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Database: UniProt
Entry: A0A1H6WFS6_9BURK
LinkDB: A0A1H6WFS6_9BURK
Original site: A0A1H6WFS6_9BURK 
ID   A0A1H6WFS6_9BURK        Unreviewed;       745 AA.
AC   A0A1H6WFS6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=SAMN05518853_101774 {ECO:0000313|EMBL:SEJ14566.1};
OS   Variovorax sp. OK202.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1884311 {ECO:0000313|EMBL:SEJ14566.1, ECO:0000313|Proteomes:UP000199192};
RN   [1] {ECO:0000313|EMBL:SEJ14566.1, ECO:0000313|Proteomes:UP000199192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK202 {ECO:0000313|EMBL:SEJ14566.1,
RC   ECO:0000313|Proteomes:UP000199192};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNZJ01000001; SEJ14566.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6WFS6; -.
DR   Proteomes; UP000199192; 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   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;  82374 MW;  446BB93A69C225A8 CRC64;
     MSSKQPTIVY TLTDEAPLLA TYAFLPIIRA FTNPAGINVT TSDISVAARV LGEFPEFLSD
     AQKVPDNLSE LGKLTLQADA NIIKLPNISA SVSQLKAAIK ELQGKGYKIP DYPESPSTDE
     DKDIRARYNK CTGSAVNPVL REGNSDRRAP NAVKEYARKN PHSMADWSQA SRSHVSHMHG
     GDFYHGEKSM TLDRARNVKM ELITKSGKTI VLKPKIALLD REVIDSMFMS KKALLAFYEK
     EIEDAHKTGV MFSLHVKATM MKVSHPIVFG HCVKIFYKEA FEKHGKLFDE LGINVNNGMV
     DLYTKIATLP QSTQDEIKRD LHACHENRPE LAMVDSAKGI TNFHSPNDVI VDASMPAMIR
     NGGKMWGADG RLKDVKAVMP ESTFARIYQE IINFCKWHGA FDPKTMGTVP NVGLMAQKAE
     EYGSHDKTFE IPEDGVANIT DLDSGEVLMS EDVEQGDIWR MCQVKDAAIR DWVKLAVTRA
     RNSGMPVVFW LDAYRPHEAQ LITKVKMYLH EHNTSGLDIQ IMSQVRAMRY TLERVVRGLD
     TISATGNILR DYLTDLFPIM ELGTSAKMLS IVPLMAGGGL YETGAGGSAP KHVQQLVEEN
     HLRWDSLGEF LALAVSLEDL GLKTGNKQAA ILARTLDTAT GKLLDNNKNP SPKTGQLDNR
     GSQFYLAMYW AQELAAQTED KDLQAKFKKL AETLTSNEQK IVDELAAVQG KAVDIGGYYL
     ADPEKYAAVM RPSATLNATL ASAQA
//
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