EST_GEOSE
ID EST_GEOSE Reviewed; 246 AA.
AC Q06174; Q79M83;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Carboxylesterase;
DE EC=3.1.1.1;
GN Name=est; Synonyms=est30;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12980 / DSM 22 / CCM 2062 / JCM 2501 / NBRC 12550 / NCIMB 8923
RC / NCTC 10339 / R-35646 / VKM B-510;
RX PubMed=1369099; DOI=10.1271/bbb.56.2074;
RA Kugimiya W., Otani Y., Hashimoto Y.;
RT "Molecular cloning and structure of the gene for esterase from a
RT thermophilic bacterium, Bacillus stearothermophilus IFO 12550.";
RL Biosci. Biotechnol. Biochem. 56:2074-2075(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, CATALYTIC
RP ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP AND REACTION MECHANISM.
RC STRAIN=ATCC 29609 / DSM 2027 / NCA 1503 / NCIMB 8924;
RX PubMed=15033540; DOI=10.1016/j.gene.2003.12.029;
RA Ewis H.E., Abdelal A.T., Lu C.D.;
RT "Molecular cloning and characterization of two thermostable carboxyl
RT esterases from Geobacillus stearothermophilus.";
RL Gene 329:187-195(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
RX PubMed=15327954; DOI=10.1016/j.jmb.2004.06.069;
RA Liu P., Wang Y.-F., Ewis H.E., Abdelal A.T., Lu C.-D., Harrison R.W.,
RA Weber I.T.;
RT "Covalent reaction intermediate revealed in crystal structure of the
RT Geobacillus stearothermophilus carboxylesterase Est30.";
RL J. Mol. Biol. 342:551-561(2004).
CC -!- FUNCTION: Involved in the detoxification of xenobiotics. Shows maximal
CC activity with C6 substrates, with gradually decreasing activity from C8
CC to C12 substrates. No activity for higher chain length substrates acids
CC rather than long-chain ones.
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:0000269|PubMed:15033540};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.16 uM for p-nitrophenyl caproate (at 60 degrees Celsius)
CC {ECO:0000269|PubMed:15033540};
CC pH dependence:
CC Optimum pH is 9. {ECO:0000269|PubMed:15033540};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:15033540};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15033540,
CC ECO:0000269|PubMed:15327954}.
CC -!- SIMILARITY: Belongs to the lipase/esterase LIP3/BchO family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN81911.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA02182.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D12681; BAA02182.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY186197; AAN81911.1; ALT_INIT; Genomic_DNA.
DR PIR; JC1374; JC1374.
DR RefSeq; WP_033008930.1; NZ_RCTK01000068.1.
DR PDB; 1R1D; X-ray; 2.00 A; A/B=1-246.
DR PDB; 1TQH; X-ray; 1.63 A; A=1-246.
DR PDBsum; 1R1D; -.
DR PDBsum; 1TQH; -.
DR AlphaFoldDB; Q06174; -.
DR SMR; Q06174; -.
DR DrugBank; DB01670; Propyl acetate.
DR ESTHER; geost-est30; CarbLipBact_1.
DR MEROPS; S09.946; -.
DR GeneID; 58574698; -.
DR BRENDA; 3.1.1.1; 623.
DR SABIO-RK; Q06174; -.
DR EvolutionaryTrace; Q06174; -.
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; IPR012354; Esterase_lipase.
DR InterPro; IPR022742; Hydrolase_4.
DR Pfam; PF12146; Hydrolase_4; 1.
DR PIRSF; PIRSF017388; Esterase_lipase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Serine esterase.
FT CHAIN 1..246
FT /note="Carboxylesterase"
FT /id="PRO_0000008548"
FT ACT_SITE 93
FT /note="Nucleophile"
FT ACT_SITE 192
FT /note="Charge relay system"
FT ACT_SITE 222
FT /note="Charge relay system"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:1TQH"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:1TQH"
FT HELIX 29..40
FT /evidence="ECO:0007829|PDB:1TQH"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:1TQH"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1TQH"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:1TQH"
FT HELIX 65..81
FT /evidence="ECO:0007829|PDB:1TQH"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:1TQH"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:1TQH"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:1TQH"
FT HELIX 123..141
FT /evidence="ECO:0007829|PDB:1TQH"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:1TQH"
FT HELIX 163..175
FT /evidence="ECO:0007829|PDB:1TQH"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:1TQH"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:1TQH"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:1TQH"
FT HELIX 199..206
FT /evidence="ECO:0007829|PDB:1TQH"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:1TQH"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:1TQH"
FT HELIX 230..243
FT /evidence="ECO:0007829|PDB:1TQH"
SQ SEQUENCE 246 AA; 28256 MW; AF99719B68A5709A CRC64;
MKIVPPKPFF FEAGERAVLL LHGFTGNSAD VRMLGRFLES KGYTCHAPIY KGHGVPPEEL
VHTGPDDWWQ DVMNGYEFLK NKGYEKIAVA GLSLGGVFSL KLGYTVPIEG IVTMCAPMYI
KSEETMYEGV LEYAREYKKR EGKSEEQIEQ EMEKFKQTPM KTLKALQELI ADVRDHLDLI
YAPTFVVQAR HDEMINPDSA NIIYNEIESP VKQIKWYEQS GHVITLDQEK DQLHEDIYAF
LESLDW
