ID   MSHB_MYCUA              Reviewed;         301 AA.
AC   A0PMQ6;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase {ECO:0000255|HAMAP-Rule:MF_01696};
DE            Short=GlcNAc-Ins deacetylase {ECO:0000255|HAMAP-Rule:MF_01696};
DE            EC=3.5.1.103 {ECO:0000255|HAMAP-Rule:MF_01696};
DE   AltName: Full=N-acetyl-1-D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase;
GN   Name=mshB {ECO:0000255|HAMAP-Rule:MF_01696}; OrderedLocusNames=MUL_1017;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA   Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
CC   -!- FUNCTION: Catalyzes the deacetylation of 1D-myo-inositol 2-acetamido-2-
CC       deoxy-alpha-D-glucopyranoside (GlcNAc-Ins) in the mycothiol
CC       biosynthesis pathway. {ECO:0000255|HAMAP-Rule:MF_01696}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside +
CC         H2O = 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside +
CC         acetate; Xref=Rhea:RHEA:26180, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:52442, ChEBI:CHEBI:58886; EC=3.5.1.103;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01696};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01696};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01696};
CC   -!- SIMILARITY: Belongs to the MshB deacetylase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01696}.
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DR   EMBL; CP000325; ABL03625.1; -; Genomic_DNA.
DR   RefSeq; WP_011739248.1; NC_008611.1.
DR   AlphaFoldDB; A0PMQ6; -.
DR   SMR; A0PMQ6; -.
DR   STRING; 362242.MUL_1017; -.
DR   EnsemblBacteria; ABL03625; ABL03625; MUL_1017.
DR   KEGG; mul:MUL_1017; -.
DR   eggNOG; COG2120; Bacteria.
DR   HOGENOM; CLU_049311_2_1_11; -.
DR   OMA; YWNRVPR; -.
DR   Proteomes; UP000000765; Chromosome.
DR   GO; GO:0035595; F:N-acetylglucosaminylinositol deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0010125; P:mycothiol biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.10320; -; 1.
DR   HAMAP; MF_01696; MshB; 1.
DR   InterPro; IPR003737; GlcNAc_PI_deacetylase-related.
DR   InterPro; IPR024078; LmbE-like_dom_sf.
DR   InterPro; IPR017810; Mycothiol_biosynthesis_MshB.
DR   PANTHER; PTHR12993; PTHR12993; 1.
DR   Pfam; PF02585; PIG-L; 1.
DR   SUPFAM; SSF102588; SSF102588; 1.
DR   TIGRFAMs; TIGR03445; mycothiol_MshB; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..301
FT                   /note="1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-
FT                   glucopyranoside deacetylase"
FT                   /id="PRO_0000400208"
FT   BINDING         13
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
SQ   SEQUENCE   301 AA;  32027 MW;  E57984E5B0153569 CRC64;
     MPETPRLLFV HAHPDDESLS NGATIAHYAA RGAQVHVVTC TLGEEGEVIG DRWAQLAVDH
     ADQLGGYRIG ELTAALQRLG VDAPIYLGGA GRWRDSGMAG TEQRSRRRFV DADDREAVGA
     LVAIIRELRP HVVVTYDPDG GYGHPDHVQA HVVTTAAVAA AGSVGDCDYP GDPWVVPKFY
     WTVLGVSAFL AGRQALTPDD LLPEWVLPPE DIPFIYPDER IDAVVTGDSD ARAAKIAALA
     AHATQVTVGP SGRACALSNN MALPILADEH YLLVAGRAGA RDERGWEIDL LAGLGFTGFG
     T