ID   NLHH_MYCTO              Reviewed;         319 AA.
AC   P9WK86; 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 35.
DE   RecName: Full=Carboxylesterase NlhH {ECO:0000250|UniProtKB:P9WK87};
DE            EC=3.1.1.1 {ECO:0000250|UniProtKB:P9WK87};
GN   Name=nlhH; Synonyms=lipH; OrderedLocusNames=MT1443;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Hydrolyzes various short-chain esters.
CC       {ECO:0000250|UniProtKB:P9WK87}.
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:0000250|UniProtKB:P9WK87};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P9WK87}.
CC   -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK45708.1; -; Genomic_DNA.
DR   PIR; D70900; D70900.
DR   RefSeq; WP_003407276.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WK86; -.
DR   SMR; P9WK86; -.
DR   MEROPS; S09.951; -.
DR   EnsemblBacteria; AAK45708; AAK45708; MT1443.
DR   GeneID; 45425377; -.
DR   KEGG; mtc:MT1443; -.
DR   PATRIC; fig|83331.31.peg.1551; -.
DR   HOGENOM; CLU_012494_6_4_11; -.
DR   Proteomes; UP000001020; Chromosome.
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; IPR013094; AB_hydrolase_3.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Serine esterase.
FT   CHAIN           1..319
FT                   /note="Carboxylesterase NlhH"
FT                   /id="PRO_0000427697"
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:Q5NUF3"
FT   ACT_SITE        260
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
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