/min/mg enzyme towards NADP at 60 degrees Celsius;
CC Vmax=14.5 umol/min/mg enzyme towards NAD;
CC pH dependence:
CC Optimum pH is 8.6.;
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius. Thermostable.;
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; Z96105; CAB09535.1; -; Genomic_DNA.
DR EMBL; AE000782; AAB90591.1; -; Genomic_DNA.
DR PIR; G69330; G69330.
DR RefSeq; WP_010878150.1; NC_000917.1.
DR PDB; 2IV0; X-ray; 2.50 A; A/B=1-412.
DR PDBsum; 2IV0; -.
DR AlphaFoldDB; O29610; -.
DR SMR; O29610; -.
DR STRING; 224325.AF_0647; -.
DR PaxDb; 224325-AF_0647; -.
DR EnsemblBacteria; AAB90591; AAB90591; AF_0647.
DR GeneID; 1483865; -.
DR KEGG; afu:AF_0647; -.
DR eggNOG; arCOG01164; Archaea.
DR HOGENOM; CLU_031953_7_1_2; -.
DR OrthoDB; 23624at2157; -.
DR PhylomeDB; O29610; -.
DR BRENDA; 1.1.1.42; 414.
DR SABIO-RK; O29610; -.
DR EvolutionaryTrace; O29610; -.
DR Proteomes; UP000002199; 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; Direct protein sequencing; Glyoxylate bypass; Magnesium;
KW Manganese; Metal-binding; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..412
FT /note="Isocitrate dehydrogenase [NADP]"
FT /id="PRO_0000083572"
FT BINDING 100
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P08200"
FT BINDING 333..339
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 156
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 223
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:2IV0"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:2IV0"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:2IV0"
FT HELIX 39..57
FT /evidence="ECO:0007829|PDB:2IV0"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:2IV0"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:2IV0"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:2IV0"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2IV0"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:2IV0"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:2IV0"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:2IV0"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2IV0"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:2IV0"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:2IV0"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:2IV0"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:2IV0"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:2IV0"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:2IV0"
FT HELIX 196..212
FT /evidence="ECO:0007829|PDB:2IV0"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:2IV0"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:2IV0"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:2IV0"
FT HELIX 231..245
FT /evidence="ECO:0007829|PDB:2IV0"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:2IV0"
FT HELIX 253..260
FT /evidence="ECO:0007829|PDB:2IV0"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:2IV0"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:2IV0"
FT HELIX 279..285
FT /evidence="ECO:0007829|PDB:2IV0"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:2IV0"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:2IV0"
FT HELIX 297..310
FT /evidence="ECO:0007829|PDB:2IV0"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:2IV0"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:2IV0"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:2IV0"
FT TURN 338..341
FT /evidence="ECO:0007829|PDB:2IV0"
FT HELIX 348..360
FT /evidence="ECO:0007829|PDB:2IV0"
FT HELIX 364..379
FT /evidence="ECO:0007829|PDB:2IV0"
FT HELIX 385..391
FT /evidence="ECO:0007829|PDB:2IV0"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:2IV0"
FT HELIX 398..411
FT /evidence="ECO:0007829|PDB:2IV0"
SQ SEQUENCE 412 AA; 45842 MW; A2E1A3AA7662D3EA CRC64;
MQYEKVKPPE NGEKIRYENG KLIVPDNPII PYFEGDGIGK DVVPAAIRVL DAAADKIGKE
VVWFQVYAGE DAYKLYGNYL PDDTLNAIKE FRVALKGPLT TPVGGGYRSL NVTIRQVLDL
YANVRPVYYL KGVPSPIKHP EKVNFVIFRE NTEDVYAGIE WPRGSEEALK LIRFLKNEFG
VTIREDSGIG IKPISEFATK RLVRMAIRYA IENNRKSVTL VHKGNIMKYT EGAFRDWGYE
VAKQEFGEYC ITEDELWDKY GGKQPEGKIV VKDRIADNMF QQILTRTDEY DVIALPNLNG
DYLSDAAAAL IGGLGIAPGS NIGDGIGVFE PVHGSAPKYA GQNKVNPTAE ILTGALMFEY
IGWKDASEMI KKAVEMTISS GIVTYDIHRH MGGTKVGTRE FAEAVVENLQ SL
//
