ID V7L1E9_MYCAV Unreviewed; 745 AA.
AC V7L1E9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
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 ORFNames=P863_02065 {ECO:0000313|EMBL:ETB15353.1};
OS Mycobacterium avium subsp. silvaticum ATCC 49884.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1401690 {ECO:0000313|EMBL:ETB15353.1, ECO:0000313|Proteomes:UP000018526};
RN [1] {ECO:0000313|EMBL:ETB15353.1, ECO:0000313|Proteomes:UP000018526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49884 {ECO:0000313|EMBL:ETB15353.1,
RC ECO:0000313|Proteomes:UP000018526};
RA Bannantine J.;
RT "Genome sequence of Mycobacterium avium subspecies silvaticum.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETB15353.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYOC01000067; ETB15353.1; -; Genomic_DNA.
DR AlphaFoldDB; V7L1E9; -.
DR PATRIC; fig|1401690.3.peg.379; -.
DR Proteomes; UP000018526; Unassembled WGS sequence.
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:ETB15353.1};
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; 83086 MW; 1668C6997D874C05 CRC64;
MSAEKPTVIY TLTDEAPLLA TYAFLPIVRA FAEPAGIEIK TSDISVAARI LAEFPEHLTE
EQRVPDNLAE LGRLTKLADT NIIKLPNISA SVPQLIAAVK ELQGKGYKIP DFPQSPKTDE
DREIRERYAK CLGSAVNPVL RQGNSDRRAP KAVKEYARKH PHHMAEWSPA SRTHVATMKH
GDFYHGEKSM TLDRARNVKM ELETKSGKTI VLKPMVSLRT GDIIDSMFMS KKALVEFYEQ
QMQDAYETGV MFSLHVKATM MKVSHPIVFG HAVKVFYKEA FAKHQALFDE LGVDVNNGLV
DLYSKIESLP ASLHDEIIRD LHACHEHRPE LAMVDSAKGI TNFHSPSDVI VDASMPAMIR
AGGKMYGADG RQKDTKAVNP ESTFSRIYQE IINFCKTHGA FDPATMGTVP NVGLMAQQAE
EYGSHDKTFE IPEDGVANIV DLDTGEVLLT QNVETGDIWR MPIVRDEPIR DWVKLAVTRA
RNSGMTAVFW LDTERPHEVE LCKKVKEYLK EHDTEGLHIQ IMPQVWAMRY TLERAMRGQD
TIAVTGNILR DYLTDLFPIL ELGTSAKMLS IVPLMSGGGM YETGAGGSAP KHVHQLVEEN
HLRWDSLGEF LALGACFEDI GIKTGNQRAK LLGKTLDAAI GKLLENNKSP SRKTGELDNR
GSQFYLALYW AQELAAQNDD DELRRHFAAL AESLGENEQR IVEELAEVQG RPVDIGGYYQ
PDSEKTTAVM RPSKTFNEAL AASQR
//
