MSHB_MYCTF
ID MSHB_MYCTF Reviewed; 303 AA.
AC A5WLJ9;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
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=TBFG_11195;
OS Mycobacterium tuberculosis (strain F11).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=336982;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F11;
RA Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L.,
RA Grabherr M., Mauceli E., Brockman W., Young S., LaButti K., Pushparaj V.,
RA Sykes S., Baldwin J., Fitzgerald M., Bloom T., Zimmer A., Settipalli S.,
RA Shea T., Arachchi H., Macdonald P., Abouelleil A., Lui A., Priest M.,
RA Berlin A., Gearin G., Brown A., Aftuck L., Bessette D., Allen N.,
RA Lubonja R., Lokyitsang T., Matthews C., Dunbar C., Benamara M., Nguyen T.,
RA Negash T., DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P.,
RA Pearson M., Howarth C., Kodira C., Zeng Q., Yandava C., O'Leary S.,
RA Alvarado L., Victor T., Murray M.;
RT "The complete genome sequence of Mycobacterium tuberculosis F11.";
RL Submitted (APR-2007) 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: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; CP000717; ABR05538.1; -; Genomic_DNA.
DR RefSeq; WP_003406154.1; NZ_KK339377.1.
DR AlphaFoldDB; A5WLJ9; -.
DR SMR; A5WLJ9; -.
DR GeneID; 45425142; -.
DR KEGG; mtf:TBFG_11195; -.
DR PATRIC; fig|336982.11.peg.1317; -.
DR HOGENOM; CLU_049311_2_1_11; -.
DR OMA; YWNRVPR; -.
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; Zinc.
FT CHAIN 1..303
FT /note="1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-
FT glucopyranoside deacetylase"
FT /id="PRO_0000400206"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
SQ SEQUENCE 303 AA; 31742 MW; 09824FF2C02FB3C7 CRC64;
MSETPRLLFV HAHPDDESLS NGATIAHYTS RGAQVHVVTC TLGEEGEVIG DRWAQLTADH
ADQLGGYRIG ELTAALRALG VSAPIYLGGA GRWRDSGMAG TDQRSQRRFV DADPRQTVGA
LVAIIRELRP HVVVTYDPNG GYGHPDHVHT HTVTTAAVAA AGVGSGTADH PGDPWTVPKF
YWTVLGLSAL ISGARALVPD DLRPEWVLPR ADEIAFGYSD DGIDAVVEAD EQARAAKVAA
LAAHATQVVV GPTGRAAALS NNLALPILAD EHYVLAGGSA GARDERGWET DLLAGLGFTA
SGT
