ID   A1VTJ8_POLNA            Unreviewed;       745 AA.
AC   A1VTJ8;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 91.
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=Pnap_3680 {ECO:0000313|EMBL:ABM38976.1};
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044 {ECO:0000313|EMBL:ABM38976.1, ECO:0000313|Proteomes:UP000000644};
RN   [1] {ECO:0000313|Proteomes:UP000000644}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2 {ECO:0000313|Proteomes:UP000000644};
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(2009).
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; CP000529; ABM38976.1; -; Genomic_DNA.
DR   RefSeq; WP_011803042.1; NC_008781.1.
DR   AlphaFoldDB; A1VTJ8; -.
DR   STRING; 365044.Pnap_3680; -.
DR   KEGG; pna:Pnap_3680; -.
DR   eggNOG; COG2838; Bacteria.
DR   HOGENOM; CLU_025308_1_0_4; -.
DR   OrthoDB; 9807643at2; -.
DR   Proteomes; UP000000644; 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   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};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR009407,
KW   ECO:0000313|EMBL:ABM38976.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000644};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT   BINDING         134..141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
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   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;  82437 MW;  FA1F3F6567DD1086 CRC64;
     MTAGKSKIIY TLTDEAPLLA TWSFLPVVRA FTAPAGIEVA ESDISVAARV LAEFPEFLSD
     AQKVPNTLAE LGRLTQDPDT NIIKLPNISA SQGQLVSAIK ELQSKGFNLP DYPESPKSDE
     DKAIRARYAR CIGSSVNPVL REGNSDRRAP LAVKNYARKN PHSMADWSQA SRSHVSHMHH
     GDFYHGEKSM TLDKARDVKM ELITKSGKTI VLKPLTKLLD REVIDSMFMS KKELLDFYEQ
     EIDDAYKTGV MFSLHVKATM MKVSHPIVFG HCVKIFYKDA FEKHAKLFDE LGVNVNNGMA
     NLYDKISTLP QSTQDEIKRD LHACHEHRPE LAMVDSAKGI TNFHSPNDVI VDASMPAMIR
     NGGKMWGADG RLKDVKAVMP ESTFARIYQE IINFCKWHGA FDPKTMGTVP NVGLMAQQAE
     EYGSHDKTFE ISEDGVANIT DVATGEVLLS QNVEAGDIWR MCQCKDAAIR DWVKLAVNRA
     RNSGMPVVFW LDAYRPHEAQ LITKVKMYLH EHNTSGLDIQ IMSQVRAMRY TLERVVRGQD
     TISATGNILR DYLTDLFPIM ELGTSAKMLS IVPLMAGGGM YETGAGGSAP KHVQQLVEEN
     HLRWDSLGEF LALAVSLEDL GIKTGNDQAK LLAKTLDAAT GKLLDNNKGP KTRTGELDNR
     GSHFYLAMYW AQALAEQTQD AALQARFAPL AKSLAENEAQ IVAEFKEVQG KPVDIGGYYL
     LDAEKVKAVM RPSATFNAVL SAAQA
//