LIPI_MYCTU
ID LIPI_MYCTU Reviewed; 320 AA.
AC P71668; F2GF44; I6XBE2; L0T9A4;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Esterase LipI {ECO:0000305};
DE EC=3.1.1.- {ECO:0000269|PubMed:27154903};
GN Name=lipI {ECO:0000303|PubMed:27154903};
GN OrderedLocusNames=Rv1400c {ECO:0000312|EMBL:CCP44159.1};
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] {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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF SER-165 AND HIS-291.
RC STRAIN=H37Rv;
RX PubMed=27154903; DOI=10.1016/j.pep.2016.04.013;
RA Lin Y., Li Q., Xie L., Xie J.;
RT "Mycobacterium tuberculosis rv1400c encodes functional lipase/esterase.";
RL Protein Expr. Purif. 129:143-149(2017).
CC -!- FUNCTION: Esterase that can hydrolyze short-chain esters with the
CC carbon chain containing 2 to 12 carbon atoms. In vitro, pNP-butyrate is
CC the preferred substrate. {ECO:0000269|PubMed:27154903}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acid ester + H2O = a fatty acid + an aliphatic alcohol
CC + H(+); Xref=Rhea:RHEA:59388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:35748;
CC Evidence={ECO:0000269|PubMed:27154903};
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:27154903};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) +
CC octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657;
CC Evidence={ECO:0000269|PubMed:27154903};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoate ester + H2O = an aliphatic alcohol + decanoate +
CC H(+); Xref=Rhea:RHEA:47360, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:87658;
CC Evidence={ECO:0000269|PubMed:27154903};
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:27154903};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate
CC + H(+); Xref=Rhea:RHEA:47364, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:87659;
CC Evidence={ECO:0000269|PubMed:27154903};
CC -!- ACTIVITY REGULATION: Inhibited by ionic detergents SDS (anions) and
CC CTAB (cationic). Strongly inhibited by Zn(2+).
CC {ECO:0000269|PubMed:27154903}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.32 uM for pNP-butyrate {ECO:0000269|PubMed:27154903};
CC Note=kcat is 210 min(-1) with pNP-butyrate as substrate.
CC {ECO:0000269|PubMed:27154903};
CC pH dependence:
CC Optimum pH is 8.0. Stable between pH 6.0 to 9.0.
CC {ECO:0000269|PubMed:27154903};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:27154903};
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44159.1; -; Genomic_DNA.
DR RefSeq; NP_215916.1; NC_000962.3.
DR RefSeq; WP_003407279.1; NZ_NVQJ01000038.1.
DR AlphaFoldDB; P71668; -.
DR SMR; P71668; -.
DR STRING; 83332.Rv1400c; -.
DR ChEMBL; CHEMBL4105752; -.
DR SwissLipids; SLP:000001356; -.
DR ESTHER; myctu-Rv1400c; Hormone-sensitive_lipase_like.
DR PaxDb; P71668; -.
DR PRIDE; P71668; -.
DR DNASU; 886728; -.
DR GeneID; 886728; -.
DR KEGG; mtu:Rv1400c; -.
DR PATRIC; fig|83332.111.peg.1559; -.
DR TubercuList; Rv1400c; -.
DR eggNOG; COG0657; Bacteria.
DR OMA; LWYPSTM; -.
DR PhylomeDB; P71668; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0008126; F:acetylesterase activity; IEA:RHEA.
DR GO; GO:0034338; F:short-chain carboxylesterase activity; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR002168; Lipase_GDXG_HIS_AS.
DR InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..320
FT /note="Esterase LipI"
FT /id="PRO_0000448851"
FT ACT_SITE 165
FT /evidence="ECO:0000250|UniProtKB:O06350"
FT ACT_SITE 261
FT /evidence="ECO:0000250|UniProtKB:O06350"
FT ACT_SITE 291
FT /evidence="ECO:0000250|UniProtKB:O06350"
FT MUTAGEN 165
FT /note="S->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:27154903"
FT MUTAGEN 291
FT /note="H->A: 90% loss of activity."
FT /evidence="ECO:0000269|PubMed:27154903"
SQ SEQUENCE 320 AA; 34053 MW; D95637B78DEB12BD CRC64;
MPSLDNTADE KPAIDPILLK VLDAVPFRLS IDDGIEAVRQ RLRDLPRQPV HPELRVVDLA
IDGPAGPIGT RIYWPPTCPD QAEAPVVLYF HGGGFVMGDL DTHDGTCRQH AVGADAIVVS
VDYRLAPEHP YPAAIEDAWA ATRWVAEHGR QVGADLGRIA VAGDSAGGTI AAVIAQRARD
MGGPPIVFQL LWYPSTLWDQ SLPSLAENAD APILDVKAIA AFSRWYAGEI DLHNPPAPMA
PGRAENLADL PPAYIAVAGY DPLRDDGIRY GELLAAAGVP VEVHNAQTLV HGYVGYAGVV
PAATEATNRG LVALRVVLHG
