EST5B_DROPE
ID EST5B_DROPE Reviewed; 545 AA.
AC O16172;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Esterase-5B;
DE Short=Est-5B;
DE EC=3.1.1.1;
DE AltName: Full=Carboxylic-ester hydrolase 5B;
DE Short=Carboxylesterase-5B;
DE Flags: Precursor;
GN Name=Est-5B; Synonyms=Est5B;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9475741; DOI=10.1093/genetics/148.1.305;
RA King L.M.;
RT "The role of gene conversion in determining sequence variation and
RT divergence in the Est-5 gene family in Drosophila pseudoobscura.";
RL Genetics 148:305-315(1998).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10039};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P25726}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; AF016110; AAB70223.1; -; Genomic_DNA.
DR AlphaFoldDB; O16172; -.
DR SMR; O16172; -.
DR STRING; 7234.FBpp0189269; -.
DR ESTHER; drope-est5b; Carb_B_Arthropoda.
DR MEROPS; S09.947; -.
DR eggNOG; KOG1516; Eukaryota.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Hydrolase; Secreted; Serine esterase; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..545
FT /note="Esterase-5B"
FT /id="PRO_0000008556"
FT ACT_SITE 207
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 467
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 84..103
FT /evidence="ECO:0000250"
FT DISULFID 259..271
FT /evidence="ECO:0000250"
FT DISULFID 515..536
FT /evidence="ECO:0000255"
SQ SEQUENCE 545 AA; 60729 MW; 6705B7FAE68F222E CRC64;
MYCAKLILLL GCFWISSSAS DPADPLLVDL PNGKLRGRDN GNYYSYESLP YAEPPVGDLR
FEAPQPYKQQ WTDTFDATQP PVSCMQWDQF IRGDDKLAGN EDCLTVSVYR PKNSSRNSFP
VVAQIHGGAF MFGGASQNGH ENFMREGNLI LVKISYRLGP LGFVSTGDAD LSGNFGLKDQ
RLALLWIKQN IASFGGEPEN ILVIGHSAGG GSVHLQVLRE DFSKVAKAAI SFSGNALDPW
VVQQGGRGRA FELGRIVGCG QASDSVTLKK CLKSKPASEI VSAVRNFLVF AYVPFTPFGP
VVESPDAPEA FISQHPVDII KSGKFAQVPW AVTYTTEDGG YNAALLLEEQ ASSGREWIVD
LNDRWFDWAP YLLFYRDSMT TIKDMDDYSR KLRQEYLGDR RFSVESYWDL QRLFTDVLFK
NSTEISLDLH RKHGKSPVYA FVYDNPANTG IGQGLAQRTD INFGTVHGDD YFLIFENIVR
EPQLRSDEET ISRNFLKMLN DFVLSENGTL AFGTCVFQDN VGSSKLQLLS ITRNGCENLE
LESFP
