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Database: UniProt
Entry: Q5IQL0_9ESCH
LinkDB: Q5IQL0_9ESCH
Original site: Q5IQL0_9ESCH 
ID   Q5IQL0_9ESCH            Unreviewed;       208 AA.
AC   Q5IQL0;
DT   15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2005, sequence version 1.
DT   24-JAN-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:AAU86508.1};
OS   Escherichia albertii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=208962 {ECO:0000313|EMBL:AAU86508.1};
RN   [1] {ECO:0000313|EMBL:AAU86508.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=9194 {ECO:0000313|EMBL:AAU86508.1};
RX   PubMed=15629933; DOI=10.1128/JB.187.2.619-628.2005;
RA   Hyma K.E., Lacher D.W., Nelson A.M., Bumbaugh A.C., Janda J.M.,
RA   Strockbine N.A., Young V.B., Whittam T.S.;
RT   "Evolutionary genetics of a new pathogenic Escherichia species: Escherichia
RT   albertii and related Shigella boydii strains.";
RL   J. Bacteriol. 187:619-628(2005).
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; AY696895; AAU86508.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5IQL0; -.
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:InterPro.
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..208
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
FT   BINDING         8
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         32
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         186
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-3"
FT   SITE            39
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT   SITE            109
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT   MOD_RES         21
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT   MOD_RES         121
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAU86508.1"
FT   NON_TER         208
FT                   /evidence="ECO:0000313|EMBL:AAU86508.1"
SQ   SEQUENCE   208 AA;  23059 MW;  96B9031D1047BB03 CRC64;
     LDLYICLRPV RYYQGTPSPV KHPELTDMVI FRENSEDIYA GIEWKADSAD AEKVIKFLRE
     EMGVKKIRFP EHCGIGIKPC SEEGTKRLVR AAIEYAIAND RDSVTLVHKG NIMKFTEGAF
     KDWGYQLARE EFGGELIDGG PWLKVKNPNT GKEIVIKDVI ADAFLQQILL RPAEYDVIAC
     MNLNGDYISD ALAAQVGGIG IAPGANIG
//
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