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Q83M39

- AES_SHIFL

UniProt

Q83M39 - AES_SHIFL

Protein

Acetyl esterase

Gene

aes

Organism
Shigella flexneri
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 2 (13 Jun 2006)
      Previous versions | rss
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    • Comment

    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

    1. carboxylic ester hydrolase activity Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl esteraseUniRule annotation (EC:3.1.1.-UniRule annotation)
    Gene namesi
    Name:aesUniRule annotation
    Ordered Locus Names:SF0421, S0428
    OrganismiShigella flexneri
    Taxonomic identifieri623 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
    ProteomesiUP000001006: Chromosome, UP000002673: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 319319Acetyl esterasePRO_0000239713Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer. Interacts with MalT and MelA.UniRule annotation

    Protein-protein interaction databases

    STRINGi198214.SF0421.

    Structurei

    3D structure databases

    ProteinModelPortaliQ83M39.
    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

    eggNOGiCOG0657.
    HOGENOMiHOG000117644.
    KOiK01066.
    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_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.

    Q83M39-1 [UniParc]FASTAAdd to Basket

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    MKPENKLPVL DLISAEMKTV VNTLQPDLPS WPATGTIAEQ RQYYTLERRF    50
    WNAGAPEMAT RAYMVPTKYG QVETRLFCPQ PDSPATLFYL HGGGFILGNL 100
    DTHDRIMRLL ASYSQCTVIG INYTLSPEAR FPQAIEEIVA ACCYFHQQAE 150
    DYQINMSRIG FAGDSAGAML ALASALWLRD KQIDCGKIAG VLLWYGLYGL 200
    RDSVTRRLLG GVWDGLTQQD LQMYEEAYLS NDADRESPYY CLFNNDLTRE 250
    VPPCFIAGAE FDPLLDDSRL LYQTLAAHQQ PCEFKLYPGT LHAFLHYSRM 300
    MKTADEALRD GAQFFTAQL 319
    Length:319
    Mass (Da):36,037
    Last modified:June 13, 2006 - v2
    Checksum:iA61E91C47CEB35D6
    GO

    Sequence cautioni

    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.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005674 Genomic DNA. Translation: AAN42076.1. Sequence problems.
    AE014073 Genomic DNA. Translation: AAP15953.1. Sequence problems.
    RefSeqiNP_706369.1. NC_004337.2.
    NP_836147.1. NC_004741.1.

    Genome annotation databases

    EnsemblBacteriaiAAN42076; AAN42076; SF0421.
    AAP15953; AAP15953; S0428.
    GeneIDi1027722.
    1076865.
    KEGGisfl:SF0421.
    sfx:S0428.
    PATRICi18701879. VBIShiFle31049_0472.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005674 Genomic DNA. Translation: AAN42076.1 . Sequence problems.
    AE014073 Genomic DNA. Translation: AAP15953.1 . Sequence problems.
    RefSeqi NP_706369.1. NC_004337.2.
    NP_836147.1. NC_004741.1.

    3D structure databases

    ProteinModelPortali Q83M39.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 198214.SF0421.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN42076 ; AAN42076 ; SF0421 .
    AAP15953 ; AAP15953 ; S0428 .
    GeneIDi 1027722.
    1076865.
    KEGGi sfl:SF0421.
    sfx:S0428.
    PATRICi 18701879. VBIShiFle31049_0472.

    Phylogenomic databases

    eggNOGi COG0657.
    HOGENOMi HOG000117644.
    KOi K01066.
    OrthoDBi EOG6SZ1F1.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    HAMAPi MF_01958. Acetyl_esterase.
    InterProi IPR029058. AB_hydrolase.
    IPR013094. AB_hydrolase_3.
    IPR023508. Acetyl_esterase.
    IPR002168. Lipase_GDXG_AS.
    [Graphical view ]
    Pfami PF07859. Abhydrolase_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS01173. LIPASE_GDXG_HIS. 1 hit.
    PS01174. LIPASE_GDXG_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700930 / 2457T / Serotype 2a.

    Entry informationi

    Entry nameiAES_SHIFL
    AccessioniPrimary (citable) accession number: Q83M39
    Secondary accession number(s): Q7C2W8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2006
    Last sequence update: June 13, 2006
    Last modified: October 1, 2014
    This is version 70 of the entry and version 2 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

    External Data

    Dasty 3