ID A0A0M4SY75_9GAMM Unreviewed; 738 AA.
AC A0A0M4SY75;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=AOC03_08045 {ECO:0000313|EMBL:ALF59998.1};
OS Psychrobacter urativorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=45610 {ECO:0000313|EMBL:ALF59998.1, ECO:0000313|Proteomes:UP000059847};
RN [1] {ECO:0000313|EMBL:ALF59998.1, ECO:0000313|Proteomes:UP000059847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R10.10B {ECO:0000313|EMBL:ALF59998.1,
RC ECO:0000313|Proteomes:UP000059847};
RA See-Too W.S., Chan K.G.;
RT "Complete genome of Psychrobacter urativorans R10.10B.";
RL Submitted (SEP-2015) 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; CP012678; ALF59998.1; -; Genomic_DNA.
DR RefSeq; WP_062534928.1; NZ_CP012678.1.
DR AlphaFoldDB; A0A0M4SY75; -.
DR STRING; 45610.AOC03_08045; -.
DR KEGG; pur:AOC03_08045; -.
DR OrthoDB; 9807643at2; -.
DR Proteomes; UP000059847; 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 ECO:0000313|EMBL:ALF59998.1};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT REGION 102..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 738 AA; 81546 MW; 5F7702BC6BB65E08 CRC64;
MTKIIYTKTD EAPALATLSF LPIVQAFTKT AGIEIETADI SLAGRIIALF SEFLPEEQRI
PSAFVALSEL VKQPGANIIK LPNISASIPQ LKAAIKELQD KGYDLPDYPD HPETDKEKDA
RERYDKIKGS AINPVLREGN SDRRAPKAVK AFARNHPHSM GAWSADSKSH VATMQHGDFA
DTEQSVTLDK ATDYRIEFTA EDGTVTELKA PAPLLAGELI DAAILSHTAL VEFLEEQVED
AKAEDVLFSL HLKATMMKVS DPIIFGEAVK IFFKELFAKH GDTFKELDVN VNNGFSNLLA
KIQELPEAKR KEIEADIQTI YKNNPDLAMV DSAKGITNLH VPSDVIVDAS MPAMIRSSGK
MWGADNELHD TKAVIPDSSY ACIYDETIKF SKEHGAFDPT TMGSVPNVGL MAQKAEEYGS
HDKTFLIPSA GKVQVLDSEG NVLTEHQVEA EDIWRMNQVK DAPIQDWVKL AVTRARASGI
PTVFWLNHKR PHHAELIKKV EKYLKDYDTT GLDIRIMPVR EATRFTLERL KEGKDTISVT
GNVLRDYLTD LFPILELGTS AKMLSIVPLM NGGGLFETGA GGSAPKHVQQ LVEENHLRWD
SLGEFLALAV SLEHLAVKND NAKAQILADT LDKATEKLLL NNKSPSRKTG ELDNRGSHFY
LAMYWAQELA AQTEDKELAA QFAPLAEKLA SNEDAIVKEL NDVQGQPANI DGYYFFDEAL
ATKVMRPSQL LNDTIDSL
//
