MSHB2_SACEN
ID MSHB2_SACEN Reviewed; 274 AA.
AC A4F9Z0;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside deacetylase 2 {ECO:0000255|HAMAP-Rule:MF_01696};
DE Short=GlcNAc-Ins deacetylase 2 {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 2;
GN Name=mshB2 {ECO:0000255|HAMAP-Rule:MF_01696}; OrderedLocusNames=SACE_1543;
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Saccharopolyspora.
OX NCBI_TaxID=405948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
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}.
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DR EMBL; AM420293; CAM00865.1; -; Genomic_DNA.
DR RefSeq; WP_009948198.1; NZ_PDBV01000001.1.
DR AlphaFoldDB; A4F9Z0; -.
DR SMR; A4F9Z0; -.
DR STRING; 405948.SACE_1543; -.
DR EnsemblBacteria; CAM00865; CAM00865; SACE_1543.
DR KEGG; sen:SACE_1543; -.
DR eggNOG; COG2120; Bacteria.
DR HOGENOM; CLU_049311_2_1_11; -.
DR OMA; IGDYGHP; -.
DR OrthoDB; 1380748at2; -.
DR Proteomes; UP000006728; 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..274
FT /note="1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-
FT glucopyranoside deacetylase 2"
FT /id="PRO_0000400219"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
SQ SEQUENCE 274 AA; 29876 MW; 827AB9FC6636E29D CRC64;
MLVHAHPDDE STGTGATMAR YANEGATVSL VTCTSGELGE VVADDLAHLR GNPDALGEHR
RGEIAEALRE LGDIRHHWLG GPGRFRDSGM AGEDTNDAAE CFAKADRDDV TRAMVEILRA
ERPHVVVTYD DTGGYGHPDH IAANHALMYA LGPAADPAYL PELGEPWDVP KVYWMTLPRS
FVKDVQAAGI EGFEPFTVPD EDITAVLDGR DHHAKKLAAL RTYRSQVSLD DGDFFATLVQ
DPRFAIEHYV LVRGERGPGS GPHNWENDLF AGLD