ID L7UY07_MYCL1 Unreviewed; 745 AA.
AC L7UY07;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR009407};
DE EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR009407};
DE AltName: Full=Oxalosuccinate decarboxylase {ECO:0000256|PIRNR:PIRNR009407};
GN Name=icd2 {ECO:0000313|EMBL:AGC60276.1};
GN OrderedLocusNames=MULP_00143 {ECO:0000313|EMBL:AGC60276.1};
OS Mycobacterium liflandii (strain 128FXT).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=459424 {ECO:0000313|EMBL:AGC60276.1, ECO:0000313|Proteomes:UP000011157};
RN [1] {ECO:0000313|EMBL:AGC60276.1, ECO:0000313|Proteomes:UP000011157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=128FXT {ECO:0000313|EMBL:AGC60276.1,
RC ECO:0000313|Proteomes:UP000011157};
RX PubMed=23204453; DOI=10.1128/JB.02132-12;
RA Tobias N.J., Doig K.D., Medema M.H., Chen H., Haring V., Moore R.,
RA Seemann T., Stinear T.P.;
RT "Complete Genome Sequence of the Frog Pathogen Mycobacterium ulcerans
RT Ecovar Liflandii.";
RL J. Bacteriol. 195:556-564(2013).
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 Evidence={ECO:0000256|PIRNR:PIRNR009407};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR009407-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR009407-3};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000256|PIRSR:PIRSR009407-3};
CC -!- SIMILARITY: Belongs to the monomeric-type IDH family.
CC {ECO:0000256|PIRNR:PIRNR009407}.
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DR EMBL; CP003899; AGC60276.1; -; Genomic_DNA.
DR RefSeq; WP_012392157.1; NC_020133.1.
DR AlphaFoldDB; L7UY07; -.
DR KEGG; mli:MULP_00143; -.
DR PATRIC; fig|459424.11.peg.148; -.
DR HOGENOM; CLU_025308_1_0_11; -.
DR Proteomes; UP000011157; Chromosome.
DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR004436; Isocitrate_DH_NADP_mono.
DR NCBIfam; TIGR00178; monomer_idh; 1.
DR PANTHER; PTHR36999; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR PANTHER; PTHR36999:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR Pfam; PF03971; IDH; 1.
DR PIRSF; PIRSF009407; IDH_monmr; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE 3: Inferred from homology;
KW Glyoxylate bypass {ECO:0000256|PIRNR:PIRNR009407};
KW Magnesium {ECO:0000256|PIRSR:PIRSR009407-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR009407-3};
KW NADP {ECO:0000256|PIRNR:PIRNR009407, ECO:0000256|PIRSR:PIRSR009407-4};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR009407,
KW ECO:0000313|EMBL:AGC60276.1};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT BINDING 84..89
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 134..141
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 137
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 352
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 550
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 551
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 555
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 587..588
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 592
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 603..605
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 652
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT SITE 257
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT SITE 422
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ SEQUENCE 745 AA; 82350 MW; 8C8AF8D36A9A8798 CRC64;
MSAEQPTIIY TLTDEAPLLA TYAFLPIVRA FAEPAGIQIK TSDISVAARI LAEFPDYLTD
EQRVPDNLAE LGELTQDPDT NIIKLPNISA SVPQLKAAIK ELQDKGYAIP DYPADPKTDE
EKALKERYAR CLGSAVNPVL RQGNSDRRAP NAVKEYARKH PHSMGEWSMA SRTHVAHMRH
GDFYAGEKSI TLDRAHKVKM ELVTKGGQTL VLKPEVSLDD GDIIDSMFMS KKALCEFYEE
QIEDAYKTGV MFSLHVKATM MKVSHPIVFG HAVKTFYRDA FAKHQKLFDE LGVNVNNGLS
DLYSKIETLP ASQHDEIIDD LHRCHEHRPE LAMVDSARGI TNFHSPSDVI VDASMPAMIR
AGGKMYGADG KLKDTKAVNP ESTFSRIYQE IINFCKTNGQ FDPTTMGTVP NVGLMAQQAE
EYGSHDKTFE VPEDGVANIV DLDTGEVLLT QDVEAGDIWR MCVVKDAPIR DWVKLAVTRA
RNSGMPVLFW LDPYRPHENE LIKKVKTYLK DHHTEGLDIQ IMSQVRSMRY TLERLIRGLD
TIAATGNILR DYLTDLFPIL ELGTSAKMLS IVPLMAGGGM YETGAGGSAP KHVKQLVEEN
HLRWDSLGEF LALGASLEDM GIKIGNDRAK ILARTLDDAI GKLLGNNKSP SRKTGELDNR
GSQFYLALYW AQELAEQTDD AELAEHFAKL AKALADGEEA IVAELAEAQG EAVDIGGYYA
PDNEKTTAVM RPSKTLNAAL EAAQG
//
