MSHB_GORB4
ID MSHB_GORB4 Reviewed; 283 AA.
AC D0LD40;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 54.
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=Gbro_3329;
OS Gordonia bronchialis (strain ATCC 25592 / DSM 43247 / BCRC 13721 / JCM 3198
OS / KCTC 3076 / NBRC 16047 / NCTC 10667) (Rhodococcus bronchialis).
OC Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia.
OX NCBI_TaxID=526226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25592 / DSM 43247 / BCRC 13721 / JCM 3198 / KCTC 3076 / NBRC
RC 16047 / NCTC 10667;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Jando M., Schneider S., Goeker M., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Gordonia bronchialis DSM 43247.";
RL Submitted (OCT-2009) 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; CP001802; ACY22533.1; -; Genomic_DNA.
DR RefSeq; WP_012835048.1; NC_013441.1.
DR AlphaFoldDB; D0LD40; -.
DR SMR; D0LD40; -.
DR STRING; 526226.Gbro_3329; -.
DR EnsemblBacteria; ACY22533; ACY22533; Gbro_3329.
DR KEGG; gbr:Gbro_3329; -.
DR eggNOG; COG2120; Bacteria.
DR HOGENOM; CLU_049311_2_1_11; -.
DR OMA; YWNRVPR; -.
DR OrthoDB; 1380748at2; -.
DR Proteomes; UP000001219; 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..283
FT /note="1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-
FT glucopyranoside deacetylase"
FT /id="PRO_0000400189"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01696"
SQ SEQUENCE 283 AA; 29802 MW; 50413529E8E483B8 CRC64;
MLLVHAHPDD ETIMTGGTIA RYLDEGVDVR VLTFTLGEEG EVIGDRWAQL VADGGADQLG
GFRIGELTGA LAALSPPGGS PVQPWFLGGA GRWRDSGMAG SAAARHPRAL VNAGFDEPVG
VLTDILESFA PQVVITYDSA GTYGHPDHKL VHEVTAAALA RVAASRPEQI KVYESVTEHS
ALQAGLVAAA RRVPDGWRMP GPGELPSYPD AMVTAEIDVR TQYDRKVAAL AAHATQVTVA
PSGTEYALSN NIVQPIFGHE HFIRVDAAAV AGPRETDLFD GIG
