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Protein

Acetyl esterase

Gene

aes

Organism
Escherichia coli O45:K1 (strain S88 / ExPEC)
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)DescriptionActionsGraphical viewLength
Active sitei165UniRule annotation1
Active sitei262UniRule annotation1
Active sitei292UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

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:ECS88_0473
OrganismiEscherichia coli O45:K1 (strain S88 / ExPEC)
Taxonomic identifieri585035 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000747 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001889761 – 319Acetyl esteraseAdd BLAST319

Interactioni

Subunit structurei

Homodimer. Interacts with MalT and MelA.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB7MDZ8.
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.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000117644.
KOiK01066.
OMAiPGVTGHQ.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_01958. Acetyl_esterase. 1 hit.
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.

B7MDZ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPENKLPVL DLISAEMKTV VNTLQPDLPP WPATGAIAEQ RQYYTLERRF
60 70 80 90 100
WNVGAPEMAT RAYRVPTKYG QVKTRLFYPQ 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 FDPLLDDSCL LYQTLAAHQQ PCEFKLYSGM LHAFLHYSRM
310
MKTADEALRD GAQFFTAQL
Length:319
Mass (Da):36,083
Last modified:February 10, 2009 - v1
Checksum:i6FBEAA2C3AF6C48F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928161 Genomic DNA. Translation: CAR01820.1.

Genome annotation databases

EnsemblBacteriaiCAR01820; CAR01820; ECS88_0473.
KEGGiecz:ECS88_0473.
PATRICi18408624. VBIEscCol91599_0474.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928161 Genomic DNA. Translation: CAR01820.1.

3D structure databases

ProteinModelPortaliB7MDZ8.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERiecoli-Aes. Hormone-sensitive_lipase_like_1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAR01820; CAR01820; ECS88_0473.
KEGGiecz:ECS88_0473.
PATRICi18408624. VBIEscCol91599_0474.

Phylogenomic databases

HOGENOMiHOG000117644.
KOiK01066.
OMAiPGVTGHQ.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
HAMAPiMF_01958. Acetyl_esterase. 1 hit.
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...

Entry informationi

Entry nameiAES_ECO45
AccessioniPrimary (citable) accession number: B7MDZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: November 2, 2016
This is version 54 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.