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Q83M39 (AES_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetyl esterase

EC=3.1.1.-
Gene names
Name:aes
Ordered Locus Names:SF0421, S0428
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length319 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_01958

Subunit structure

Homodimer. Interacts with MalT and MelA By similarity. HAMAP-Rule MF_01958

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01958.

Sequence similarities

Belongs to the 'GDXG' lipolytic enzyme family.

Sequence caution

The sequence AAN42076.1 differs from that shown. Reason: Erroneous termination at position 273. Translated as Gln.

The sequence AAP15953.1 differs from that shown. Reason: Erroneous termination at position 273. Translated as Gln.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
Serine esterase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncarboxylic ester hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 319319Acetyl esterase HAMAP-Rule MF_01958
PRO_0000239713

Regions

Motif91 – 933Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole By similarity

Sites

Active site1651 By similarity
Active site2621 By similarity
Active site2921 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q83M39 [UniParc].

Last modified June 13, 2006. Version 2.
Checksum: A61E91C47CEB35D6

FASTA31936,037
        10         20         30         40         50         60 
MKPENKLPVL DLISAEMKTV VNTLQPDLPS WPATGTIAEQ RQYYTLERRF WNAGAPEMAT 

        70         80         90        100        110        120 
RAYMVPTKYG QVETRLFCPQ PDSPATLFYL HGGGFILGNL DTHDRIMRLL ASYSQCTVIG 

       130        140        150        160        170        180 
INYTLSPEAR FPQAIEEIVA ACCYFHQQAE DYQINMSRIG FAGDSAGAML ALASALWLRD 

       190        200        210        220        230        240 
KQIDCGKIAG VLLWYGLYGL RDSVTRRLLG GVWDGLTQQD LQMYEEAYLS NDADRESPYY 

       250        260        270        280        290        300 
CLFNNDLTRE VPPCFIAGAE FDPLLDDSRL LYQTLAAHQQ PCEFKLYPGT LHAFLHYSRM 

       310 
MKTADEALRD GAQFFTAQL 

« Hide

References

[1]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005674 Genomic DNA. Translation: AAN42076.1. Sequence problems.
AE014073 Genomic DNA. Translation: AAP15953.1. Sequence problems.
RefSeqNP_706369.1. NC_004337.2.
NP_836147.1. NC_004741.1.

3D structure databases

ProteinModelPortalQ83M39.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198214.SF0421.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN42076; AAN42076; SF0421.
AAP15953; AAP15953; S0428.
GeneID1027722.
1076865.
KEGGsfl:SF0421.
sfx:S0428.
PATRIC18701879. VBIShiFle31049_0472.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0657.
HOGENOMHOG000117644.
KOK01066.
OrthoDBEOG6SZ1F1.

Family and domain databases

HAMAPMF_01958. Acetyl_esterase.
InterProIPR013094. AB_hydrolase_3.
IPR023508. Acetyl_esterase.
IPR002168. Lipase_GDXG_AS.
[Graphical view]
PfamPF07859. Abhydrolase_3. 1 hit.
[Graphical view]
PROSITEPS01173. LIPASE_GDXG_HIS. 1 hit.
PS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAES_SHIFL
AccessionPrimary (citable) accession number: Q83M39
Secondary accession number(s): Q7C2W8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: June 13, 2006
Last modified: February 19, 2014
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families