ID   Q5NET6_FRATT            Unreviewed;       747 AA.
AC   Q5NET6;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 107.
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=idh {ECO:0000313|EMBL:CAG46159.1};
GN   OrderedLocusNames=FTT_1526c {ECO:0000313|EMBL:CAG46159.1};
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416 {ECO:0000313|EMBL:CAG46159.1, ECO:0000313|Proteomes:UP000001174};
RN   [1] {ECO:0000313|EMBL:CAG46159.1, ECO:0000313|Proteomes:UP000001174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4 {ECO:0000313|Proteomes:UP000001174};
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M., Duffield M., Fuxelius H.H.,
RA   Garcia E., Halltorp G., Johansson D., Isherwood K., Karp P., Larsson E.,
RA   Lui Y., Michell S., Prior J., Prior R., Sjostedt A., Svensson K.,
RA   Thompson N., Vergez L., Wagg J., Wren B., Lindler L.E., Andersson S.G.,
RA   Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG46159.1; -; Genomic_DNA.
DR   RefSeq; YP_170456.1; NC_006570.2.
DR   AlphaFoldDB; Q5NET6; -.
DR   IntAct; Q5NET6; 2.
DR   DNASU; 3192248; -.
DR   EnsemblBacteria; CAG46159; CAG46159; FTT_1526c.
DR   KEGG; ftu:FTT_1526c; -.
DR   OrthoDB; 9807643at2; -.
DR   Proteomes; UP000001174; 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:CAG46159.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001174};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT   BINDING         89..94
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         139..146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         142
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         357
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         554
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         555
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         559
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         591..592
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         596
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         607..609
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         656
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   SITE            262
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT   SITE            427
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ   SEQUENCE   747 AA;  83454 MW;  0DA5A2486A37EEFD CRC64;
     MKFYLQEIFM HKIFYTFTDE APALATGSFL PIVESFTKVA DIELETKDIS LSARILANFN
     DYLTAEQKCS DDLAILGELA KTPDANIIKL PNISASIPQL TAAIKELQSK GYKIPDYPYE
     PKDDKEQEIK ARYAKVLGSA VNPVLREGNS DRRVADAVKK YAEKHPHSMG EWTKDSKSHV
     ASMSADDFYA NEKSYIVPKA TKVKIVHIDT KGTQTVLKDN LALEEKEIID ATKISIKALR
     EFYKNEIAKA KKEGTLLSLH LKATMMKVSD PILFGHAVEI FFEDIFKKYA KEFKELGVNP
     RNGWGDAVEK IKQLPQELQD KINADIEKVF AKQPDIAMVN SNKGITNLNV PSDVIIDASM
     PAAIRSSGKM WNKDGKLQDM KAMIPDRCYA GVYAATIDFC KENGAFDVAT MGDVSNVGLM
     AKKAEEYGSH DKTFEIQADG KVEVIDAEGN VIFEHQVEKG DIWRACQTKD IAVKDWVKLV
     VNRAKITQNP AIFWLDSKRA HDRNLIAKVN EYLTHHDTTG LDIQILSPVE ATKYSLKRMK
     EGKNTISVTG NVLRDYLTDL FPILELGTSA KMLSIVPLLA GGGLFETGAG GSAPKHVEQL
     IEENHLRWDS LGEFLALGAS LEDLAIKTRD AKIKVLAETL SQANKDFLDN DKSPRRKVGE
     LDTRGSHFYL AYYWVKALAE QTGNAELKAK FEPIYIELKA NKDKIVKELN DAQGKKVDVG
     GYYHMDRVKL DAVMRPSKTF NTILAQI
//