ID   MSHB_MYCMM              Reviewed;         301 AA.
AC   B2HSB3;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 61.
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=MMAR_4283;
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
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; CP000854; ACC42691.1; -; Genomic_DNA.
DR   RefSeq; WP_012395852.1; NC_010612.1.
DR   AlphaFoldDB; B2HSB3; -.
DR   SMR; B2HSB3; -.
DR   STRING; 216594.MMAR_4283; -.
DR   EnsemblBacteria; ACC42691; ACC42691; MMAR_4283.
DR   KEGG; mmi:MMAR_4283; -.
DR   eggNOG; COG2120; Bacteria.
DR   HOGENOM; CLU_049311_2_1_11; -.
DR   OMA; YWNRVPR; -.
DR   OrthoDB; 1380748at2; -.
DR   Proteomes; UP000001190; 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; Reference proteome; Zinc.
FT   CHAIN           1..301
FT                   /note="1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-
FT                   glucopyranoside deacetylase"
FT                   /id="PRO_0000400200"
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;  32013 MW;  8B2C00FF209B6E3B CRC64;
     MPETPRLLFV HAHPDDESLS NGATIAHYAA RGAQVHVVTC TLGEEGEVIG DRWAQLAVDH
     ADQLGGYRIG ELTAALQRLG VDAPIYLGGA GRWRDSGMAG TEQRGRRRFV DADDREAVGA
     LVAIIRELRP HVVVTYDPDG GYGHPDHVQA HVVTTAAVAA AGSVGDCDYP GDPWVVPKFY
     WTILGLSAFL AGRQALTPDD LLPEWVLPPE DIPFIYPDER IDAVVTGDSD ARAAKIAALA
     AHATQVTVGP SGRACALSNN MALPILADEH YLLVAGRAGA RDERGWETDL LAGLGFTGFG
     T