ID   Q2JAX0_FRACC            Unreviewed;       739 AA.
AC   Q2JAX0;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   02-SEP-2026, entry version 112.
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   OrderedLocusNames=Francci3_2203 {ECO:0000313|EMBL:ABD11572.1};
OS   Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
OC   Frankiaceae; Frankia.
OX   NCBI_TaxID=106370 {ECO:0000313|EMBL:ABD11572.1, ECO:0000313|Proteomes:UP000001937};
RN   [1] {ECO:0000313|EMBL:ABD11572.1, ECO:0000313|Proteomes:UP000001937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45818 / CECT 9043 / CcI3
RC   {ECO:0000313|Proteomes:UP000001937};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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|ARBA:ARBA00023554,
CC         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|ARBA:ARBA00046318, ECO:0000256|PIRNR:PIRNR009407}.
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DR   EMBL; CP000249; ABD11572.1; -; Genomic_DNA.
DR   RefSeq; WP_011436619.1; NC_007777.1.
DR   AlphaFoldDB; Q2JAX0; -.
DR   STRING; 106370.Francci3_2203; -.
DR   KEGG; fra:Francci3_2203; -.
DR   eggNOG; COG2838; Bacteria.
DR   HOGENOM; CLU_025308_1_0_11; -.
DR   OrthoDB; 9807643at2; -.
DR   PhylomeDB; Q2JAX0; -.
DR   Proteomes; UP000001937; Chromosome.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   InterPro; IPR004436; Isocitrate_DH_NADP_mono.
DR   NCBIfam; TIGR00178; monomer_idh; 1.
DR   PANTHER; PTHR36999:SF1; ISOCITRATE DEHYDROGENASE (NADP(+)); 1.
DR   PANTHER; PTHR36999; 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|ARBA:ARBA00022435,
KW   ECO:0000256|PIRNR:PIRNR009407};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR009407-3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR009407-3};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR009407};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR009407};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001937};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|PIRNR:PIRNR009407}.
FT   BINDING         82..87
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         132..139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         135
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         145
FT                   /ligand="D-threo-isocitrate"
FT                   /ligand_id="ChEBI:CHEBI:15562"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         348
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         545
FT                   /ligand="D-threo-isocitrate"
FT                   /ligand_id="ChEBI:CHEBI:15562"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         546
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         550
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         582..583
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         587
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         598..600
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         647
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   SITE            255
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT   SITE            418
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ   SEQUENCE   739 AA;  78945 MW;  3FB68196C50F95F2 CRC64;
     MTDSTIIYTH TDEAPALATY SFLPVVQAYA ATAGVSVDSR DISLAGRIIA SFPEDLEEAQ
     RIEDALAELG ELARTPEANI IKLPNISASI PQLKAAIVEL QKRGYALPDY PDDPKTDEER
     EIRARYDKVK GSAVNPVLRE GNSDRRAPAS VKNYARTHPH RMGAWTPDSK TNVATMGAGD
     FRSTEKSTII AAAGTLRIEL AGDDGSTTVL LPSLPVLAGE VVDAAVLRVA ALREFLTAQI
     ARAKAEGVLF SVHLKATMMK VSDPIIFGHV VRAFFPKTFA THGATLAAAG LSPNDGLGGI
     LKGLESLPEG AQIKASFAAE LAEGPALAMV DSDRGITNLH VPSDVIVDAS MPAMIRTSGH
     MWGPDGREAD TLAVLPDSSY AGIYQVAIDD CRAHGAYDPA TMGSVANVGL MAQKAEEYGS
     HDKTFEIPTT GTVRIVDQAG TVVLEQAVAA GDIFRACQTK DAPIRDWVKL AVARARATGD
     PAVFWLDENR AHDARLIEKV RAYLPGHDTS GLRIEIKAPV DAIAFSLERI RRGENTISVT
     GNVLRDYLTD LFPILELGTS AKMLSIVPLM NGGGLFETGA GGSAPKHVQQ LLRENYLRWD
     SLGEFLALAA SFEQFARTTG NARAQVLADT LDRATATFLN EDKSPSRRLG GLDNRGSHFY
     LALYWAQELA AQIGDPRLAE AFAGLAKTLA DQEKAIVDEL IAVQGSPADI GGYYQPDPVK
     AAAVMRPSKI FNEAIASLG
//