ID   MSHB_COREF              Reviewed;         311 AA.
AC   Q8FQG1;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=CE1158;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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; BA000035; BAC17968.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8FQG1; -.
DR   SMR; Q8FQG1; -.
DR   STRING; 196164.23492996; -.
DR   EnsemblBacteria; BAC17968; BAC17968; BAC17968.
DR   KEGG; cef:CE1158; -.
DR   eggNOG; COG2120; Bacteria.
DR   HOGENOM; CLU_049311_2_1_11; -.
DR   OMA; YWNRVPR; -.
DR   Proteomes; UP000001409; 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..311
FT                   /note="1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-
FT                   glucopyranoside deacetylase"
FT                   /id="PRO_0000400177"
FT   BINDING         29
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
FT   BINDING         32
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
SQ   SEQUENCE   311 AA;  33230 MW;  83D98137727D7E8E CRC64;
     MASRAQRTGG RMILHNDLSG LRVVAVHAHP DDEAITTGGA LHHLATRGAD VTVVTCTLGE
     QGEVIGETWQ QLVNGDADQL GGFRIHELLS SLRILGASGC FLGGAGRWRD SGMVGDPAND
     HPRSFVRSGD QAEEQLVEIF TMLRPHLVIT YGPDGGYGHP DHIRAHEITH GAAGRVEGIQ
     RILWAVTGRT DLQAGLDAIS AVPTGWRAAG DDELACQDRV DFALELDDRA YHAKVESMRA
     HATQLWIADG GVSDTNPHAA FAEVTDRAAA PVVFALSNLI AQPVMRREHY QLGAGTAFPA
     DAQGPADGLQ W