NLHH_MYCTU
ID NLHH_MYCTU Reviewed; 319 AA.
AC P9WK87; F2GF45; L0T9I5; P71667; Q7D8H2;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=Carboxylesterase NlhH {ECO:0000305};
DE EC=3.1.1.1 {ECO:0000269|PubMed:15373841};
DE AltName: Full=NLH-H {ECO:0000303|PubMed:15373841};
GN Name=nlhH; Synonyms=lipH {ECO:0000303|PubMed:15373841};
GN OrderedLocusNames=Rv1399c;
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 FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND GENE NAME.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15373841; DOI=10.1111/j.1432-1033.2004.04335.x;
RA Canaan S., Maurin D., Chahinian H., Pouilly B., Durousseau C.,
RA Frassinetti F., Scappuccini-Calvo L., Cambillau C., Bourne Y.;
RT "Expression and characterization of the protein Rv1399c from Mycobacterium
RT tuberculosis. A novel carboxyl esterase structurally related to the HSL
RT family.";
RL Eur. J. Biochem. 271:3953-3961(2004).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
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 [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=27690385; DOI=10.1021/acsinfecdis.6b00135;
RA Tallman K.R., Levine S.R., Beatty K.E.;
RT "Small-molecule probes reveal esterases with persistent activity in dormant
RT and reactivating Mycobacterium tuberculosis.";
RL ACS Infect. Dis. 2:936-944(2016).
CC -!- FUNCTION: Hydrolyzes various short-chain esters, such as
CC triacylglycerols and vinyl esters. Has no activity against emulsified
CC substrates. {ECO:0000269|PubMed:15373841}.
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:15373841};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21165;
CC Evidence={ECO:0000269|PubMed:15373841};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a propanoate ester + H2O = an aliphatic alcohol + H(+) +
CC propanoate; Xref=Rhea:RHEA:48484, ChEBI:CHEBI:2571,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17272,
CC ChEBI:CHEBI:36243; Evidence={ECO:0000269|PubMed:15373841};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48485;
CC Evidence={ECO:0000269|PubMed:15373841};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tripropanoylglycerol + H2O = dipropanoylglycerol + H(+)
CC + propanoate; Xref=Rhea:RHEA:48024, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17272, ChEBI:CHEBI:88153,
CC ChEBI:CHEBI:88155; Evidence={ECO:0000269|PubMed:15373841};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48025;
CC Evidence={ECO:0000269|PubMed:15373841};
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:15373841};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349;
CC Evidence={ECO:0000269|PubMed:15373841};
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:15373841};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12958;
CC Evidence={ECO:0000269|PubMed:15373841};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tributanoylglycerol + H2O = butanoate +
CC dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020,
CC ChEBI:CHEBI:76478; Evidence={ECO:0000269|PubMed:15373841};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC Evidence={ECO:0000269|PubMed:15373841};
CC -!- ACTIVITY REGULATION: Strongly inhibited by diethyl paranitrophenyl
CC phosphate, which is a specific inhibitor of serine hydrolases.
CC {ECO:0000269|PubMed:15373841}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:15373841};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:15373841};
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:15373841}.
CC -!- DEVELOPMENTAL STAGE: Remains active in dormant M.tuberculosis.
CC {ECO:0000269|PubMed:27690385}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44158.1; -; Genomic_DNA.
DR PIR; D70900; D70900.
DR RefSeq; NP_215915.1; NC_000962.3.
DR RefSeq; WP_003407276.1; NZ_NVQJ01000038.1.
DR AlphaFoldDB; P9WK87; -.
DR SMR; P9WK87; -.
DR STRING; 83332.Rv1399c; -.
DR SwissLipids; SLP:000001381; -.
DR iPTMnet; P9WK87; -.
DR PaxDb; P9WK87; -.
DR DNASU; 886731; -.
DR GeneID; 45425377; -.
DR GeneID; 886731; -.
DR KEGG; mtu:Rv1399c; -.
DR TubercuList; Rv1399c; -.
DR eggNOG; COG0657; Bacteria.
DR OMA; HTFPTAW; -.
DR PhylomeDB; P9WK87; -.
DR SABIO-RK; P9WK87; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0008126; F:acetylesterase activity; IEA:RHEA.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0034338; F:short-chain carboxylesterase activity; IDA:MTBBASE.
DR GO; GO:0009056; P:catabolic process; IDA:MTBBASE.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acetylation; Hydrolase; Reference proteome; Serine esterase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..319
FT /note="Carboxylesterase NlhH"
FT /id="PRO_0000419169"
FT MOTIF 88..90
FT /note="Involved in the stabilization of the negatively
FT charged intermediate by the formation of the oxyanion hole"
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 162
FT /evidence="ECO:0000250|UniProtKB:O06350"
FT ACT_SITE 260
FT /evidence="ECO:0000250|UniProtKB:O06350"
FT ACT_SITE 290
FT /evidence="ECO:0000250|UniProtKB:O06350"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
SQ SEQUENCE 319 AA; 33906 MW; E7CFD7B1D8848699 CRC64;
MTEPTVARPD IDPVLKMLLD TFPVTFTAAD GVEVARARLR QLKTPPELLP ELRIEERTVG
YDGLTDIPVR VYWPPVVRDN LPVVVYYHGG GWSLGGLDTH DPVARAHAVG AQAIVVSVDY
RLAPEHPYPA GIDDSWAALR WVGENAAELG GDPSRIAVAG DSAGGNISAV MAQLARDVGG
PPLVFQLLWY PTTMADLSLP SFTENADAPI LDRDVIDAFL AWYVPGLDIS DHTMLPTTLA
PGNADLSGLP PAFIGTAEHD PLRDDGACYA ELLTAAGVSV ELSNEPTMVH GYVNFALVVP
AAAEATGRGL AALKRALHA
