MSHB_STRAW
ID MSHB_STRAW Reviewed; 294 AA.
AC Q82IJ5;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase {ECO:0000255|HAMAP-Rule:MF_01696};
DE Short=GlcNAc-Ins deacetylase {ECO:0000255|HAMAP-Rule:MF_01696};
DE EC=3.5.1.103 {ECO:0000255|HAMAP-Rule:MF_01696};
DE AltName: Full=N-acetyl-1-D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase;
GN Name=mshB {ECO:0000255|HAMAP-Rule:MF_01696}; OrderedLocusNames=SAV_3138;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
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:0000255|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:0000255|HAMAP-Rule:MF_01696};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01696};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01696};
CC -!- SIMILARITY: Belongs to the MshB deacetylase family. {ECO:0000255|HAMAP-
CC Rule:MF_01696}.
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; BA000030; BAC70849.1; -; Genomic_DNA.
DR RefSeq; WP_010984568.1; NZ_JZJK01000090.1.
DR AlphaFoldDB; Q82IJ5; -.
DR SMR; Q82IJ5; -.
DR STRING; 227882.SAV_3138; -.
DR EnsemblBacteria; BAC70849; BAC70849; SAVERM_3138.
DR KEGG; sma:SAVERM_3138; -.
DR eggNOG; COG2120; Bacteria.
DR HOGENOM; CLU_049311_2_1_11; -.
DR OMA; YWNRVPR; -.
DR OrthoDB; 1380748at2; -.
DR Proteomes; UP000000428; Chromosome.
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; -; 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 PANTHER; PTHR12993; PTHR12993; 1.
DR Pfam; PF02585; PIG-L; 1.
DR SUPFAM; SSF102588; SSF102588; 1.
DR TIGRFAMs; TIGR03445; mycothiol_MshB; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..294
FT /note="1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-
FT glucopyranoside deacetylase"
FT /id="PRO_0000400224"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
SQ SEQUENCE 294 AA; 31773 MW; 25D7861DBC3DE674 CRC64;
MKDLPDRRLL LVHAHPDDES INNGATMARY AAEGAQVTLV TCTLGEEGEV IPPALAHLTP
DRDDALGPYR VGELAAAMKE LGVTDHRFLG GPGRYRDSGM MGGEQNHRAG AFWAADLDEA
AGHLVAVVRE VRPQVLVTYD PDGGYGHPDH IQAHRVAVRA AELAADPAFR PELGTPWEIA
KVYWNRVPRP VAEEGFARLR LALPGTRFAK SAAVDDVPGV VDESVITTEI DGTPFAAAKA
AAMRAHATQV EVDGPWFALS NELAQPLFTT EYYELVRGER GSPRETDLFE GVAP
