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Database: UniProt
Entry: J7LAC6_NOCAA
LinkDB: J7LAC6_NOCAA
Original site: J7LAC6_NOCAA 
ID   J7LAC6_NOCAA            Unreviewed;       292 AA.
AC   J7LAC6;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Mycothiol S-conjugate amidase {ECO:0000256|HAMAP-Rule:MF_01482};
DE            EC=3.5.1.115 {ECO:0000256|HAMAP-Rule:MF_01482};
GN   Name=mca {ECO:0000256|HAMAP-Rule:MF_01482,
GN   ECO:0000313|EMBL:AFR09616.1};
GN   OrderedLocusNames=B005_2887 {ECO:0000313|EMBL:AFR09616.1};
OS   Nocardiopsis alba (strain ATCC BAA-2165 / BE74).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=1205910 {ECO:0000313|EMBL:AFR09616.1, ECO:0000313|Proteomes:UP000003779};
RN   [1] {ECO:0000313|EMBL:AFR09616.1, ECO:0000313|Proteomes:UP000003779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2165 / BE74 {ECO:0000313|Proteomes:UP000003779};
RX   PubMed=23105086; DOI=10.1128/JB.01522-12;
RA   Qiao J., Chen L., Li Y., Wang J., Zhang W., Chen S.;
RT   "Whole-Genome Sequence of Nocardiopsis alba Strain ATCC BAA-2165,
RT   Associated with Honeybees.";
RL   J. Bacteriol. 194:6358-6359(2012).
RN   [2] {ECO:0000313|Proteomes:UP000003779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2165 / BE74 {ECO:0000313|Proteomes:UP000003779};
RA   Qiao J., Chen L., Li Y., Wang J., Zhang W., Chen S.;
RT   "Whole-genome sequence of Nocardiopsis alba strain ATCC BAA-2165 associated
RT   with honeybees.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: A mycothiol (MSH, N-acetylcysteinyl-glucosaminyl-inositol) S-
CC       conjugate amidase, it recycles conjugated MSH to the N-acetyl cysteine
CC       conjugate (AcCys S-conjugate, a mercapturic acid) and the MSH
CC       precursor. Involved in MSH-dependent detoxification of a number of
CC       alkylating agents and antibiotics. {ECO:0000256|HAMAP-Rule:MF_01482}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + mycothiol S-conjugate = 1D-myo-inositol 2-amino-2-deoxy-
CC         alpha-D-glucopyranoside + an N-acetyl-L-cysteine-S-conjugate;
CC         Xref=Rhea:RHEA:36543, ChEBI:CHEBI:15377, ChEBI:CHEBI:58718,
CC         ChEBI:CHEBI:58886, ChEBI:CHEBI:59633; EC=3.5.1.115;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01482};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01482};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01482};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01482}.
CC   -!- SIMILARITY: Belongs to the MshB deacetylase family. Mca subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01482}.
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DR   EMBL; CP003788; AFR09616.1; -; Genomic_DNA.
DR   RefSeq; WP_014912071.1; NC_018524.1.
DR   AlphaFoldDB; J7LAC6; -.
DR   STRING; 1205910.B005_2887; -.
DR   KEGG; nal:B005_2887; -.
DR   PATRIC; fig|1205910.3.peg.2728; -.
DR   eggNOG; COG2120; Bacteria.
DR   HOGENOM; CLU_049311_2_2_11; -.
DR   OMA; QEWLGFV; -.
DR   Proteomes; UP000003779; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0010126; P:mycothiol metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0010127; P:mycothiol-dependent detoxification; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.10320; LmbE-like; 1.
DR   HAMAP; MF_01482; Mca; 1.
DR   InterPro; IPR003737; GlcNAc_PI_deacetylase-related.
DR   InterPro; IPR024078; LmbE-like_dom_sf.
DR   InterPro; IPR017811; Mca.
DR   NCBIfam; TIGR03446; mycothiol_Mca; 1.
DR   PANTHER; PTHR12993:SF11; N-ACETYLGLUCOSAMINYL-PHOSPHATIDYLINOSITOL DE-N-ACETYLASE; 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_01482};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01482};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003779};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01482}.
FT   BINDING         13
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01482"
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01482"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01482"
SQ   SEQUENCE   292 AA;  32997 MW;  74DAA1F79FE3FA26 CRC64;
     MSERLRLMAV HAHPDDESSK GAATMARYVQ EGAEVLVVTM TGGERGDILN PAMERPEIRE
     NIAEVRRQEM DRAREILGIE QEFAGFVDSG LPEGDPLPPL PEGCFATLPV EEAAAPLVAA
     IRRFRPHVIL TYDENGGYPH PDHIMTHKAS MHAFDAAPEP EAYPEAGEPW QPLKLYYFVG
     FPPERFDALA RTLAEHGMEN PFEEWAARVK DMERRRWEIT TRVHCSEYFE VANDALRAHA
     TQIDPNGFWF AVPNEIVAEA WPTEDYHLVR SLVDTEVPEK DLFAGVREAV RV
//
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