ID   MSHB2_FRACC             Reviewed;         314 AA.
AC   Q2J678;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase 2 {ECO:0000255|HAMAP-Rule:MF_01696};
DE            Short=GlcNAc-Ins deacetylase 2 {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 2;
GN   Name=mshB2 {ECO:0000255|HAMAP-Rule:MF_01696};
GN   OrderedLocusNames=Francci3_3864;
OS   Frankia casuarinae (strain DSM 45818 / CECT 9043 / CcI3).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=106370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45818 / CECT 9043 / CcI3;
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(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; CP000249; ABD13214.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2J678; -.
DR   SMR; Q2J678; -.
DR   STRING; 106370.Francci3_3864; -.
DR   EnsemblBacteria; ABD13214; ABD13214; Francci3_3864.
DR   KEGG; fra:Francci3_3864; -.
DR   eggNOG; COG2120; Bacteria.
DR   HOGENOM; CLU_049311_2_1_11; -.
DR   OMA; YWNRVPR; -.
DR   PhylomeDB; Q2J678; -.
DR   Proteomes; UP000001937; 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..314
FT                   /note="1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-
FT                   glucopyranoside deacetylase 2"
FT                   /id="PRO_0000400186"
FT   BINDING         25
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
FT   BINDING         28
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
SQ   SEQUENCE   314 AA;  33683 MW;  31FEA7F02FA6A784 CRC64;
     MTTATPSSPS TAPLPTRRAM FVHAHPDDEV ISTGIALASY AASPDTHVTL VTCTLGEEGE
     VLVPELIHLR ADRGDQLGGY RIGELAGACA ALGITDQRFL GGPGRWRDSG MIGTPANDHP
     RCLWRADLDE AAAELVRIVR EVRPQVLVSY DARGGYGHPD HIRAHELTRR AFTDAADPSF
     APQAGSVWQV AKRYETALAR SSAVAGFEYF RDSAAESNPF AGLTSVDELG VTLVDDADIT
     TELSAPHFFE AKIAAMRSHR TQMSVDGFFF ALADGIGQRA WSVEHFVLAE GARGPGDGPD
     GRERDLFAGL VCEP