ID V7JPD2_MYCAV Unreviewed; 303 AA.
AC V7JPD2;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=O982_06795 {ECO:0000313|EMBL:ETA99384.1};
OS Mycobacterium avium 10-5581.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1392000 {ECO:0000313|EMBL:ETA99384.1, ECO:0000313|Proteomes:UP000018557};
RN [1] {ECO:0000313|EMBL:ETA99384.1, ECO:0000313|Proteomes:UP000018557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10-5581 {ECO:0000313|EMBL:ETA99384.1,
RC ECO:0000313|Proteomes:UP000018557};
RA Bannantine J.P., Robbe-Austerman S., O'Connell C.;
RT "Genome sequence of MAC strains.";
RL Submitted (OCT-2013) 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:ETA99384.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYNT01000076; ETA99384.1; -; Genomic_DNA.
DR AlphaFoldDB; V7JPD2; -.
DR PATRIC; fig|1392000.4.peg.1438; -.
DR Proteomes; UP000018557; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01696}.
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01696"
FT BINDING 19
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 303 AA; 32363 MW; B6E54A3F97F8050E CRC64;
MRFMAETPRL LFVHAHPDDE SLGTGATIAH YTAAGADVRV VTCTLGEEGE VIGERWAELA
VDRADQLGGY RIGELTAALR ELGVGEPCYL GGAGRWRDSG MPGTPRRRRQ RFIDADEREA
VGALVAVIRE QRPHVVVGYD PAGGYGHPDH VHVHTVTTAA VAAAGAGDFP GEPWAVSKFY
WSVFATRPFE AAVQALTPED LRPDWSMPSA EQFTFGYADD HIDAVVAAGP HAWAAKRAAL
AAHATQVVVG PTGRACALSN NVALPILDEE HYVLVAGAAG ARDERGWETD LLAGLEFGAA
PRR
//