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Database: UniProt
Entry: A0A1H8DN39_9ACTN
LinkDB: A0A1H8DN39_9ACTN
Original site: A0A1H8DN39_9ACTN 
ID   A0A1H8DN39_9ACTN        Unreviewed;       283 AA.
AC   A0A1H8DN39;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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   ORFNames=SAMN05216267_1001184 {ECO:0000313|EMBL:SEN08224.1};
OS   Actinacidiphila rubida.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Actinacidiphila.
OX   NCBI_TaxID=310780 {ECO:0000313|EMBL:SEN08224.1, ECO:0000313|Proteomes:UP000181951};
RN   [1] {ECO:0000313|EMBL:SEN08224.1, ECO:0000313|Proteomes:UP000181951}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.2026 {ECO:0000313|EMBL:SEN08224.1,
RC   ECO:0000313|Proteomes:UP000181951};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FODD01000001; SEN08224.1; -; Genomic_DNA.
DR   RefSeq; WP_069461816.1; NZ_MDCQ01000022.1.
DR   AlphaFoldDB; A0A1H8DN39; -.
DR   STRING; 310780.SAMN05216267_1001184; -.
DR   OrthoDB; 158614at2; -.
DR   Proteomes; UP000181951; Unassembled WGS sequence.
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:UP000181951};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01482}.
FT   BINDING         11
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01482"
FT   BINDING         14
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01482"
FT   BINDING         139
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01482"
SQ   SEQUENCE   283 AA;  30717 MW;  FA1115121660F2D3 CRC64;
     MVLRIMAVHA HPDDESSKGA ATLAHYAAQG VEATVVTCTG GERGDVLNPL LDTPEVRADL
     PAVRRREMAA AAAVLGVRQR FLGFADSGLV AEGEPLPDGC FALQDVAVAA ERLVAVIREI
     RPHVVVTYDP SGGYPHPDHV QTHRVAVAAF DAAGEEAAYP DAGPAWRPDK LYYLAAYSRS
     WFETLHNGML AAGVPSAMGA VLDDWPDWAP DLSPTTRVVC DGHFATRDRA FRAHATQAAP
     DAPFFAHPRD LERRLWPTED YVLARSRRPA RLPEANLFDG IQE
//
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