ID   EST1_THEFU              Reviewed;         497 AA.
AC   P86325;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Carboxylesterase {ECO:0000303|Ref.1};
DE            EC=3.1.1.1;
OS   Thermobifida fusca (Thermomonospora fusca).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=2021;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC
RP   ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC   STRAIN=KW3 {ECO:0000269|Ref.1};
RA   Billig S., Oeser T., Birkemeyer C., Zimmermann W.;
RT   "Hydrolysis of cyclic poly(ethylene terephthalate) trimers by a
RT   carboxylesterase from Thermobifida fusca KW3.";
RL   Submitted (JUN-2009) to UniProtKB.
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, ECO:0000269|Ref.1};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.272 mM for p-nitrophenol acetate {ECO:0000269|Ref.1};
CC         KM=0.164 mM for p-nitrophenol butyrate {ECO:0000269|Ref.1};
CC         KM=0.198 mM for p-nitrophenol caprylate {ECO:0000269|Ref.1};
CC         KM=0.468 mM for cyclic PET trimers {ECO:0000269|Ref.1};
CC         Vmax=46 umol/min/mg enzyme with p-nitrophenol acetate as substrate
CC         {ECO:0000269|Ref.1};
CC         Vmax=88 umol/min/mg enzyme with p-nitrophenol butyrate as substrate
CC         {ECO:0000269|Ref.1};
CC         Vmax=64 umol/min/mg enzyme with p-nitrophenol caprylate as substrate
CC         {ECO:0000269|Ref.1};
CC         Vmax=9.3 umol/min/mg enzyme with cyclic PET trimers as substrate
CC         {ECO:0000269|Ref.1};
CC       pH dependence:
CC         Optimum pH is 6 with cyclic PET trimers as substrate (at 60 degrees
CC         Celsius). {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius with cyclic PET trimers as
CC         substrate. {ECO:0000269|Ref.1};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000255}.
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DR   AlphaFoldDB; P86325; -.
DR   SMR; P86325; -.
DR   ESTHER; thefu-1831; Carb_B_Bacteria.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Secreted; Serine esterase.
FT   CHAIN           1..497
FT                   /note="Carboxylesterase"
FT                   /id="PRO_0000379928"
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;  EB2CDDA380FBC1D9 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 PFITSDYVTA HLAKSGLDAD AAKAYTAEGR
     GEEPGDILAS IITDQVFRIP ALRIAESRVD APARTFGYEF AWRTPQLDGI LGACHAVELP
     FVFRTLDRAA SLVGTNPPEE LAETVHNAWV RFATSGDPGW PAWNPETRSV MRFDHPVSEM
     VTDPYPATRA LWDGVPL