IDH_RICTY
ID IDH_RICTY Reviewed; 483 AA.
AC Q68XA5;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=RT0256;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
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 -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; AE017197; AAU03737.1; -; Genomic_DNA.
DR RefSeq; WP_011190722.1; NC_006142.1.
DR AlphaFoldDB; Q68XA5; -.
DR SMR; Q68XA5; -.
DR STRING; 257363.RT0256; -.
DR EnsemblBacteria; AAU03737; AAU03737; RT0256.
DR KEGG; rty:RT0256; -.
DR eggNOG; COG0473; Bacteria.
DR HOGENOM; CLU_031953_1_3_5; -.
DR OMA; TCAHKAN; -.
DR OrthoDB; 1551125at2; -.
DR Proteomes; UP000000604; 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 InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR014273; Isocitrate_DH_aproteobac-typ.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR040978; TT1725.
DR PANTHER; PTHR11835:SF43; PTHR11835:SF43; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR Pfam; PF18324; TT1725; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR02924; ICDH_alpha; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 3: Inferred from homology;
KW Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP;
KW Oxidoreductase; Phosphoprotein; Tricarboxylic acid cycle.
FT CHAIN 1..483
FT /note="Isocitrate dehydrogenase [NADP]"
FT /id="PRO_0000083558"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT SITE 128
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 175
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 483 AA; 54161 MW; D6AAA410411169AF CRC64;
MAEFTPITIA YGDGIGPEIM DAVLYILRQA EARISLETIE VGEKLYKKHY TSGISEESWN
VIQRTGIILK APITTPQSGG YKSLNVTIRK TLQLFANIRP AVSFHPFTRT LHPNLNLTII
RENEEDLYSG IEYRQTHNMY ESLKLISHTG CKKIIRYAFE YAVKNNRKKV TCLSKDNIMK
FSDGIFHRVF NEIAKEYPQI DNEHYIIDIG TAKLATTPEI FDIIVTSNLY GDIISDVAAE
ISGSVGLAGS ANIGQHYAMF EAVHGSAPDI AGKGIANPSG LLNAAIMMLV HIGQGDIASL
IENAWKKTIE DGVHTFDIYS EHSSSKKVCT KEFAEEVIKR LGQLPMTLPK ASYPLIVKKQ
ESKIEYKIDT TEVKKLVGTD IFINIHVFSA HDIADKINKL DIGNFELKTI SSKGLKLWPH
DLRFEIISDH WCCRFMNKDG TEIKHLDIII LLQALSKANI DFIKVENLFE FDGVACYSLA
QGE
