ESTD_THEMA
ID ESTD_THEMA Reviewed; 412 AA.
AC Q9WYH1; G4FHP9;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Esterase EstD {ECO:0000312|EMBL:AHD17901.1};
DE EC=3.1.1.1 {ECO:0000269|PubMed:17466017};
DE Flags: Precursor;
GN Name=estD {ECO:0000303|PubMed:17466017};
GN OrderedLocusNames=TM_0336 {ECO:0000312|EMBL:AAD35423.1};
GN ORFNames=THEMA_03040 {ECO:0000312|EMBL:AHD17901.1},
GN Tmari_0334 {ECO:0000312|EMBL:AGL49259.1};
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485;
RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H.,
RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y.,
RA Zengler K.;
RT "The genome organization of Thermotoga maritima reflects its lifestyle.";
RL PLoS Genet. 9:E1003485-E1003485(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RG DOE Joint Genome Institute;
RA Noll K.M., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, SUBUNIT, 3D-STRUCTURE MODELING,
RP MUTAGENESIS OF SER-243; ASP-347 AND HIS-378, ACTIVE SITE, AND
RP BIOTECHNOLOGY.
RX PubMed=17466017; DOI=10.1111/j.1742-4658.2007.05817.x;
RA Levisson M., van der Oost J., Kengen S.W.;
RT "Characterization and structural modeling of a new type of thermostable
RT esterase from Thermotoga maritima.";
RL FEBS J. 274:2832-2842(2007).
CC -!- FUNCTION: Exhibits significant esterase activity with a preference for
CC short acyl chain esters (C4-C8) in vitro. Its physiological function is
CC not known. Displays neither proteolytic activity using casein as
CC substrate, nor peptidase activity when assayed with L-leucine p-
CC nitroanilide and L-proline p-nitroanilide.
CC {ECO:0000269|PubMed:17466017}.
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:17466017};
CC -!- ACTIVITY REGULATION: Is strongly inhibited by phenylmethylsulfonyl
CC fluoride, a serine protease inhibitor, and by mercury chloride. Diethyl
CC pyrocarbonate, a histidine modifier, also inhibits the reaction, albeit
CC less pronounced than phenylmethylsulfonyl fluoride. EDTA and
CC dithiothreitol have no effect on enzyme activity.
CC {ECO:0000269|PubMed:17466017}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=148 uM for pNP-acetate (at pH 7 and 70 degrees Celsius)
CC {ECO:0000269|PubMed:17466017};
CC KM=227 uM for pNP-butyrate (at pH 7 and 70 degrees Celsius)
CC {ECO:0000269|PubMed:17466017};
CC KM=66 uM for pNP-valerate (at pH 7 and 70 degrees Celsius)
CC {ECO:0000269|PubMed:17466017};
CC KM=11 uM for pNP-octanoate (at pH 7 and 70 degrees Celsius)
CC {ECO:0000269|PubMed:17466017};
CC KM=72 uM for pNP-decanoate (at pH 7 and 70 degrees Celsius)
CC {ECO:0000269|PubMed:17466017};
CC Note=kcat is 1.0 sec(-1) with pNP-acetate as substrate. kcat is 14.9
CC sec(-1) with pNP-butyrate as substrate. kcat is 10.2 sec(-1) with
CC pNP-valerate as substrate. kcat is 1.6 sec(-1) with pNP-octanoate as
CC substrate. kcat is 1.3 sec(-1) with pNP-decanoate as substrate (at pH
CC 7 and 70 degrees Celsius). {ECO:0000269|PubMed:17466017};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:17466017};
CC Temperature dependence:
CC Optimum temperature is around 95 degrees Celsius. Shows >70% of its
CC maximal activity in the pH range of 5-9. Displays a relatively high
CC thermostability with a half-life of 1 hour at 100 degrees Celsius.
CC {ECO:0000269|PubMed:17466017};
CC -!- SUBUNIT: Exists mainly as a monomer and, to some extent as a dimer.
CC {ECO:0000269|PubMed:17466017}.
CC -!- BIOTECHNOLOGY: The high thermal stability and activity in the presence
CC of organic solvents makes EstD an attractive catalyst for future
CC applications in industry. {ECO:0000305|PubMed:17466017}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Esterase 10
CC family. {ECO:0000305|PubMed:17466017}.
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DR EMBL; AE000512; AAD35423.1; -; Genomic_DNA.
DR EMBL; CP004077; AGL49259.1; -; Genomic_DNA.
DR EMBL; CP007013; AHD17901.1; -; Genomic_DNA.
DR PIR; B72391; B72391.
DR RefSeq; NP_228147.1; NC_000853.1.
DR RefSeq; WP_004083104.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9WYH1; -.
DR STRING; 243274.THEMA_03040; -.
DR ESTHER; thema-TM0336; Bacterial_EstLip_FamX.
DR EnsemblBacteria; AAD35423; AAD35423; TM_0336.
DR EnsemblBacteria; AGL49259; AGL49259; Tmari_0334.
DR KEGG; tma:TM0336; -.
DR KEGG; tmi:THEMA_03040; -.
DR KEGG; tmm:Tmari_0334; -.
DR KEGG; tmw:THMA_0344; -.
DR PATRIC; fig|243274.17.peg.333; -.
DR eggNOG; COG1073; Bacteria.
DR InParanoid; Q9WYH1; -.
DR OMA; NWWTQSG; -.
DR OrthoDB; 721431at2; -.
DR Proteomes; UP000008183; Chromosome.
DR Proteomes; UP000013901; Chromosome.
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; IPR024981; DUF3887.
DR InterPro; IPR022742; Hydrolase_4.
DR Pfam; PF13026; DUF3887; 1.
DR Pfam; PF12146; Hydrolase_4; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome; Serine esterase; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..412
FT /note="Esterase EstD"
FT /id="PRO_0000432501"
FT ACT_SITE 243
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:17466017"
FT ACT_SITE 347
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:17466017"
FT ACT_SITE 378
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:17466017"
FT MUTAGEN 243
FT /note="S->A: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:17466017"
FT MUTAGEN 347
FT /note="D->N: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:17466017"
FT MUTAGEN 378
FT /note="H->N: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:17466017"
SQ SEQUENCE 412 AA; 46550 MW; 70BC812D936425A5 CRC64;
MRLTVFLSLF LGVMVFGAFD QEAFLFVQHL TSENFESALN MCSNQVKAQL SVQSLSNIWN
SLKAQLSDFR EIAGYEKIIQ AEYEIYNFTL KFDRGEISAL VTMDREGKVA GLFFKQATKT
EYELPDYVDP ESFEEKDITV NGLPGKITIP KGSGPFPAVV LVHGSGPNDM DETIGPNKIF
KDIAYGLSSK GIIVLRYHKR TFVEKVDPTT LTVEKEVIED ALEAVKILKE RKDVSRVYVL
GHSLGAMLTP EIAERSKADG VVMIAPPARP LEEVMEDQLK YLQSLGLASN VEETLNILEK
LKRKEIPPDE FVLGAPAKYF YDLRERDPAS IAKRLTIPML LIFGGRDYQV TEKDQEIWLK
ELSGRENVKI LVFDDLNHLM ISGEGKSTPV EYMKKGHVDK RVIDEIARWM VK
