IDH_RICBR
ID IDH_RICBR Reviewed; 483 AA.
AC Q1RJU4;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=RBE_0289;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
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; CP000087; ABE04370.1; -; Genomic_DNA.
DR RefSeq; WP_011476981.1; NC_007940.1.
DR AlphaFoldDB; Q1RJU4; -.
DR SMR; Q1RJU4; -.
DR STRING; 336407.RBE_0289; -.
DR EnsemblBacteria; ABE04370; ABE04370; RBE_0289.
DR KEGG; rbe:RBE_0289; -.
DR eggNOG; COG0473; Bacteria.
DR HOGENOM; CLU_031953_1_2_5; -.
DR OMA; TCAHKAN; -.
DR OrthoDB; 1551125at2; -.
DR Proteomes; UP000001951; 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; Metal-binding; NADP; Oxidoreductase;
KW Phosphoprotein; Tricarboxylic acid cycle.
FT CHAIN 1..483
FT /note="Isocitrate dehydrogenase [NADP]"
FT /id="PRO_0000292202"
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; 53959 MW; D02F3B5F38A5FF9D CRC64;
MAEFTPITIA YGDGIGPEIM EAVLYILRKA EARIRLETIE VGEKLYVKHY SSGISEQSWE
SIERTGVILK APITTPQGGG YKSLNVTIRK TLQLFANIRP SVSFYPFTKT LHPNLNLTII
RENEEDLYAG IEYRQTHNMY ESVKLISRTG CEKIIRYAFE YAVKNNRKKV TCLSKDNIMK
FSDGIFHKVF NEIAKEYPQI NNEHYIIDIG TARLATKPEI FDVIVTSNLY GDIISDVAAE
ISGSVGLAGS ANIGEHYAMF EAVHGSAPDI AGQDIANPSG LLNAAIMMLV HIGQGDIATL
IENAWKKTIE DGMHTADIYN KDHSTKKVGT KEFAEEVVKR LGQKPEKLAK ADYPLVTKKQ
ESNTTYKINT KEVKKLVGTD IFVGMNVASA HDIADKVNKL DIGNFELKTI SSKGLKLWPR
DTRFETISDH WCCRFMAKDG VELKHLDITK LLETLSKANI DFIKVENLFE FDGAAGYSLA
QGE