ID   EST1_THEFY              Reviewed;         497 AA.
AC   Q47M62;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Carboxylesterase {ECO:0000250|UniProtKB:P86325, ECO:0000312|EMBL:AAZ56460.1};
DE            EC=3.1.1.1;
GN   OrderedLocusNames=Tfu_2427;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/jb.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA   Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA   Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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:0000250|UniProtKB:P86325, ECO:0000255|PROSITE-
CC         ProRule:PRU10039};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P86325}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000255}.
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DR   EMBL; CP000088; AAZ56460.1; -; Genomic_DNA.
DR   RefSeq; WP_011292850.1; NC_007333.1.
DR   AlphaFoldDB; Q47M62; -.
DR   SMR; Q47M62; -.
DR   STRING; 269800.Tfu_2427; -.
DR   ESTHER; thefu-1831; Carb_B_Bacteria.
DR   EnsemblBacteria; AAZ56460; AAZ56460; Tfu_2427.
DR   KEGG; tfu:Tfu_2427; -.
DR   eggNOG; COG2272; Bacteria.
DR   HOGENOM; CLU_006586_16_0_11; -.
DR   OMA; VYEFAWP; -.
DR   OrthoDB; 489066at2; -.
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   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Secreted; Serine esterase.
FT   CHAIN           1..497
FT                   /note="Carboxylesterase"
FT                   /id="PRO_0000379929"
FT   ACT_SITE        185
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P21836,
FT                   ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        319
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P21836"
FT   ACT_SITE        415
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P37967"
SQ   SEQUENCE   497 AA;  52941 MW;  CCA6E4F6AEF09793 CRC64;
     MEIVIRTGSG DVRGSKENGI AVFRGIPYAE PPVGAHRFTA PRPPRPWDGV RDATEFSATA
     PRPPYPEAIG ALLIERFIPG DDYLTLNVWT PDPNAVGLPV MVWIHGGAFT NGSGSEPVYD
     GAAFARDGVV FVSFNYRLGI IGFADLPDAP SNRGLLDQIA ALEWVRDNIA RFGGDPGNVT
     VFGESAGAMS VCTLMATPRA RGLFRRAILQ SGAGNMAVAA EDATTIAAVI AHRLGVEPTA
     AALAHVPVAQ LLDVQQQVAQ EIQGAPDPAV WGERIAGGSV LLPFAPVIDG ELLSQRPAEA
     IAGGAGHDVD LLFGTTTDEY RLFLAPTGLL PFITGDYVTT HLAKSGLDAD AAKAYTAEGR
     GEEPGDILAS IITDQVFRIP ALRIAESRVD APARTFGYEF AWRTPQLDGI LGACHAVELP
     FVFRTLDRAA SLVGTNPPEE LAETVHNAWV RFATSGDPGW PAWNPETRSV MRFDHPVSEM
     VTDPYPATRA LWDGVPL