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Database: UniProt
Entry: A0A1H8SDV7_9ACTN
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ID   A0A1H8SDV7_9ACTN        Unreviewed;       297 AA.
AC   A0A1H8SDV7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=SAMN05660991_01611 {ECO:0000313|EMBL:SEO76534.1};
OS   Blastococcus endophyticus.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=673521 {ECO:0000313|EMBL:SEO76534.1, ECO:0000313|Proteomes:UP000198960};
RN   [1] {ECO:0000313|EMBL:SEO76534.1, ECO:0000313|Proteomes:UP000198960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45413 {ECO:0000313|EMBL:SEO76534.1,
RC   ECO:0000313|Proteomes:UP000198960};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOEE01000004; SEO76534.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8SDV7; -.
DR   STRING; 673521.SAMN05660991_01611; -.
DR   Proteomes; UP000198960; 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:SF26; 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   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01696}.
FT   REGION          276..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   297 AA;  31473 MW;  99351A311099A20D CRC64;
     MIDRRLLLVH AHPDDETINN GATMARYVAE GARVTLLTCT LGEEGEVLVP GLAQLAADQA
     DQLGGFRIGE LAAAMAALGV TDWRFLGGAG RYRDSGMIGT EANAKPRAFW NADLDEAVGH
     AVAVVRETRP QVLVTYDDNG GYGHPDHIQA HRVAMAAVDA AADPGYRPEL GEPWSVAKVY
     WCCVPRSVLR EGAEAMASLG EASPFEQLGD VEEIPFAVPD EVVTAAVDGR DAAGAKHAAM
     RAHATQITVD GPFFALSNNF GQEVLGVEHY RLVRGERGPA GPGPHGWEDD LFAGLGG
//
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