ID A0A1P8LZ69_9MICC Unreviewed; 739 AA.
AC A0A1P8LZ69;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=BWQ92_04310 {ECO:0000313|EMBL:APX01053.1};
OS Arthrobacter sp. QXT-31.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1357915 {ECO:0000313|EMBL:APX01053.1, ECO:0000313|Proteomes:UP000186821};
RN [1] {ECO:0000313|EMBL:APX01053.1, ECO:0000313|Proteomes:UP000186821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QXT-31 {ECO:0000313|EMBL:APX01053.1,
RC ECO:0000313|Proteomes:UP000186821};
RA Liang J.S.;
RT "Microbe-microbe interactions indirectly alter the fate of arsenic in
RT presence of MnII.";
RL Submitted (JAN-2017) 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; CP019304; APX01053.1; -; Genomic_DNA.
DR RefSeq; WP_076798447.1; NZ_CP019304.1.
DR AlphaFoldDB; A0A1P8LZ69; -.
DR STRING; 1357915.BWQ92_04310; -.
DR KEGG; arq:BWQ92_04310; -.
DR OrthoDB; 9807643at2; -.
DR Proteomes; UP000186821; 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 Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT BINDING 80..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 130..137
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 133
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 348
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 545
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 546
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 550
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
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 253
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; 79663 MW; 49220A13CE0A7EE6 CRC64;
MAKIIYTHTD EAPMLATYSF LPIIEAFAST AGVQVETRDI SLAGRIIAVF GDYLTEEQRI
GDALAELGEL AKKPEANIIK LPNISASVPQ LKAAIAELQS QGYKLPDYPD NPTSDEETAI
RSRYDKIKGS AVNPVLREGN SDRRAPLSVK NYARQNPHSM GAWTPESKTN VAHMDANDFR
SNEQSVVVPA DGTIEIQLVR EDGTVKVLKK AFPVLAGEVI DGTVMRAAAL DEFLAAQVTR
AKEEGVLFSA HLKATMMKVS DPIIFGHVVK AYFSELFDTY GKQLAAAGLS PNNGLASILN
GLDELPEDVR EGVQTAIKKG LEEGPALAMV DSDKGITNLH VPSDVIVDAS MPAMIRTSGH
MWGPDGQEAD TLAVLPDSSY AGIYQVVIDD CRANGAFDPT TMGTVPNVGL MAQAAEEYGS
HDKTFEAQVP GKIQVVDGSG NVLIEHEVAP GDIWRACQTK DLAIRDWVKL AVNRARASQT
PAVFWLDEAR AHDAKLIGKV REYLQEHDTE GLQIEILSPV KATAFTLERI RKGEDTISVT
GNVLRDYLTD LFPILELGTS AKMLSIVPLI NGGGLFETGA GGSAPKHVQQ LLKENHLRWD
SLGEFLALAV SFEHLANTTD NARAQVLADT LDRATGTFLL ENKSPSRKAG EIDNRGSHYY
LAQYWAQELA KQTEDADLAA SFAPVAEALT SNEDAIVSEL LGAQGQPADI GGYYHPDAEK
AAAVMRPSAT LNKIVASLG
//
