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Database: UniProt
Entry: C5T7J6_ACIDE
LinkDB: C5T7J6_ACIDE
Original site: C5T7J6_ACIDE 
ID   C5T7J6_ACIDE            Unreviewed;       745 AA.
AC   C5T7J6;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 57.
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=AcdelDRAFT_2876 {ECO:0000313|EMBL:EER59552.1};
OS   Acidovorax delafieldii 2AN.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=573060 {ECO:0000313|EMBL:EER59552.1, ECO:0000313|Proteomes:UP000003856};
RN   [1] {ECO:0000313|EMBL:EER59552.1, ECO:0000313|Proteomes:UP000003856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2AN {ECO:0000313|EMBL:EER59552.1,
RC   ECO:0000313|Proteomes:UP000003856};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Shelobolina E.S.,
RA   Picardal F., Roden E., Emerson D.;
RT   "The draft genome of Acidovorax delafieldii 2AN.";
RL   Submitted (MAY-2009) 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:EER59552.1}.
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DR   EMBL; ACQT01000116; EER59552.1; -; Genomic_DNA.
DR   RefSeq; WP_005797820.1; NZ_ACQT01000116.1.
DR   AlphaFoldDB; C5T7J6; -.
DR   PATRIC; fig|573060.9.peg.2182; -.
DR   OrthoDB; 9807643at2; -.
DR   Proteomes; UP000003856; 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   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:EER59552.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003856};
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;  82429 MW;  C0ABD1350E25D819 CRC64;
     MSTQQPTIIY TLTDEAPRLA TASFLPIIRT FAAPAGINVT ESDISVAARV LGEFPEFLRD
     DQKVPNTLAE LGKKTLQADA NIIKLPNISA SVGQLITCIK ELQSKGYAVP DYPEDPKTEE
     EKAIRARYAK CIGSAVNPVL REGNSDRRAP KAVKEYARKN PHSMAEWSQA SRSHVSHMHA
     GDFYHGEKSI TLDRARDVKM ELITKSGKTV VLKPKVSLLD REIIDSMFMS KKALLEFYER
     EIEDARKTGV MFSLHVKATM MKVSHPIVFG HCVKIFYKDA FEKHAKLFEE LGVNVNNGMA
     NLYDKISTLP QSKQDEIKRD LHACHEHRPE LAMVDSAKGI TNFHSPNDVI VDASMPAMIR
     NGGKMWGADG RLKDVKAVMP ESTFARIYQE IINFCKWHGA FDPKTMGTVP NVGLMAQQAE
     EYGSHDKTFE IPEDGVANIT DLATGEVLLS QNVEAGDIWR MCQVKDAAIR DWVKLAVNRA
     RNSGMPVVFW LDSYRPHEAQ LITKVKMYLH EHDTTGLDIQ IMSQVRAMRY TLERVIRGQD
     TISATGNILR DYLTDLFPIM ELGTSAKMLS IVPLMAGGGM YETGAGGSAP KHVQQLVEEN
     HLRWDSLGEF LALAVSLEDL GLKTGNAKAK VLSKTLDAAT GKLLDNNKNP SPKTGQLDNR
     GSQFYLALFW AQELAAQTDD AELAKLFAPL AQKLAANEQK IVDELNAVQG KPADIGGYYL
     PDLAKLDAVM RPSQTFNGTL ATLGA
//
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