(data stored in ACNUC7421 zone)

SWISSPROT: AES_ECO27

ID   AES_ECO27               Reviewed;         319 AA.
AC   B7UKF6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=Acetyl esterase {ECO:0000255|HAMAP-Rule:MF_01958};
DE            EC=3.1.1.- {ECO:0000255|HAMAP-Rule:MF_01958};
GN   Name=aes {ECO:0000255|HAMAP-Rule:MF_01958};
GN   OrderedLocusNames=E2348C_0411;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Displays esterase activity towards short chain fatty
CC       esters (acyl chain length of up to 8 carbons). Able to hydrolyze
CC       triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin),
CC       but not trioleylglycerol (triolein) or cholesterol oleate.
CC       Negatively regulates MalT activity by antagonizing maltotriose
CC       binding. Inhibits MelA galactosidase activity. {ECO:0000255|HAMAP-
CC       Rule:MF_01958}.
CC   -!- SUBUNIT: Homodimer. Interacts with MalT and MelA.
CC       {ECO:0000255|HAMAP-Rule:MF_01958}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01958}.
CC   -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC       {ECO:0000255|HAMAP-Rule:MF_01958}.
DR   EMBL; FM180568; CAS07959.1; -; Genomic_DNA.
DR   RefSeq; WP_000801821.1; NC_011601.1.
DR   SMR; B7UKF6; -.
DR   ESTHER; ecoli-Aes; Hormone-sensitive_lipase_like.
DR   EnsemblBacteria; CAS07959; CAS07959; E2348C_0411.
DR   KEGG; ecg:E2348C_0411; -.
DR   KO; K01066; -.
DR   OMA; HPFIAMD; -.
DR   BioCyc; ECOL574521:E2348C_RS02155-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_01958; Acetyl_esterase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   InterPro; IPR023508; Acetyl_esterase.
DR   InterPro; IPR002168; Lipase_GDXG_HIS_AS.
DR   InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
DR   PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UKF6.
DR   SWISS-2DPAGE; B7UKF6.
KW   Complete proteome; Cytoplasm; Hydrolase; Serine esterase.
FT   CHAIN         1    319       Acetyl esterase.
FT                                /FTId=PRO_1000188975.
FT   MOTIF        91     93       Involved in the stabilization of the
FT                                negatively charged intermediate by the
FT                                formation of the oxyanion hole.
FT                                {ECO:0000250|UniProtKB:Q5NUF3}.
FT   ACT_SITE    165    165       {ECO:0000255|HAMAP-Rule:MF_01958}.
FT   ACT_SITE    262    262       {ECO:0000255|HAMAP-Rule:MF_01958}.
FT   ACT_SITE    292    292       {ECO:0000255|HAMAP-Rule:MF_01958}.
SQ   SEQUENCE   319 AA;  36103 MW;  344A1F65AD6D82D4 CRC64;
     MKPENKLPVL DLISAEMKTV VNTLQPDLPP WPATGTIAEQ RQYYTLERRF WNVGAPEMAT
     RAYRVPTKYG QVKTRIFYPQ PDSPATLFYL HGGGFILGNL DTHDRIMRLL ASYSQCTVIG
     IDYTLSPEAR FPQAIEEIVA ACCYFHQQAE DYQINMSRIG FAGDSAGAML ALASALWLRD
     KQIDCGKVAG VLLWYGLYGL RDSVTRRLLG GVWDGLTQQD LQMYEEAYLS NDADRESPYY
     CLFNNDLTRE VPPCFIAGAE FDPLLDDSRL LYQTLAAHQQ PCEFKLYPGT LHAFLHYSRM
     MKTADEALLD GAQFFTAQL
//

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