ID A0A1P8JZW8_9BURK Unreviewed; 745 AA.
AC A0A1P8JZW8;
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=RD110_20520 {ECO:0000313|EMBL:APW39304.1};
OS Rhodoferax koreense.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=1842727 {ECO:0000313|EMBL:APW39304.1, ECO:0000313|Proteomes:UP000186609};
RN [1] {ECO:0000313|EMBL:APW39304.1, ECO:0000313|Proteomes:UP000186609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCY110 {ECO:0000313|EMBL:APW39304.1,
RC ECO:0000313|Proteomes:UP000186609};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
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; CP019236; APW39304.1; -; Genomic_DNA.
DR RefSeq; WP_076201589.1; NZ_CP019236.1.
DR AlphaFoldDB; A0A1P8JZW8; -.
DR STRING; 1842727.RD110_20520; -.
DR KEGG; rhy:RD110_20520; -.
DR OrthoDB; 9807643at2; -.
DR Proteomes; UP000186609; 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};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR009407};
KW Reference proteome {ECO:0000313|Proteomes:UP000186609};
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; 82098 MW; 91E189E17BC4EADE CRC64;
MATAKSKIIY TLTDEAPFLA TAAFLPVVRT FAAPAGIEVA EADISVAGRV LAEFPEYLTD
AQKVPATLAE LGRLTLLPDT NIIKLPNISA SVGQLQACIK ELQAKGFAIP DFPEDPKTEE
EKAIRARYSK CIGSAVNPVL REGNSDRRAP KAVKEYARKN PHSMAEWSQA SRSHVSHMHS
GDFYHGEKSL TLDKARDVKM ELITKSGKTV VLKPKVSLKD GEIIDSMFMS KKALVEFYEK
EIEDAHKTGV MFSLHVKATM MKVSHPIVFG HCVKIFYKDA FAKHGKLFDE LGVNVNNGMA
NLYDKVATLP TAKREEVLKD LHACHANRPE LAMVDSAKGI TNFHSPNDII VDASMPAMIR
NGGKMWGADG RLKDVKAVMP ESTFARIYQE IINFCKWHGA FDPKTMGTVP NVGLMAQQAE
EYGSHDKTFE IAEDGVANIV DLATGEILLT QNVEEGDIWR MCQVKDAAIR DWVKLAVTRA
RNSGMPAVFW LDPYRPHENE VIKKVQTYLK EHDTSGLHIE IMSQVRAMRY TLERVIRGLD
TISVTGNILR DYLTDLFPIM ELGTSAKMLS IVPLMAGGGM YETGAGGSAP KHVQQLVEEN
HLRWDSLGEF LALAVSLEDL GIKTGNTQAK LLAKTLDAAT GKLLDNNKGP SPKTGQLDNR
GSQFYIAMYW AQALAEQTED KALQAHFAKL AKTLTEKEAE IVEELRVVQG KPVDIGGYYK
PDTQKTAEVM RPSPTFNAAI AAAQV
//
