ID A0A2M9JMT6_9ACTN Unreviewed; 297 AA.
AC A0A2M9JMT6;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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:PJN08180.1};
GN ORFNames=CG723_29690 {ECO:0000313|EMBL:PJN08180.1};
OS Streptomyces sp. CB01635.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2020326 {ECO:0000313|EMBL:PJN08180.1, ECO:0000313|Proteomes:UP000232157};
RN [1] {ECO:0000313|Proteomes:UP000232157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01635 {ECO:0000313|Proteomes:UP000232157};
RA Pan G., Xu Z., Guo Z., Ma M., Yang D., Zhou H., Gansemans Y., Zhu X.,
RA Zhao L.-X., Jiang Y., Cheng J., van Nieuwerburgh F., Suh J.W., Duan Y.,
RA Shen B.;
RT "Discovery of the Leinamycin Family of Natural Products by Mining
RT Actinobacterial Genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:0-0(2017).
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:PJN08180.1}.
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DR EMBL; NNBL01000015; PJN08180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9JMT6; -.
DR OrthoDB; 158614at2; -.
DR Proteomes; UP000232157; 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:UP000232157};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, 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 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01696"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01696"
SQ SEQUENCE 297 AA; 31918 MW; BB669170740CD469 CRC64;
MTELPDRRLL LVHAHPDDES INNGATMAKY AADGAHVTLV TCTLGEEGEV IPDVLAHLAP
DREDILGPHR IGELTAAMKE LGVTDHRFLG GPGRFRDSGM TGAEQNDRPG AFWAADLDEA
AAHLVEVIRE VRPQVLVTYD PDGGYGHPDH IKAHRVAMRA AELAAEPAFR RDLGDTHAVS
KIYWNRVPRS VVEERFRWLA GVLGSTPYGT AAEIGDVPGV VDDERVTAEI DGRAFAAAKT
AAMRAHATQV EIAPGGEPVF ALSNGLAQPV FDVEYYELAR GEAAAPHETD LFAGVVA
//
