ID Q7WV62_ECOLX Unreviewed; 389 AA.
AC Q7WV62;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|RuleBase:RU004446};
DE EC=1.1.1.42 {ECO:0000256|RuleBase:RU004446};
DE Flags: Fragment;
GN Name=icd {ECO:0000313|EMBL:AAN06324.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:AAN06324.1};
RN [1] {ECO:0000313|EMBL:AAN06324.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ECOR4 {ECO:0000313|EMBL:AAN06324.1};
RX PubMed=15022774; DOI=10.1016/S1055-7903(03)00181-7;
RA Escobar-Paramo P., Sabbagh A., Darlu P., Pradillon O., Vaury C.,
RA Denamur E., Lecointre G.;
RT "Decreasing the effects of horizontal gene transfer on bacterial phylogeny:
RT the Escherichia coli case study.";
RL Mol. Phylogenet. Evol. 30:243-250(2004).
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|ARBA:ARBA00023554};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR604439-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR604439-3};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000256|PIRSR:PIRSR604439-3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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DR EMBL; AY132828; AAN06324.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7WV62; -.
DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004439; Isocitrate_DH_NADP_dimer_prok.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR NCBIfam; TIGR00183; prok_nadp_idh; 1.
DR PANTHER; PTHR43504; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR PANTHER; PTHR43504:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 3: Inferred from homology;
KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435,
KW ECO:0000256|RuleBase:RU004446};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR604439-3};
KW Manganese {ECO:0000256|PIRSR:PIRSR604439-3, ECO:0000256|RuleBase:RU004446};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004446};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR604439-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU004446}.
FT DOMAIN 13..388
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-3"
FT BINDING 325..331
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 338
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 377
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 381
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT SITE 146
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT SITE 216
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT MOD_RES 86
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 228
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAN06324.1"
FT NON_TER 389
FT /evidence="ECO:0000313|EMBL:AAN06324.1"
SQ SEQUENCE 389 AA; 42875 MW; 0B22C66769F4C746 CRC64;
TLQNGKLNVP ENPITPYIEG DGIGVDVTPA MLKVVDAAGE KAYKGERKIS WMEIYTGEKS
TQVYGQDVWL PAETLDLIRE YRVAIKGRMT TPDGGGIRSL NVALRQELDL YICLRPVRYY
QGTPSPVKHP ELTDMVIFRE NSEDIYAGIE WKADSADAEK VIKFLREEMG VKKIRFPEHC
GIGIKPCSEE GTKRLVRAAI EYAIANDRDS VTLVHKGNIM KFTEGAFKDW GYQLAREEFG
GELIDGGPWL KVKNPNTGKE IVIKDVIADA FLQQILLRPA EYDVIACMNL NGDYISDALA
AQVGGIGIAP GANIGDECAL FEATHGTAPK YAGQDKVNPG SIILSAEMML RHMGWTEAAD
LIVKGMEGAI NAKTVTYDFE RLMEGAKLL
//
