EST45_MYCTU
ID EST45_MYCTU Reviewed; 298 AA.
AC I6XU97;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Esterase Rv0045c {ECO:0000305|PubMed:20957207};
DE EC=3.1.1.1 {ECO:0000269|PubMed:20957207, ECO:0000269|PubMed:25354081};
GN OrderedLocusNames=Rv0045c {ECO:0000312|EMBL:CCP42767.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP CRYSTALLIZATION, AND SUBUNIT.
RX PubMed=21139199; DOI=10.1107/s1744309110026606;
RA Xu L., Guo J., Zheng X., Wen T., Sun F., Liu S., Pang H.;
RT "Crystallization and preliminary X-ray analysis of a novel esterase Rv0045c
RT from Mycobacterium tuberculosis.";
RL Acta Crystallogr. F 66:1579-1582(2010).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20957207; DOI=10.1371/journal.pone.0013143;
RA Guo J., Zheng X., Xu L., Liu Z., Xu K., Li S., Wen T., Liu S., Pang H.;
RT "Characterization of a novel esterase Rv0045c from Mycobacterium
RT tuberculosis.";
RL PLoS ONE 5:e13143-e13143(2010).
RN [4] {ECO:0007744|PubMed:21969609}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVE SITE, AND
RP MUTAGENESIS OF SER-122; ASP-146 AND HIS-277.
RX PubMed=25354081; DOI=10.1021/bi501108u;
RA Lukowski J.K., Savas C.P., Gehring A.M., McKary M.G., Adkins C.T.,
RA Lavis L.D., Hoops G.C., Johnson R.J.;
RT "Distinct substrate selectivity of a metabolic hydrolase from Mycobacterium
RT tuberculosis.";
RL Biochemistry 53:7386-7395(2014).
RN [6] {ECO:0007744|PDB:3P2M}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), ACTIVE SITE, AND DOMAIN.
RX PubMed=21637775; DOI=10.1371/journal.pone.0020506;
RA Zheng X., Guo J., Xu L., Li H., Zhang D., Zhang K., Sun F., Wen T., Liu S.,
RA Pang H.;
RT "Crystal structure of a novel esterase Rv0045c from Mycobacterium
RT tuberculosis.";
RL PLoS ONE 6:e20506-e20506(2011).
CC -!- FUNCTION: Esterase likely involved in ester/lipid metabolism. Shows
CC strong substrate selectivity toward short, straight chain alkyl esters
CC with the highest activity toward four atom chains. The physiological
CC substrate is unknown (PubMed:25354081). Is able to hydrolyze ester
CC bonds within a wide range of p-nitrophenyl derivatives (C2-C14) in
CC vitro (PubMed:20957207). {ECO:0000269|PubMed:20957207,
CC ECO:0000269|PubMed:25354081}.
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:20957207, ECO:0000269|PubMed:25354081};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate +
CC H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477;
CC Evidence={ECO:0000269|PubMed:25354081};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+);
CC Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622;
CC Evidence={ECO:0000269|PubMed:20957207};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a hexanoate ester + H2O = an aliphatic alcohol + H(+) +
CC hexanoate; Xref=Rhea:RHEA:47352, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:87656;
CC Evidence={ECO:0000269|PubMed:20957207};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tetradecanoate ester + H2O = an aliphatic alcohol + H(+) +
CC tetradecanoate; Xref=Rhea:RHEA:47388, ChEBI:CHEBI:2571,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807,
CC ChEBI:CHEBI:87691; Evidence={ECO:0000269|PubMed:20957207};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0 for the hydrolysis of p-nitrophenyl hexanoate.
CC {ECO:0000269|PubMed:20957207};
CC Temperature dependence:
CC Optimum temperature is 39 degrees Celsius for the hydrolysis of p-
CC nitrophenyl hexanoate. {ECO:0000269|PubMed:20957207};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:21139199}.
CC -!- DOMAIN: Contains two distinct structural domains: an almost globular
CC alpha/beta fold domain and an inserted cap domain which interacts with
CC the alpha/beta fold domain. {ECO:0000269|PubMed:21637775}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP42767.1; -; Genomic_DNA.
DR RefSeq; NP_214559.1; NC_000962.3.
DR RefSeq; WP_003400489.1; NZ_NVQJ01000005.1.
DR PDB; 3P2M; X-ray; 2.80 A; A=2-298.
DR PDB; 6WYM; X-ray; 2.00 A; A=2-298.
DR PDB; 6WYN; X-ray; 1.81 A; A=2-298.
DR PDBsum; 3P2M; -.
DR PDBsum; 6WYM; -.
DR PDBsum; 6WYN; -.
DR AlphaFoldDB; I6XU97; -.
DR SMR; I6XU97; -.
DR STRING; 83332.Rv0045c; -.
DR SwissLipids; SLP:000001363; -.
DR ESTHER; myctu-RV0045C; 6_AlphaBeta_hydrolase.
DR PaxDb; I6XU97; -.
DR PRIDE; I6XU97; -.
DR DNASU; 887029; -.
DR GeneID; 45424004; -.
DR GeneID; 887029; -.
DR KEGG; mtu:Rv0045c; -.
DR PATRIC; fig|83332.111.peg.51; -.
DR TubercuList; Rv0045c; -.
DR eggNOG; COG0596; Bacteria.
DR eggNOG; COG2021; Bacteria.
DR OMA; GTWTWRY; -.
DR PhylomeDB; I6XU97; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
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; IPR000073; AB_hydrolase_1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome; Serine esterase.
FT CHAIN 1..298
FT /note="Esterase Rv0045c"
FT /id="PRO_0000451571"
FT ACT_SITE 122
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:21637775,
FT ECO:0000305|PubMed:25354081"
FT ACT_SITE 146
FT /evidence="ECO:0000305|PubMed:25354081"
FT ACT_SITE 277
FT /evidence="ECO:0000305|PubMed:21637775,
FT ECO:0000305|PubMed:25354081"
FT SITE 58
FT /note="Involved in substrate selectivity"
FT /evidence="ECO:0000269|PubMed:25354081"
FT SITE 155
FT /note="Involved in substrate selectivity"
FT /evidence="ECO:0000269|PubMed:25354081"
FT MUTAGEN 122
FT /note="S->A: 550-fold decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:25354081"
FT MUTAGEN 146
FT /note="D->A: 55-fold decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:25354081"
FT MUTAGEN 277
FT /note="H->A: 9000-fold decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:25354081"
FT TURN 12..15
FT /evidence="ECO:0007829|PDB:6WYN"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:6WYN"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:6WYN"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:6WYN"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:6WYN"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:6WYN"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:6WYN"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:6WYN"
FT HELIX 97..111
FT /evidence="ECO:0007829|PDB:6WYN"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:6WYN"
FT HELIX 123..134
FT /evidence="ECO:0007829|PDB:6WYN"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:6WYN"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:6WYN"
FT HELIX 149..167
FT /evidence="ECO:0007829|PDB:6WYN"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:6WYM"
FT HELIX 178..188
FT /evidence="ECO:0007829|PDB:6WYN"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:6WYN"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:6WYN"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:6WYN"
FT HELIX 227..235
FT /evidence="ECO:0007829|PDB:6WYN"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:6WYN"
FT HELIX 253..262
FT /evidence="ECO:0007829|PDB:6WYN"
FT STRAND 264..272
FT /evidence="ECO:0007829|PDB:6WYN"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:6WYN"
FT HELIX 284..295
FT /evidence="ECO:0007829|PDB:6WYN"
SQ SEQUENCE 298 AA; 32131 MW; 7EB753899DC49281 CRC64;
MLSDDELTGL DEFALLAENA EQAGVNGPLP EVERVQAGAI SALRWGGSAP RVIFLHGGGQ
NAHTWDTVIV GLGEPALAVD LPGHGHSAWR EDGNYSPQLN SETLAPVLRE LAPGAEFVVG
MSLGGLTAIR LAAMAPDLVG ELVLVDVTPS ALQRHAELTA EQRGTVALMH GEREFPSFQA
MLDLTIAAAP HRDVKSLRRG VFHNSRRLDN GNWVWRYDAI RTFGDFAGLW DDVDALSAPI
TLVRGGSSGF VTDQDTAELH RRATHFRGVH IVEKSGHSVQ SDQPRALIEI VRGVLDTR
