ID   Y3376_MYCTO             Reviewed;         217 AA.
AC   P9WMS4; F2GEC2; L0TDY8; O50405; Q7D5L7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Phosphatase MT3486;
DE            EC=3.1.-.-;
GN   OrderedLocusNames=MT3486;
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: Able to hydrolyze geranyl diphosphate (GPP), farnesyl
CC       diphosphate (FPP) and geranylgeranyl diphosphate (GGPP) to respectively
CC       yield geraniol, farnesol and geranylgeraniol. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK47822.1; -; Genomic_DNA.
DR   PIR; G70972; G70972.
DR   RefSeq; WP_003417903.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMS4; -.
DR   SMR; P9WMS4; -.
DR   EnsemblBacteria; AAK47822; AAK47822; MT3486.
DR   KEGG; mtc:MT3486; -.
DR   PATRIC; fig|83331.31.peg.3743; -.
DR   HOGENOM; CLU_045011_9_3_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR023214; HAD_sf.
DR   PRINTS; PR00413; HADHALOGNASE.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR   TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..217
FT                   /note="Phosphatase MT3486"
FT                   /id="PRO_0000427251"
FT   ACT_SITE        9
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   217 AA;  23664 MW;  0AFCDC61F2BD0156 CRC64;
     MSISAVVFDR DGVLTSFDWT RAEEDVRRIT GLPLEEIERR WGGWLNGLTI DDAFVETQPI
     SEFLSSLARE LELGSKARDE LVRLDYMAFA QGYPDARPAL EEARRRGLKV GVLTNNSLLV
     SARSLLQCAA LHDLVDVVLS SQMIGAAKPD PRAYQAIAEA LGVSTTSCLF FDDIADWVEG
     ARCAGMRAYL VDRSGQTRDG VVRDLSSLGA ILDGAGP