IDH_MYCTU
ID IDH_MYCTU Reviewed; 409 AA.
AC P9WKL1; L0TFB7; O53389; P65097;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
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=Rv3339c; ORFNames=MTV016.39c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP46160.1; -; Genomic_DNA.
DR PIR; B70846; B70846.
DR RefSeq; NP_217856.1; NC_000962.3.
DR RefSeq; WP_003417452.1; NZ_NVQJ01000051.1.
DR PDB; 4HCX; X-ray; 2.18 A; A/B=1-409.
DR PDBsum; 4HCX; -.
DR AlphaFoldDB; P9WKL1; -.
DR SMR; P9WKL1; -.
DR STRING; 83332.Rv3339c; -.
DR PaxDb; P9WKL1; -.
DR DNASU; 888013; -.
DR GeneID; 888013; -.
DR KEGG; mtu:Rv3339c; -.
DR PATRIC; fig|83332.111.peg.3724; -.
DR TubercuList; Rv3339c; -.
DR eggNOG; COG0538; Bacteria.
DR OMA; HGTVQRH; -.
DR PhylomeDB; P9WKL1; -.
DR BioCyc; MetaCyc:G185E-7615-MON; -.
DR BRENDA; 1.1.1.42; 3445.
DR SABIO-RK; P9WKL1; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IDA:MTBBASE.
DR GO; GO:0006097; P:glyoxylate cycle; IDA:MTBBASE.
DR GO; GO:0006102; P:isocitrate metabolic process; IDA:MTBBASE.
DR GO; GO:0006739; P:NADP metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:MTBBASE.
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 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..409
FT /note="Isocitrate dehydrogenase [NADP]"
FT /id="PRO_0000083555"
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"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:4HCX"
FT HELIX 20..33
FT /evidence="ECO:0007829|PDB:4HCX"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:4HCX"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:4HCX"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:4HCX"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:4HCX"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:4HCX"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:4HCX"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:4HCX"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:4HCX"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:4HCX"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:4HCX"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:4HCX"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:4HCX"
FT STRAND 153..161
FT /evidence="ECO:0007829|PDB:4HCX"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:4HCX"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:4HCX"
FT HELIX 189..206
FT /evidence="ECO:0007829|PDB:4HCX"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:4HCX"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:4HCX"
FT HELIX 220..237
FT /evidence="ECO:0007829|PDB:4HCX"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:4HCX"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:4HCX"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:4HCX"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:4HCX"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:4HCX"
FT HELIX 274..287
FT /evidence="ECO:0007829|PDB:4HCX"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:4HCX"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:4HCX"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:4HCX"
FT HELIX 316..324
FT /evidence="ECO:0007829|PDB:4HCX"
FT HELIX 333..350
FT /evidence="ECO:0007829|PDB:4HCX"
FT HELIX 353..370
FT /evidence="ECO:0007829|PDB:4HCX"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:4HCX"
FT HELIX 377..383
FT /evidence="ECO:0007829|PDB:4HCX"
FT HELIX 392..404
FT /evidence="ECO:0007829|PDB:4HCX"
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
