(data stored in ACNUC7421 zone)

SWISSPROT: AES_ECODH

ID   AES_ECODH               Reviewed;         319 AA.
AC   B1XFR3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 57.
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=ECDH10B_0432;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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; CP000948; ACB01603.1; -; Genomic_DNA.
DR   RefSeq; WP_000801813.1; NC_010473.1.
DR   ProteinModelPortal; B1XFR3; -.
DR   SMR; B1XFR3; -.
DR   ESTHER; ecoli-Aes; Hormone-sensitive_lipase_like_1.
DR   EnsemblBacteria; ACB01603; ACB01603; ECDH10B_0432.
DR   KEGG; ecd:ECDH10B_0432; -.
DR   eggNOG; ENOG4105F2M; Bacteria.
DR   eggNOG; COG0657; LUCA.
DR   HOGENOM; HOG000117644; -.
DR   KO; K01066; -.
DR   OMA; GIIGMNS; -.
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; B1XFR3.
DR   SWISS-2DPAGE; B1XFR3.
KW   Cytoplasm; Hydrolase; Serine esterase.
FT   CHAIN         1    319       Acetyl esterase.
FT                                /FTId=PRO_1000188982.
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;  4F9E234E23CCE7D0 CRC64;
     MKPENKLPVL DLISAEMKTV VNTLQPDLPP WPATGTIAEQ RQYYTLERRF WNAGAPEMAT
     RAYMVPTKYG QVETRLFCPQ PDSPATLFYL HGGGFILGNL DTHDRIMRLL ASYSQCTVIG
     IDYTLSPEAR FPQAIEEIVA ACCYFHQQAE DYQINMSRIG FAGDSAGAML ALASALWLRD
     KQIDCGKVAG VLLWYGLYGL RDSVTRRLLG GVWDGLTQQD LQMYEEAYLS NDADRESPYY
     CLFNNDLTRE VPPCFIAGAE FDPLLDDSRL LYQTLAAHQQ PCEFKLYPGT LHAFLHYSRM
     MKTADEALRD GAQFFTAQL
//

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