ID A6MIM3_ECOLX Unreviewed; 189 AA.
AC A6MIM3;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=isocitrate dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00013013};
DE EC=1.1.1.42 {ECO:0000256|ARBA:ARBA00013013};
DE Flags: Fragment;
GN Name=icdA {ECO:0000313|EMBL:ABO70213.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ABO70213.1};
RN [1] {ECO:0000313|EMBL:ABO70213.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H10124 {ECO:0000313|EMBL:ABO70214.1}, and H9513
RC {ECO:0000313|EMBL:ABO70213.1};
RX PubMed=17570118; DOI=10.1086/518897;
RA Bidet P., Mahjoub-Messai F., Blanco J., Blanco J., Dehem M., Aujard Y.,
RA Bingen E., Bonacorsi S.;
RT "Combined multilocus sequence typing and O serogrouping distinguishes
RT Escherichia coli subtypes associated with infant urosepsis and/or
RT meningitis.";
RL J. Infect. Dis. 196:297-303(2007).
RN [2] {ECO:0000313|EMBL:ADI43005.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S31ST15OCT {ECO:0000313|EMBL:ADI43005.1}, S31ST23OCT
RC {ECO:0000313|EMBL:ADI43110.1}, and S5ST23JUL
RC {ECO:0000313|EMBL:ADI43073.1};
RX PubMed=21075897; DOI=10.1128/AEM.01880-10;
RA Bergholz P.W., Noar J.D., Buckley D.H.;
RT "Environmental patterns are imposed on the population structure of
RT Escherichia coli after fecal deposition.";
RL Appl. Environ. Microbiol. 77:211-219(2011).
RN [3] {ECO:0000313|EMBL:AFS17905.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SB02 {ECO:0000313|EMBL:AFS17905.1};
RA Perchec-Merien A.-M., Lewis G.D.;
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AFS17905.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SB02 {ECO:0000313|EMBL:AFS17905.1};
RX PubMed=22974403; DOI=10.1111/1574-6941.12010;
RA Perchec-Merien A.M., Lewis G.D.;
RT "Naturalized Escherichia coli from New Zealand wetland and stream
RT environments.";
RL FEMS Microbiol. Ecol. 83:494-503(2013).
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; EF141428; ABO70213.1; -; Genomic_DNA.
DR EMBL; EF141429; ABO70214.1; -; Genomic_DNA.
DR EMBL; HM222134; ADI43005.1; -; Genomic_DNA.
DR EMBL; HM222202; ADI43073.1; -; Genomic_DNA.
DR EMBL; HM222239; ADI43110.1; -; Genomic_DNA.
DR EMBL; JX467914; AFS17905.1; -; Genomic_DNA.
DR AlphaFoldDB; A6MIM3; -.
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 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 Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR604439-3};
KW Manganese {ECO:0000256|PIRSR:PIRSR604439-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 1..189
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-3"
FT SITE 25
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT SITE 95
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT MOD_RES 7
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 107
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABO70213.1"
FT NON_TER 189
FT /evidence="ECO:0000313|EMBL:ABO70213.1"
SQ SEQUENCE 189 AA; 20868 MW; 84E62BEA04F83586 CRC64;
GTPSPVKHPE LTDMVIFREN SEDIYAGIEW KADSADAEKV IKFLREEMGV KKIRFPEHCG
IGIKPCSEEG TKRLVRAAIE YAIANDRDSV TLVHKGNIMK FTEGAFKDWG YQLAREEFGG
ELIDGGPWMK VKNPNTGKEI VIKDVIADAF LQQILLRPAE YDVIACMNLN GDYISDALAA
QVGGIGIAP
//
