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Database: UniProt
Entry: A0A0Q7K2Z3_9ACTN
LinkDB: A0A0Q7K2Z3_9ACTN
Original site: A0A0Q7K2Z3_9ACTN 
ID   A0A0Q7K2Z3_9ACTN        Unreviewed;       324 AA.
AC   A0A0Q7K2Z3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
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   ORFNames=ASD06_08185 {ECO:0000313|EMBL:KQX65609.1};
OS   Angustibacter sp. Root456.
OC   Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae.
OX   NCBI_TaxID=1736539 {ECO:0000313|EMBL:KQX65609.1, ECO:0000313|Proteomes:UP000051170};
RN   [1] {ECO:0000313|EMBL:KQX65609.1, ECO:0000313|Proteomes:UP000051170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root456 {ECO:0000313|EMBL:KQX65609.1,
RC   ECO:0000313|Proteomes:UP000051170};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQX65609.1, ECO:0000313|Proteomes:UP000051170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root456 {ECO:0000313|EMBL:KQX65609.1,
RC   ECO:0000313|Proteomes:UP000051170};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQX65609.1}.
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DR   EMBL; LMER01000016; KQX65609.1; -; Genomic_DNA.
DR   RefSeq; WP_056676577.1; NZ_LMER01000016.1.
DR   AlphaFoldDB; A0A0Q7K2Z3; -.
DR   STRING; 1736539.ASD06_08185; -.
DR   OrthoDB; 158614at2; -.
DR   Proteomes; UP000051170; 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};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01696};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051170};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01696}.
FT   BINDING         25
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01696"
FT   BINDING         28
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01696"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01696"
SQ   SEQUENCE   324 AA;  34644 MW;  0910A713CACCE124 CRC64;
     MSYAFDGEPA LGHLPGRRLV LVHAHPDDET LTTGITMAQA VAEGVEVTLV TCTLGEQGEV
     IPRELKHLEG RDDAALAHHR AAELAAAMRA IGVRDHRVLG GGRWRDSGME WLEPGIAGGL
     DAAHAQAAHP AAFARADLDE AAGLLADVLR DVRPQVVVTY DPQGGYGHPD HVMAHRVTMR
     AVELAERDAA RPGWMVPAVH WVQVAQSWAD AERRAVLAAA ADGRLPEGMT ASGASDPFPP
     AVVPDDLLDV VVEAPQHLDA VVAALRSHVT QVRVEPPWFA LSNDVARRLT GREGFRRVRG
     PRAATRGRVA DDLFAGLDIG APRD
//
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