ID   Y505_MYCTO              Reviewed;         308 AA.
AC   P9WGJ2; L0T6W2; P66801; Q11169;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Putative hydrolase MT0526;
DE            EC=3.1.-.-;
GN   OrderedLocusNames=MT0526;
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK44749.1; -; Genomic_DNA.
DR   AlphaFoldDB; P9WGJ2; -.
DR   SMR; P9WGJ2; -.
DR   EnsemblBacteria; AAK44749; AAK44749; MT0526.
DR   KEGG; mtc:MT0526; -.
DR   HOGENOM; CLU_052657_0_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006385; HAD_hydro_SerB1.
DR   InterPro; IPR023214; HAD_sf.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01490; HAD-SF-IB-hyp1; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..308
FT                   /note="Putative hydrolase MT0526"
FT                   /id="PRO_0000428352"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        62
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        64
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   BINDING         62
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         64
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   308 AA;  32673 MW;  EA722C653C3A88DC CRC64;
     MMVSSHLGSP DQAGHVDLAS PADPPPPDAS ASHSPVDMPA PVAAAGSDRQ PPIDLTAAAF
     FDVDNTLVQG SSAVHFGRGL AARHYFTYRD VLGFLYAQAK FQLLGKENSN DVAAGRRKAL
     AFIEGRSVAE LVALGEEIYD EIIADKIWDG TRELTQMHLD AGQQVWLITA TPYELAATIA
     RRLGLTGALG TVAESVDGIF TGRLVGEILH GTGKAHAVRS LAIREGLNLK RCTAYSDSYN
     DVPMLSLVGT AVAINPDARL RSLARERGWE IRDFRIARKA ARIGVPSALA LGAAGGALAA
     LASRRQSR