IDH_MYCBO
ID IDH_MYCBO Reviewed; 409 AA.
AC P65098; A0A1R3Y3W8; O53389; X2BNC7;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=BQ2027_MB3371C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIU02000.1; -; Genomic_DNA.
DR RefSeq; NP_857016.1; NC_002945.3.
DR RefSeq; WP_003417452.1; NC_002945.4.
DR AlphaFoldDB; P65098; -.
DR SMR; P65098; -.
DR EnsemblBacteria; SIU02000; SIU02000; BQ2027_MB3371C.
DR PATRIC; fig|233413.5.peg.3703; -.
DR OMA; HGTVQRH; -.
DR SABIO-RK; P65098; -.
DR Proteomes; UP000001419; 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:0006102; P:isocitrate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004790; Isocitrate_DH_NADP.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR PANTHER; PTHR11822; PTHR11822; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR PIRSF; PIRSF000108; IDH_NADP; 1.
DR SMART; SM01329; Iso_dh; 1.
DR TIGRFAMs; TIGR00127; nadp_idh_euk; 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..409
FT /note="Isocitrate dehydrogenase [NADP]"
FT /id="PRO_0000083554"
FT BINDING 78..80
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 97..103
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 313..318
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 142
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT SITE 215
FT /note="Critical for catalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 409 AA; 45514 MW; FDBC1989DF42383A CRC64;
MSNAPKIKVS GPVVELDGDE MTRVIWKLIK DMLILPYLDI RLDYYDLGIE HRDATDDQVT
IDAAYAIKKH GVGVKCATIT PDEARVEEFN LKKMWLSPNG TIRNILGGTI FREPIVISNV
PRLVPGWTKP IVIGRHAFGD QYRATNFKVD QPGTVTLTFT PADGSAPIVH EMVSIPEDGG
VVLGMYNFKE SIRDFARASF SYGLNAKWPV YLSTKNTILK AYDGMFKDEF ERVYEEEFKA
QFEAAGLTYE HRLIDDMVAA CLKWEGGYVW ACKNYDGDVQ SDTVAQGYGS LGLMTSVLMT
ADGKTVEAEA AHGTVTRHYR QYQAGKPTST NPIASIFAWT RGLQHRGKLD GTPEVIDFAH
KLESVVIATV ESGKMTKDLA ILIGPEQDWL NSEEFLDAIA DNLEKELAN
