(data stored in ACNUC7421 zone)

SWISSPROT: AES_ECO57

ID   AES_ECO57               Reviewed;         319 AA.
AC   Q8XD38; Q7AGY3;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 98.
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=Z0593, ECs0529;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG54825.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33952.1; -; Genomic_DNA.
DR   PIR; A90695; A90695.
DR   PIR; E85545; E85545.
DR   RefSeq; NP_308556.1; NC_002695.1.
DR   RefSeq; WP_000801803.1; NZ_MWVM01000009.1.
DR   ProteinModelPortal; Q8XD38; -.
DR   SMR; Q8XD38; -.
DR   STRING; 155864.Z0593; -.
DR   ESTHER; ecoli-Aes; Hormone-sensitive_lipase_like_1.
DR   EnsemblBacteria; AAG54825; AAG54825; Z0593.
DR   EnsemblBacteria; BAB33952; BAB33952; BAB33952.
DR   GeneID; 914633; -.
DR   KEGG; ece:Z0593; -.
DR   KEGG; ecs:ECs0529; -.
DR   PATRIC; fig|386585.9.peg.636; -.
DR   eggNOG; ENOG4105F2M; Bacteria.
DR   eggNOG; COG0657; LUCA.
DR   HOGENOM; HOG000117644; -.
DR   KO; K01066; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
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; Q8XD38.
DR   SWISS-2DPAGE; Q8XD38.
KW   Complete proteome; Cytoplasm; Hydrolase; Serine esterase.
FT   CHAIN         1    319       Acetyl esterase.
FT                                /FTId=PRO_0000239706.
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;  36034 MW;  508621C1DCD4E8DD CRC64;
     MKPENKLPVL DLISAEMKTV VNTLQPDLPP WPATGTIAEQ RQYYTLERRF WNAGAPEMAT
     KAYMVPTKYG QVETRLFCPQ PDSPATLFYL HGGGFILGNL DTHDRIMRLL ASYSQCTVIG
     IDYTLSPEAR FPQVIEEIVA ACCYFHQQAE DYQINMSRIG FAGDSAGAML ALASALWLRD
     KQIDCGKVAG VLLWYGLYGL RDSVTRRLLG GVWDGLTQQD LQMYEEAYLS NDADRESPYY
     CLFNNDLTRE VPPCFIAGAE FDPLLDDSRL LYQTLAAHQQ PCEFKLYPGT LHAFLHYSRM
     MKTADEALRD GAQFFTAQL
//

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