ID A0A365H5Y3_9ACTN Unreviewed; 290 AA.
AC A0A365H5Y3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase {ECO:0000256|HAMAP-Rule:MF_01696};
DE Short=GlcNAc-Ins deacetylase {ECO:0000256|HAMAP-Rule:MF_01696};
DE EC=3.5.1.103 {ECO:0000256|HAMAP-Rule:MF_01696};
DE AltName: Full=N-acetyl-1-D-myo-inositol-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase {ECO:0000256|HAMAP-Rule:MF_01696};
GN Name=mshB {ECO:0000256|HAMAP-Rule:MF_01696,
GN ECO:0000313|EMBL:RAY14448.1};
GN ORFNames=DPM19_15960 {ECO:0000313|EMBL:RAY14448.1};
OS Actinomadura craniellae.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=2231787 {ECO:0000313|EMBL:RAY14448.1, ECO:0000313|Proteomes:UP000251891};
RN [1] {ECO:0000313|EMBL:RAY14448.1, ECO:0000313|Proteomes:UP000251891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LHW63021 {ECO:0000313|EMBL:RAY14448.1,
RC ECO:0000313|Proteomes:UP000251891};
RA Li L., Xu Q.H., Lin H.W., Lu Y.H.;
RT "Actinomadura craniellae sp. nov. isolated from marine sponge Craniella
RT sp.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01696};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01696};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01696};
CC -!- SIMILARITY: Belongs to the MshB deacetylase family. {ECO:0000256|HAMAP-
CC Rule:MF_01696}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RAY14448.1}.
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DR EMBL; QLYX01000006; RAY14448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365H5Y3; -.
DR OrthoDB; 158614at2; -.
DR Proteomes; UP000251891; Unassembled WGS sequence.
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; LmbE-like; 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 NCBIfam; TIGR03445; mycothiol_MshB; 1.
DR PANTHER; PTHR12993:SF31; 1D-MYO-INOSITOL 2-ACETAMIDO-2-DEOXY-ALPHA-D-GLUCOPYRANOSIDE DEACETYLASE; 1.
DR PANTHER; PTHR12993; N-ACETYLGLUCOSAMINYL-PHOSPHATIDYLINOSITOL DE-N-ACETYLASE-RELATED; 1.
DR Pfam; PF02585; PIG-L; 1.
DR SUPFAM; SSF102588; LmbE-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01696, ECO:0000313|EMBL:RAY14448.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01696};
KW Reference proteome {ECO:0000313|Proteomes:UP000251891};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01696}.
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01696"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01696"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01696"
SQ SEQUENCE 290 AA; 31889 MW; 0A88B402E1CD4E9D CRC64;
MSERRILFVH AHPDDESIGT GATMAKYAAE GVQVSLVTCT LGEEGEVIPD ELRHLAADKE
NRLGEFRTGE LAEACGALGV RDHHYLGGPG RWRDSGMMGA PSNDHPRCFW RADAEEAAAE
LVPLIRELRP QVIVTYDDRG YYGHPDHIQA HRVTRRAYEL AADPGYGEGE PWRVAKLYAT
AMPRSVLVRS IAVMAASETP FERVSGVDEL TYGVPDEEVT TVVDARDHLR AKIDALRAHR
TQIVVAEPFF ALSNNVGQQA FGVEYYTLIE GERGPSAADG RETDLFSGLS
//
