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Protein

Acetyl esterase

Gene

aes

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 2 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.UniRule annotation

Sites

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BioCyciSENT99287:GCTI-493-MONOMER.

Protein family/group databases

ESTHERisalty-AES. Hormone-sensitive_lipase_like_1.
MEROPSiS09.A47.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl esteraseUniRule annotation (EC:3.1.1.-UniRule annotation)
Gene namesi
Name:aesUniRule annotation
Ordered Locus Names:STM0490
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 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 – 323323Acetyl esterasePRO_0000239711Add
BLAST

Proteomic databases

PaxDbiQ8ZRA1.

Interactioni

Subunit structurei

Homodimer. Interacts with MalT and MelA.UniRule annotation

Protein-protein interaction databases

STRINGi99287.STM0490.

Structurei

Secondary structure

1
323
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 123Combined sources
Helixi15 – 239Combined sources
Helixi37 – 5115Combined sources
Turni52 – 543Combined sources
Beta strandi59 – 657Combined sources
Beta strandi72 – 8211Combined sources
Beta strandi86 – 905Combined sources
Turni94 – 963Combined sources
Turni100 – 1034Combined sources
Helixi104 – 11411Combined sources
Beta strandi116 – 1216Combined sources
Turni126 – 1283Combined sources
Helixi133 – 14715Combined sources
Turni148 – 1536Combined sources
Beta strandi157 – 1648Combined sources
Helixi166 – 18116Combined sources
Beta strandi185 – 19511Combined sources
Helixi204 – 2085Combined sources
Turni212 – 2143Combined sources
Helixi218 – 22811Combined sources
Helixi232 – 2365Combined sources
Turni238 – 2403Combined sources
Helixi242 – 2443Combined sources
Beta strandi254 – 2596Combined sources
Helixi265 – 27713Combined sources
Beta strandi282 – 2876Combined sources
Helixi294 – 2974Combined sources
Turni298 – 3003Combined sources
Helixi302 – 32019Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GA7X-ray1.55A1-323[»]
ProteinModelPortaliQ8ZRA1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8ZRA1.

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

eggNOGiENOG4105F2M. Bacteria.
COG0657. LUCA.
HOGENOMiHOG000117644.
KOiK01066.
OMAiRMMESAD.
PhylomeDBiQ8ZRA1.

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.
IPR033140. Lipase_GDXG_put_SER_AS.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8ZRA1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPENKIPVL TRLSDEMTAV VNFQQPGLPP WPADGDIETQ RQYYLLERRF
60 70 80 90 100
WNADAPSMTT RTCAVPTPYG DVTTRLYSPQ PTSQATLYYL HGGGFILGNL
110 120 130 140 150
DTHDRIMRLL ARYTGCTVIG IDYSLSPQAR YPQAIEETVA VCSYFSQHAD
160 170 180 190 200
EYSLNVEKIG FAGDSAGAML ALASALWLRD KHIRCGNVIA ILLWYGLYGL
210 220 230 240 250
QDSVSRRLFG GAWDGLTRED LDMYEKAYLR NDEDRESPWY CLFNNDLTRD
260 270 280 290 300
VPPCFIASAE FDPLIDDSRL LHQTLQAHQQ PCEYKMYPGT LHAFLHYSRM
310 320
MTIADDALQD GARFFMARMK TPR
Length:323
Mass (Da):36,799
Last modified:March 1, 2002 - v1
Checksum:i91A9A4EF1CCA1A45
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL19444.1.
RefSeqiNP_459485.1. NC_003197.1.
WP_000801786.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL19444; AAL19444; STM0490.
GeneIDi1252010.
KEGGistm:STM0490.
PATRICi32379325. VBISalEnt20916_0524.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL19444.1.
RefSeqiNP_459485.1. NC_003197.1.
WP_000801786.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GA7X-ray1.55A1-323[»]
ProteinModelPortaliQ8ZRA1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM0490.

Protein family/group databases

ESTHERisalty-AES. Hormone-sensitive_lipase_like_1.
MEROPSiS09.A47.

Proteomic databases

PaxDbiQ8ZRA1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL19444; AAL19444; STM0490.
GeneIDi1252010.
KEGGistm:STM0490.
PATRICi32379325. VBISalEnt20916_0524.

Phylogenomic databases

eggNOGiENOG4105F2M. Bacteria.
COG0657. LUCA.
HOGENOMiHOG000117644.
KOiK01066.
OMAiRMMESAD.
PhylomeDBiQ8ZRA1.

Enzyme and pathway databases

BioCyciSENT99287:GCTI-493-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ8ZRA1.

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.
IPR033140. Lipase_GDXG_put_SER_AS.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAES_SALTY
AccessioniPrimary (citable) accession number: Q8ZRA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: March 1, 2002
Last modified: September 7, 2016
This is version 83 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.