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Protein

Acetyl esterase

Gene

aes

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

Miscellaneous

Not essential for cell growth.

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)DescriptionActionsGraphical viewLength
Active sitei165Curated1
Active sitei262Curated1
Active sitei292Curated1

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 DNA binding transcription factor activity Source: EcoCyc
  • negative regulation of hydrolase activity Source: EcoCyc

Keywordsi

Molecular functionHydrolase, Serine esterase

Enzyme and pathway databases

BioCyciEcoCyc:EG11101-MONOMER
MetaCyc:EG11101-MONOMER
BRENDAi3.1.1.6 2026
SABIO-RKiP23872

Protein family/group databases

ESTHERiecoli-Aes Hormone-sensitive_lipase_like
MoonProtiP23872

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11101 aes

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi103H → A: Reduces enzymatic efficiency. 1 Publication1
Mutagenesisi128E → A: Reduces enzymatic efficiency. 1 Publication1
Mutagenesisi163G → A: Diminishes catalytic efficiency. 1 Publication1
Mutagenesisi164D → A: Strongly reduces enzymatic activity. 1 Publication1
Mutagenesisi165S → A: Abolishes enzymatic activity. 1 Publication1
Mutagenesisi167G → A: Diminishes substrate affinity. 1 Publication1
Mutagenesisi262D → A: Strongly reduces enzymatic activity. 1 Publication1
Mutagenesisi266D → A: Reduces enzymatic efficiency. 1 Publication1
Mutagenesisi292H → A: Abolishes enzymatic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000715551 – 319Acetyl esteraseAdd BLAST319

Proteomic databases

PaxDbiP23872
PRIDEiP23872

Interactioni

Subunit structurei

Homodimer. Interacts with MalT and MelA.2 Publications

Protein-protein interaction databases

BioGridi42631644 interactors.
DIPiDIP-9062N
IntActiP23872 8 interactors.
STRINGi316385.ECDH10B_0432

Structurei

Secondary structure

1319
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 12Combined sources4
Helixi15 – 21Combined sources7
Beta strandi26 – 28Combined sources3
Helixi37 – 52Combined sources16
Beta strandi59 – 65Combined sources7
Beta strandi72 – 78Combined sources7
Beta strandi86 – 90Combined sources5
Turni94 – 96Combined sources3
Turni100 – 103Combined sources4
Helixi104 – 114Combined sources11
Beta strandi116 – 121Combined sources6
Turni126 – 128Combined sources3
Helixi133 – 147Combined sources15
Helixi149 – 152Combined sources4
Beta strandi157 – 164Combined sources8
Helixi166 – 180Combined sources15
Beta strandi185 – 195Combined sources11
Helixi204 – 208Combined sources5
Turni212 – 214Combined sources3
Helixi218 – 228Combined sources11
Helixi232 – 236Combined sources5
Turni238 – 240Combined sources3
Helixi242 – 244Combined sources3
Beta strandi248 – 250Combined sources3
Beta strandi254 – 259Combined sources6
Helixi265 – 277Combined sources13
Beta strandi282 – 287Combined sources6
Helixi294 – 297Combined sources4
Turni298 – 300Combined sources3
Helixi302 – 317Combined sources16

3D structure databases

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

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi91 – 93Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion holeBy similarity3

Sequence similaritiesi

Belongs to the 'GDXG' lipolytic enzyme family.Curated

Phylogenomic databases

eggNOGiENOG4105F2M Bacteria
COG0657 LUCA
HOGENOMiHOG000117644
InParanoidiP23872
KOiK01066
OMAiGIIGMNS
PhylomeDBiP23872

Family and domain databases

Gene3Di3.40.50.18201 hit
HAMAPiMF_01958 Acetyl_esterase, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR013094 AB_hydrolase_3
IPR023508 Acetyl_esterase
IPR002168 Lipase_GDXG_HIS_AS
IPR033140 Lipase_GDXG_put_SER_AS
PfamiView protein in Pfam
PF07859 Abhydrolase_3, 1 hit
SUPFAMiSSF53474 SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS01173 LIPASE_GDXG_HIS, 1 hit
PS01174 LIPASE_GDXG_SER, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti18K → N in D00798 (Ref. 8) Curated1
Sequence conflicti275 – 319LAAHQ…FTAQL → VSCASAAL in BAA14305 (PubMed:2051480).CuratedAdd BLAST45

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
PATRICifig|1411691.4.peg.1800

Similar proteinsi

Entry informationi

Entry nameiAES_ECOLI
AccessioniPrimary (citable) accession number: P23872
Secondary accession number(s): P77282, Q2MBV1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1997
Last modified: April 25, 2018
This is version 142 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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