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Protein

Acetyl esterase

Gene

aes

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Displays esterase activity towards short chain fatty esters (acyl chain length of up to 8 carbons). Able to hydrolyze triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin), but not trioleylglycerol (triolein) or cholesterol oleate. Negatively regulates MalT activity by antagonizing maltotriose binding. Inhibits MelA galactosidase activity.3 Publications

Kineticsi

  1. KM=1.5 mM for p-nitrophenylacetate (at pH 7.1 and 25 degrees Celsius)1 Publication
  2. KM=0.7 mM for p-nitrophenylpropionate (at pH 7.1 and 25 degrees Celsius)1 Publication
  3. KM=0.5 mM for p-nitrophenylbutyrate (at pH 7.1 and 25 degrees Celsius)1 Publication
  4. KM=0.26 mM for p-nitrophenylvalerate (at pH 7.1 and 25 degrees Celsius)1 Publication
  5. KM=0.22 mM for p-nitrophenylhexanoate (at pH 7.1 and 25 degrees Celsius)1 Publication
  6. KM=0.16 mM for p-nitrophenyloctanoate (at pH 7.1 and 25 degrees Celsius)1 Publication
  1. Vmax=34.2 µmol/min/mg enzyme toward p-nitrophenylbutyrate (at pH 5.6 and 30 degrees Celsius)1 Publication
  2. Vmax=3.67 µmol/min/mg enzyme toward tributyrylglycerol (at pH 5.6 and 30 degrees Celsius)1 Publication
  3. Vmax=0.22 µmol/min/mg enzyme toward trioleylglycerol (at pH 5.6 and 30 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 9.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei165 – 1651Curated
Active sitei262 – 2621Curated
Active sitei292 – 2921Curated

GO - Molecular functioni

  • acetylesterase activity Source: EcoCyc
  • hydrolase activity Source: EcoliWiki
  • short-chain carboxylesterase activity Source: EcoliWiki

GO - Biological processi

  • catabolic process Source: GO_Central
  • negative regulation of hydrolase activity Source: EcoCyc
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BioCyciEcoCyc:EG11101-MONOMER.
ECOL316407:JW0465-MONOMER.
MetaCyc:EG11101-MONOMER.
BRENDAi3.1.1.6. 2026.
SABIO-RKP23872.

Protein family/group databases

ESTHERiecoli-Aes. Hormone-sensitive_lipase_like_1.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl esterase (EC:3.1.1.-)
Alternative name(s):
EcE
Gene namesi
Name:aes
Synonyms:ybaC
Ordered Locus Names:b0476, JW0465
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11101. aes.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi103 – 1031H → A: Reduces enzymatic efficiency. 1 Publication
Mutagenesisi128 – 1281E → A: Reduces enzymatic efficiency. 1 Publication
Mutagenesisi163 – 1631G → A: Diminishes catalytic efficiency. 1 Publication
Mutagenesisi164 – 1641D → A: Strongly reduces enzymatic activity. 1 Publication
Mutagenesisi165 – 1651S → A: Abolishes enzymatic activity. 1 Publication
Mutagenesisi167 – 1671G → A: Diminishes substrate affinity. 1 Publication
Mutagenesisi262 – 2621D → A: Strongly reduces enzymatic activity. 1 Publication
Mutagenesisi266 – 2661D → A: Reduces enzymatic efficiency. 1 Publication
Mutagenesisi292 – 2921H → A: Abolishes enzymatic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 319319Acetyl esterasePRO_0000071555Add
BLAST

Proteomic databases

PaxDbiP23872.

Interactioni

Subunit structurei

Homodimer. Interacts with MalT and MelA.2 Publications

Protein-protein interaction databases

BioGridi4263164. 3 interactions.
DIPiDIP-9062N.
IntActiP23872. 8 interactions.
STRINGi511145.b0476.

Structurei

Secondary structure

1
319
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 124Combined sources
Helixi15 – 217Combined sources
Beta strandi26 – 283Combined sources
Helixi37 – 5216Combined sources
Beta strandi59 – 657Combined sources
Beta strandi72 – 787Combined sources
Beta strandi86 – 905Combined sources
Turni94 – 963Combined sources
Turni100 – 1034Combined sources
Helixi104 – 11411Combined sources
Beta strandi116 – 1216Combined sources
Turni126 – 1283Combined sources
Helixi133 – 14715Combined sources
Helixi149 – 1524Combined sources
Beta strandi157 – 1648Combined sources
Helixi166 – 18015Combined sources
Beta strandi185 – 19511Combined sources
Helixi204 – 2085Combined sources
Turni212 – 2143Combined sources
Helixi218 – 22811Combined sources
Helixi232 – 2365Combined sources
Turni238 – 2403Combined sources
Helixi242 – 2443Combined sources
Beta strandi248 – 2503Combined sources
Beta strandi254 – 2596Combined sources
Helixi265 – 27713Combined sources
Beta strandi282 – 2876Combined sources
Helixi294 – 2974Combined sources
Turni298 – 3003Combined sources
Helixi302 – 31716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4KRXX-ray1.80A/B/C1-319[»]
4KRYX-ray2.30A/B/C/D/E/F1-319[»]
ProteinModelPortaliP23872.
SMRiP23872. Positions 4-319.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi91 – 933Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion holeBy similarity

Sequence similaritiesi

Belongs to the 'GDXG' lipolytic enzyme family.Curated

Phylogenomic databases

eggNOGiENOG4105F2M. Bacteria.
COG0657. LUCA.
HOGENOMiHOG000117644.
InParanoidiP23872.
KOiK01066.
OMAiRMMESAD.
OrthoDBiEOG6SZ1F1.
PhylomeDBiP23872.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_01958. Acetyl_esterase.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR023508. Acetyl_esterase.
IPR002168. Lipase_GDXG_HIS_AS.
IPR033140. Lipase_GDXG_put_SER_AS.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS01173. LIPASE_GDXG_HIS. 1 hit.
PS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23872-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPENKLPVL DLISAEMKTV VNTLQPDLPP WPATGTIAEQ RQYYTLERRF
60 70 80 90 100
WNAGAPEMAT RAYMVPTKYG QVETRLFCPQ PDSPATLFYL HGGGFILGNL
110 120 130 140 150
DTHDRIMRLL ASYSQCTVIG IDYTLSPEAR FPQAIEEIVA ACCYFHQQAE
160 170 180 190 200
DYQINMSRIG FAGDSAGAML ALASALWLRD KQIDCGKVAG VLLWYGLYGL
210 220 230 240 250
RDSVTRRLLG GVWDGLTQQD LQMYEEAYLS NDADRESPYY CLFNNDLTRE
260 270 280 290 300
VPPCFIAGAE FDPLLDDSRL LYQTLAAHQQ PCEFKLYPGT LHAFLHYSRM
310
MKTADEALRD GAQFFTAQL
Length:319
Mass (Da):36,034
Last modified:November 1, 1997 - v3
Checksum:i4F9E234E23CCE7D0
GO

Sequence cautioni

The sequence L35149 differs from that shown. Reason: Frameshift at position 37. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181K → N in D00798 (Ref. 8) Curated
Sequence conflicti275 – 31945LAAHQ…FTAQL → VSCASAAL in BAA14305 (PubMed:2051480).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90259 Genomic DNA. Translation: BAA14305.2.
U82664 Genomic DNA. Translation: AAB40230.1.
U00096 Genomic DNA. Translation: AAC73578.1.
AP009048 Genomic DNA. Translation: BAE76255.1.
D00798 Genomic DNA. No translation available.
L35149 Genomic DNA. No translation available.
PIRiC64778.
RefSeqiNP_415009.1. NC_000913.3.
WP_000801813.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73578; AAC73578; b0476.
BAE76255; BAE76255; BAE76255.
GeneIDi947514.
KEGGiecj:JW0465.
eco:b0476.
PATRICi32116109. VBIEscCol129921_0496.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90259 Genomic DNA. Translation: BAA14305.2.
U82664 Genomic DNA. Translation: AAB40230.1.
U00096 Genomic DNA. Translation: AAC73578.1.
AP009048 Genomic DNA. Translation: BAE76255.1.
D00798 Genomic DNA. No translation available.
L35149 Genomic DNA. No translation available.
PIRiC64778.
RefSeqiNP_415009.1. NC_000913.3.
WP_000801813.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4KRXX-ray1.80A/B/C1-319[»]
4KRYX-ray2.30A/B/C/D/E/F1-319[»]
ProteinModelPortaliP23872.
SMRiP23872. Positions 4-319.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263164. 3 interactions.
DIPiDIP-9062N.
IntActiP23872. 8 interactions.
STRINGi511145.b0476.

Protein family/group databases

ESTHERiecoli-Aes. Hormone-sensitive_lipase_like_1.

Proteomic databases

PaxDbiP23872.

Protocols and materials databases

DNASUi947514.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73578; AAC73578; b0476.
BAE76255; BAE76255; BAE76255.
GeneIDi947514.
KEGGiecj:JW0465.
eco:b0476.
PATRICi32116109. VBIEscCol129921_0496.

Organism-specific databases

EchoBASEiEB1093.
EcoGeneiEG11101. aes.

Phylogenomic databases

eggNOGiENOG4105F2M. Bacteria.
COG0657. LUCA.
HOGENOMiHOG000117644.
InParanoidiP23872.
KOiK01066.
OMAiRMMESAD.
OrthoDBiEOG6SZ1F1.
PhylomeDBiP23872.

Enzyme and pathway databases

BioCyciEcoCyc:EG11101-MONOMER.
ECOL316407:JW0465-MONOMER.
MetaCyc:EG11101-MONOMER.
BRENDAi3.1.1.6. 2026.
SABIO-RKP23872.

Miscellaneous databases

PROiP23872.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_01958. Acetyl_esterase.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR023508. Acetyl_esterase.
IPR002168. Lipase_GDXG_HIS_AS.
IPR033140. Lipase_GDXG_put_SER_AS.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS01173. LIPASE_GDXG_HIS. 1 hit.
PS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the aes gene of Escherichia coli encoding an enzyme with esterase activity."
    Peist R., Koch A., Bolek P., Sewitz S., Kolbus T., Boos W.
    J. Bacteriol. 179:7679-7686(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
  2. "Isolation and characterization of visible light-sensitive mutants of Escherichia coli K12."
    Miyamoto K., Nakahigashi K., Nishimura K., Inokuchi H.
    J. Mol. Biol. 219:393-398(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. Miyamoto K.
    Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  4. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Cloning and characterization of the gsk gene encoding guanosine kinase of Escherichia coli."
    Harlow K.W., Nygaard P., Hove-Jensen B.
    J. Bacteriol. 177:2236-2240(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-103.
    Strain: K12.
  8. Mori H., Iida A., Teshiba S., Fujio T.
    Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
    Strain: K12.
  9. "An esterase from Escherichia coli with a sequence similarity to hormone-sensitive lipase."
    Kanaya S., Koyanagi T., Kanaya E.
    Biochem. J. 332:75-80(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-10, FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
  10. "Identification of catalytically essential residues in Escherichia coli esterase by site-directed mutagenesis."
    Haruki M., Oohashi Y., Mizuguchi S., Matsuo Y., Morikawa M., Kanaya S.
    FEBS Lett. 454:262-266(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-103; GLU-128; GLY-163; ASP-164; SER-165; GLY-167; ASP-262; ASP-266 AND HIS-292.
  11. "The Aes protein directly controls the activity of MalT, the central transcriptional activator of the Escherichia coli maltose regulon."
    Joly N., Danot O., Schlegel A., Boos W., Richet E.
    J. Biol. Chem. 277:16606-16613(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MALT.
  12. "The Aes protein and the monomeric alpha-galactosidase from Escherichia coli form a non-covalent complex. Implications for the regulation of carbohydrate metabolism."
    Mandrich L., Caputo E., Martin B.M., Rossi M., Manco G.
    J. Biol. Chem. 277:48241-48247(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DIMERIZATION, INTERACTION WITH MELA.

Entry informationi

Entry nameiAES_ECOLI
AccessioniPrimary (citable) accession number: P23872
Secondary accession number(s): P77282, Q2MBV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Not essential for cell growth.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.