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Protein

Acetyl esterase

Gene

aes

Organism
Escherichia coli O139:H28 (strain E24377A / ETEC)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

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.UniRule annotation

Sites

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

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BioCyciECOL331111:GH7P-512-MONOMER.

Protein family/group databases

ESTHERiecoli-Aes. Hormone-sensitive_lipase_like_1.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl esteraseUniRule annotation (EC:3.1.1.-UniRule annotation)
Gene namesi
Name:aesUniRule annotation
Ordered Locus Names:EcE24377A_0514
OrganismiEscherichia coli O139:H28 (strain E24377A / ETEC)
Taxonomic identifieri331111 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000001122 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 319319Acetyl esterasePRO_1000188974Add
BLAST

PTM databases

SwissPalmiA7ZIN6.

Interactioni

Subunit structurei

Homodimer. Interacts with MalT and MelA.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA7ZIN6.
SMRiA7ZIN6. 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.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000117644.
KOiK01066.
OMAiPGVTGHQ.
OrthoDBiEOG6SZ1F1.

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.

A7ZIN6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPENKLPVL DLISAEMKTV VNTLQSDLPS WPATGTIAEQ RQYYTLERRF
60 70 80 90 100
WNAGAPEMAT RAYMVPTKYG QVETRLFCPQ PDSPATLFYL HGGGFILGNL
110 120 130 140 150
DTHDRIMRLL ASYSQCTVIG IDYPLSPEAR FPQAIEEIVA ACCYFHQQAE
160 170 180 190 200
DYQINMSRIG FAGDSAGAML TLASALWLRD KQIDCGKIAG 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):36,054
Last modified:October 23, 2007 - v1
Checksum:iC1C09FE2674CF064
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000800 Genomic DNA. Translation: ABV20987.1.
RefSeqiWP_000801847.1. NC_009801.1.

Genome annotation databases

EnsemblBacteriaiABV20987; ABV20987; EcE24377A_0514.
KEGGiecw:EcE24377A_0514.
PATRICi18290284. VBIEscCol31211_0822.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000800 Genomic DNA. Translation: ABV20987.1.
RefSeqiWP_000801847.1. NC_009801.1.

3D structure databases

ProteinModelPortaliA7ZIN6.
SMRiA7ZIN6. Positions 4-319.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERiecoli-Aes. Hormone-sensitive_lipase_like_1.

PTM databases

SwissPalmiA7ZIN6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABV20987; ABV20987; EcE24377A_0514.
KEGGiecw:EcE24377A_0514.
PATRICi18290284. VBIEscCol31211_0822.

Phylogenomic databases

HOGENOMiHOG000117644.
KOiK01066.
OMAiPGVTGHQ.
OrthoDBiEOG6SZ1F1.

Enzyme and pathway databases

BioCyciECOL331111:GH7P-512-MONOMER.

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

  1. "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
    Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
    J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: E24377A / ETEC.

Entry informationi

Entry nameiAES_ECO24
AccessioniPrimary (citable) accession number: A7ZIN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: October 23, 2007
Last modified: March 16, 2016
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. 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.