ID   MSHB1_FRAAA             Reviewed;         289 AA.
AC   Q0RKY6;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase 1 {ECO:0000255|HAMAP-Rule:MF_01696};
DE            Short=GlcNAc-Ins deacetylase 1 {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 1;
GN   Name=mshB1 {ECO:0000255|HAMAP-Rule:MF_01696}; OrderedLocusNames=FRAAL3175;
OS   Frankia alni (strain ACN14a).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=326424;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACN14a;
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; CT573213; CAJ61819.1; -; Genomic_DNA.
DR   RefSeq; WP_011604324.1; NC_008278.1.
DR   AlphaFoldDB; Q0RKY6; -.
DR   SMR; Q0RKY6; -.
DR   STRING; 326424.FRAAL3175; -.
DR   KEGG; fal:FRAAL3175; -.
DR   eggNOG; COG2120; Bacteria.
DR   HOGENOM; CLU_049311_2_1_11; -.
DR   OMA; IGDYGHP; -.
DR   OrthoDB; 1380748at2; -.
DR   Proteomes; UP000000657; 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..289
FT                   /note="1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-
FT                   glucopyranoside deacetylase 1"
FT                   /id="PRO_0000400183"
FT   BINDING         4
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
FT   BINDING         7
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
SQ   SEQUENCE   289 AA;  31209 MW;  E8CE48C3EDAE789F CRC64;
     MHAHPDDEVI ATGATMAHYA ADRDTRVVLV TCTLGEMGEV LIPELINLRA DHADQLGGYR
     IGELERACAA LGVTDHRFLG GAGRWRDSGM MSSPSNADPR SFWRADLTAA SEALVRIVRE
     VRPQVMVTYD AIGDYGHPDH IRAHDVTVRA FDDAADPDFA PQAGEPWQVS KLYETALSRA
     AVDAAVDQLW RSDLAKTAPE GISMPSDMLL SVPDAKVTTR IEAPDFFAAK VEAMRAHRTQ
     MTVDGFFFAL VNGDGQAARA TEHYVLARGT PGPPAASGKE DDLFAGLVP