ID Q47BD1_DECAR Unreviewed; 745 AA.
AC Q47BD1;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 99.
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=Daro_3120 {ECO:0000313|EMBL:AAZ47850.1};
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087 {ECO:0000313|EMBL:AAZ47850.1};
RN [1] {ECO:0000313|EMBL:AAZ47850.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RCB {ECO:0000313|EMBL:AAZ47850.1};
RA Salinero K.K., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S.,
RA Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.;
RT "Complete sequence of Dechloromonas aromatica RCB.";
RL Submitted (AUG-2005) 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; CP000089; AAZ47850.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47BD1; -.
DR SMR; Q47BD1; -.
DR STRING; 159087.Daro_3120; -.
DR KEGG; dar:Daro_3120; -.
DR eggNOG; COG2838; Bacteria.
DR HOGENOM; CLU_025308_1_0_4; -.
DR OrthoDB; 9807643at2; -.
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 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; 82777 MW; 143B883606DDA2CE CRC64;
MAGGKSKIIY TLTDEAPLLA TCAFLPIIRT FTGPAGIEIE KADISVSARV LSEFSEFLTD
EQKVPNTLGE LGKKCLLPET NIIKLPNISA SVAQLKACVK ELQEKGYKIP DYPETANTDE
DKALKARFGK CLGSAVNPVL REGNSDRRAP GAVKNYAKKR PHSMGEWKQW SQTHVSHMEH
GDFYHGEKSM TLDKPREVRM ELIAKGGKTT VLKPKLSLLE GEIIDSMFMS KKALCDFYEA
QLEDCREAGI LFSLHVKATM MKVSHPIVFG HCVKIYYKEA FEKHAKTFDE LGINVNNGMV
DLYDKIKNLP ESKRDEIIRD LHACQEHRPR LAMVDSAKGI TNFHSPNDII VDASMPAMIR
QGGKMWGADG KQYDSKCVMP ESTFARIYQE MINFVKWHGN FDPRTMGTVP NVGLMAQQAE
EYGSHDKTFE IAEDGIANIV DNATGEVLLT QNVEAGDIWR MCQVKDAPIR DWVKLAVTRA
RQSGMPAIFW LDAYRPHENE LIKKVQKYLK DHDTSGLDIQ IMSQVRAMRF TLERVARGLD
TISVTGNILR DYLTDLFPIM ELGTSAKMLS IVPLMNGGGM YETGAGGSAP KHVQQLTQEN
HLRWDSLGEF LALAVSLEEQ GIKDGNKRAV LLAKTLDAAT GKLLDNNKSP SPKTGELDNR
GSQFYLAMYW AQELAAQKED AELAAHFAKL AKALSDNEGQ IVAEMKSVQG RPVDIGGYYK
ADAEKCKAVM RPSPTLNAAL KAARI
//
