AES_ECOLI
ID AES_ECOLI Reviewed; 319 AA.
AC P23872; P77282; Q2MBV1;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Acetyl esterase;
DE EC=3.1.1.-;
DE AltName: Full=EcE;
GN Name=aes; Synonyms=ybaC; OrderedLocusNames=b0476, JW0465;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=9401025; DOI=10.1128/jb.179.24.7679-7686.1997;
RA Peist R., Koch A., Bolek P., Sewitz S., Kolbus T., Boos W.;
RT "Characterization of the aes gene of Escherichia coli encoding an enzyme
RT with esterase activity.";
RL J. Bacteriol. 179:7679-7686(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2051480; DOI=10.1016/0022-2836(91)90180-e;
RA Miyamoto K., Nakahigashi K., Nishimura K., Inokuchi H.;
RT "Isolation and characterization of visible light-sensitive mutants of
RT Escherichia coli K12.";
RL J. Mol. Biol. 219:393-398(1991).
RN [3]
RP SEQUENCE REVISION.
RA Miyamoto K.;
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-103.
RC STRAIN=K12;
RX PubMed=7721718; DOI=10.1128/jb.177.8.2236-2240.1995;
RA Harlow K.W., Nygaard P., Hove-Jensen B.;
RT "Cloning and characterization of the gsk gene encoding guanosine kinase of
RT Escherichia coli.";
RL J. Bacteriol. 177:2236-2240(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RC STRAIN=K12;
RA Mori H., Iida A., Teshiba S., Fujio T.;
RL Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, SUBCELLULAR LOCATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9576853; DOI=10.1042/bj3320075;
RA Kanaya S., Koyanagi T., Kanaya E.;
RT "An esterase from Escherichia coli with a sequence similarity to hormone-
RT sensitive lipase.";
RL Biochem. J. 332:75-80(1998).
RN [10]
RP MUTAGENESIS OF HIS-103; GLU-128; GLY-163; ASP-164; SER-165; GLY-167;
RP ASP-262; ASP-266 AND HIS-292.
RX PubMed=10431819; DOI=10.1016/s0014-5793(99)00813-3;
RA Haruki M., Oohashi Y., Mizuguchi S., Matsuo Y., Morikawa M., Kanaya S.;
RT "Identification of catalytically essential residues in Escherichia coli
RT esterase by site-directed mutagenesis.";
RL FEBS Lett. 454:262-266(1999).
RN [11]
RP FUNCTION, AND INTERACTION WITH MALT.
RX PubMed=11867639; DOI=10.1074/jbc.m200991200;
RA Joly N., Danot O., Schlegel A., Boos W., Richet E.;
RT "The Aes protein directly controls the activity of MalT, the central
RT transcriptional activator of the Escherichia coli maltose regulon.";
RL J. Biol. Chem. 277:16606-16613(2002).
RN [12]
RP FUNCTION, DIMERIZATION, AND INTERACTION WITH MELA.
RX PubMed=12374803; DOI=10.1074/jbc.m207398200;
RA Mandrich L., Caputo E., Martin B.M., Rossi M., Manco G.;
RT "The Aes protein and the monomeric alpha-galactosidase from Escherichia
RT coli form a non-covalent complex. Implications for the regulation of
RT carbohydrate metabolism.";
RL J. Biol. Chem. 277:48241-48247(2002).
CC -!- FUNCTION: Displays esterase activity towards short chain fatty esters
CC (acyl chain length of up to 8 carbons). Able to hydrolyze
CC triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin), but
CC not trioleylglycerol (triolein) or cholesterol oleate. Negatively
CC regulates MalT activity by antagonizing maltotriose binding. Inhibits
CC MelA galactosidase activity. {ECO:0000269|PubMed:11867639,
CC ECO:0000269|PubMed:12374803, ECO:0000269|PubMed:9576853}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 mM for p-nitrophenylacetate (at pH 7.1 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:9576853};
CC KM=0.7 mM for p-nitrophenylpropionate (at pH 7.1 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:9576853};
CC KM=0.5 mM for p-nitrophenylbutyrate (at pH 7.1 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:9576853};
CC KM=0.26 mM for p-nitrophenylvalerate (at pH 7.1 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:9576853};
CC KM=0.22 mM for p-nitrophenylhexanoate (at pH 7.1 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:9576853};
CC KM=0.16 mM for p-nitrophenyloctanoate (at pH 7.1 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:9576853};
CC Vmax=34.2 umol/min/mg enzyme toward p-nitrophenylbutyrate (at pH 5.6
CC and 30 degrees Celsius) {ECO:0000269|PubMed:9576853};
CC Vmax=3.67 umol/min/mg enzyme toward tributyrylglycerol (at pH 5.6 and
CC 30 degrees Celsius) {ECO:0000269|PubMed:9576853};
CC Vmax=0.22 umol/min/mg enzyme toward trioleylglycerol (at pH 5.6 and
CC 30 degrees Celsius) {ECO:0000269|PubMed:9576853};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:9576853};
CC -!- SUBUNIT: Homodimer. Interacts with MalT and MelA.
CC {ECO:0000269|PubMed:11867639, ECO:0000269|PubMed:12374803}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9576853}.
CC -!- MISCELLANEOUS: Not essential for cell growth.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=L35149; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D90259; BAA14305.2; -; Genomic_DNA.
DR EMBL; U82664; AAB40230.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73578.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76255.1; -; Genomic_DNA.
DR EMBL; D00798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L35149; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; C64778; C64778.
DR RefSeq; NP_415009.1; NC_000913.3.
DR RefSeq; WP_000801813.1; NZ_SSZK01000009.1.
DR PDB; 4KRX; X-ray; 1.80 A; A/B/C=1-319.
DR PDB; 4KRY; X-ray; 2.30 A; A/B/C/D/E/F=1-319.
DR PDBsum; 4KRX; -.
DR PDBsum; 4KRY; -.
DR AlphaFoldDB; P23872; -.
DR SMR; P23872; -.
DR BioGRID; 4263164; 4.
DR DIP; DIP-9062N; -.
DR IntAct; P23872; 8.
DR STRING; 511145.b0476; -.
DR ESTHER; ecoli-Aes; Hormone-sensitive_lipase_like.
DR MEROPS; S09.A47; -.
DR MoonProt; P23872; -.
DR jPOST; P23872; -.
DR PaxDb; P23872; -.
DR PRIDE; P23872; -.
DR DNASU; 947514; -.
DR EnsemblBacteria; AAC73578; AAC73578; b0476.
DR EnsemblBacteria; BAE76255; BAE76255; BAE76255.
DR GeneID; 947514; -.
DR KEGG; ecj:JW0465; -.
DR KEGG; eco:b0476; -.
DR PATRIC; fig|1411691.4.peg.1800; -.
DR EchoBASE; EB1093; -.
DR eggNOG; COG0657; Bacteria.
DR HOGENOM; CLU_012494_6_4_6; -.
DR InParanoid; P23872; -.
DR OMA; LWYPSTM; -.
DR PhylomeDB; P23872; -.
DR BioCyc; EcoCyc:EG11101-MON; -.
DR BioCyc; MetaCyc:EG11101-MON; -.
DR BRENDA; 3.1.1.6; 2026.
DR SABIO-RK; P23872; -.
DR PRO; PR:P23872; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; NAS:EcoliWiki.
DR GO; GO:0008126; F:acetylesterase activity; IDA:EcoCyc.
DR GO; GO:0016787; F:hydrolase activity; IDA:EcoliWiki.
DR GO; GO:0034338; F:short-chain carboxylesterase activity; IDA:EcoliWiki.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:EcoCyc.
DR GO; GO:0051346; P:negative regulation of hydrolase activity; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Reference proteome; Serine esterase.
FT CHAIN 1..319
FT /note="Acetyl esterase"
FT /id="PRO_0000071555"
FT MOTIF 91..93
FT /note="Involved in the stabilization of the negatively
FT charged intermediate by the formation of the oxyanion hole"
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 165
FT /evidence="ECO:0000305"
FT ACT_SITE 262
FT /evidence="ECO:0000305"
FT ACT_SITE 292
FT /evidence="ECO:0000305"
FT MUTAGEN 103
FT /note="H->A: Reduces enzymatic efficiency."
FT /evidence="ECO:0000269|PubMed:10431819"
FT MUTAGEN 128
FT /note="E->A: Reduces enzymatic efficiency."
FT /evidence="ECO:0000269|PubMed:10431819"
FT MUTAGEN 163
FT /note="G->A: Diminishes catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:10431819"
FT MUTAGEN 164
FT /note="D->A: Strongly reduces enzymatic activity."
FT /evidence="ECO:0000269|PubMed:10431819"
FT MUTAGEN 165
FT /note="S->A: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:10431819"
FT MUTAGEN 167
FT /note="G->A: Diminishes substrate affinity."
FT /evidence="ECO:0000269|PubMed:10431819"
FT MUTAGEN 262
FT /note="D->A: Strongly reduces enzymatic activity."
FT /evidence="ECO:0000269|PubMed:10431819"
FT MUTAGEN 266
FT /note="D->A: Reduces enzymatic efficiency."
FT /evidence="ECO:0000269|PubMed:10431819"
FT MUTAGEN 292
FT /note="H->A: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:10431819"
FT CONFLICT 18
FT /note="K -> N (in Ref. 8; D00798)"
FT /evidence="ECO:0000305"
FT CONFLICT 275..319
FT /note="LAAHQQPCEFKLYPGTLHAFLHYSRMMKTADEALRDGAQFFTAQL -> VSC
FT ASAAL (in Ref. 2; BAA14305)"
FT /evidence="ECO:0000305"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:4KRX"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:4KRX"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:4KRY"
FT HELIX 37..52
FT /evidence="ECO:0007829|PDB:4KRX"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:4KRX"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:4KRX"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:4KRX"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:4KRX"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:4KRX"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:4KRX"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:4KRX"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:4KRX"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:4KRX"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:4KRX"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:4KRX"
FT HELIX 166..180
FT /evidence="ECO:0007829|PDB:4KRX"
FT STRAND 185..195
FT /evidence="ECO:0007829|PDB:4KRX"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:4KRX"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:4KRX"
FT HELIX 218..228
FT /evidence="ECO:0007829|PDB:4KRX"
FT HELIX 232..236
FT /evidence="ECO:0007829|PDB:4KRX"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:4KRX"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:4KRX"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:4KRY"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:4KRX"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:4KRX"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:4KRX"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:4KRX"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:4KRX"
FT HELIX 302..317
FT /evidence="ECO:0007829|PDB:4KRX"
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
