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ESTE_VIBMI
ID   ESTE_VIBMI              Reviewed;         200 AA.
AC   Q07792;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Arylesterase;
DE            EC=3.1.1.2;
DE   AltName: Full=Aryl-ester hydrolase;
DE   Flags: Precursor;
OS   Vibrio mimicus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=674;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 20-29, AND
RP   MUTAGENESIS.
RC   STRAIN=NTOU 66;
RX   PubMed=8141782; DOI=10.1042/bj2980675;
RA   Shaw J.-F., Chang R.-C., Chuang K.-H., Yen Y.-T., Wang Y.-J., Wang F.-G.;
RT   "Nucleotide sequence of a novel arylesterase gene from Vibro mimicus and
RT   characterization of the enzyme expressed in Escherichia coli.";
RL   Biochem. J. 298:675-680(1994).
CC   -!- FUNCTION: Favors the hydrolysis of several arylesters.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+);
CC         Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310; EC=3.1.1.2;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; X71116; CAA50433.1; -; Genomic_DNA.
DR   PIR; S43387; S32044.
DR   AlphaFoldDB; Q07792; -.
DR   SMR; Q07792; -.
DR   PRIDE; Q07792; -.
DR   GO; GO:0004064; F:arylesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016298; F:lipase activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1110; -; 1.
DR   InterPro; IPR008265; Lipase_GDSL_AS.
DR   InterPro; IPR013830; SGNH_hydro.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   Pfam; PF13472; Lipase_GDSL_2; 1.
DR   PROSITE; PS01098; LIPASE_GDSL_SER; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:8141782"
FT   CHAIN           20..200
FT                   /note="Arylesterase"
FT                   /id="PRO_0000017847"
FT   ACT_SITE        29
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        179
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         29
FT                   /note="S->A,C: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:8141782"
FT   MUTAGEN         31
FT                   /note="S->A: No loss of activity."
FT                   /evidence="ECO:0000269|PubMed:8141782"
SQ   SEQUENCE   200 AA;  22251 MW;  7EC1885B1112D432 CRC64;
     MIRLLSLVLF FCLSAASQAS EKLLVLGDSL SAGYQMPIEK SWPSLLPDAL LEHGQDVTVI
     NGSISGDTTG NGLARLPQLL DQHTPDLVLI ELGANDGLRG FPPKVITSNL SKMISLIKDS
     GANVVMMQIR VPPNYGKRYS DMFYDIYPKL AEHQQVQLMP FFLEHVITKP EWMMDDGLHP
     KPEAQPWIAE FVAQELVKHL
 
 
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