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Protein

Acetyl esterase

Gene

aes

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei165UniRule annotation1
Active sitei262UniRule annotation1
Active sitei292UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Serine esterase

Enzyme and pathway databases

BioCyciSENT99287:G1FZD-495-MONOMER

Protein family/group databases

ESTHERisalty-AES Hormone-sensitive_lipase_like
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002397111 – 323Acetyl esteraseAdd BLAST323

Proteomic databases

PaxDbiQ8ZRA1
PRIDEiQ8ZRA1

Interactioni

Subunit structurei

Homodimer. Interacts with MalT and MelA.UniRule annotation

Protein-protein interaction databases

STRINGi99287.STM0490

Structurei

Secondary structure

1323
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 12Combined sources3
Helixi15 – 23Combined sources9
Helixi37 – 51Combined sources15
Turni52 – 54Combined sources3
Beta strandi59 – 65Combined sources7
Beta strandi72 – 82Combined sources11
Beta strandi86 – 90Combined sources5
Turni94 – 96Combined sources3
Turni100 – 103Combined sources4
Helixi104 – 114Combined sources11
Beta strandi116 – 121Combined sources6
Turni126 – 128Combined sources3
Helixi133 – 147Combined sources15
Turni148 – 153Combined sources6
Beta strandi157 – 164Combined sources8
Helixi166 – 181Combined sources16
Beta strandi185 – 195Combined sources11
Helixi204 – 208Combined sources5
Turni212 – 214Combined sources3
Helixi218 – 228Combined sources11
Helixi232 – 236Combined sources5
Turni238 – 240Combined sources3
Helixi242 – 244Combined sources3
Beta strandi254 – 259Combined sources6
Helixi265 – 277Combined sources13
Beta strandi282 – 287Combined sources6
Helixi294 – 297Combined sources4
Turni298 – 300Combined sources3
Helixi302 – 320Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GA7X-ray1.55A1-323[»]
ProteinModelPortaliQ8ZRA1
SMRiQ8ZRA1
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8ZRA1

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

eggNOGiENOG4105F2M Bacteria
COG0657 LUCA
HOGENOMiHOG000117644
KOiK01066
OMAiGIIGMNS
PhylomeDBiQ8ZRA1

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
HAMAPiMF_01958 Acetyl_esterase, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR013094 AB_hydrolase_3
IPR023508 Acetyl_esterase
IPR033140 Lipase_GDXG_put_SER_AS
PfamiView protein in Pfam
PF07859 Abhydrolase_3, 1 hit
SUPFAMiSSF53474 SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS01174 LIPASE_GDXG_SER, 1 hit

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_003197.2
WP_000801786.1, NC_003197.2

Genome annotation databases

EnsemblBacteriaiAAL19444; AAL19444; STM0490
GeneIDi1252010
KEGGistm:STM0490
PATRICifig|99287.12.peg.524

Similar proteinsi

Entry informationi

Entry nameiAES_SALTY
AccessioniPrimary (citable) accession number: Q8ZRA1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: March 1, 2002
Last modified: May 23, 2018
This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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