ID A0A401V0Z7_9CELL Unreviewed; 294 AA.
AC A0A401V0Z7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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:GCD20579.1};
GN ORFNames=CTKZ_21410 {ECO:0000313|EMBL:GCD20579.1};
OS Cellulomonas algicola.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=2071633 {ECO:0000313|EMBL:GCD20579.1, ECO:0000313|Proteomes:UP000288246};
RN [1] {ECO:0000313|EMBL:GCD20579.1, ECO:0000313|Proteomes:UP000288246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TKZ-21 {ECO:0000313|EMBL:GCD20579.1,
RC ECO:0000313|Proteomes:UP000288246};
RA Yamamura H., Hayashi T., Hamada M., Serisawa Y., Matsuyama K., Nakagawa Y.,
RA Otoguro M., Yanagida F., Hayakawa M.;
RT "Draft genome sequence of Cellulomonas takizawaensis strain TKZ-21.";
RL Submitted (NOV-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCD20579.1}.
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DR EMBL; BHYL01000168; GCD20579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401V0Z7; -.
DR OrthoDB; 158614at2; -.
DR Proteomes; UP000288246; 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:SF32; MYCOTHIOL S-CONJUGATE AMIDASE; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, 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 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01482"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01482"
SQ SEQUENCE 294 AA; 32311 MW; D4AE5C724F57EF13 CRC64;
MTGERLRLMA VHAHPDDESS KGAATTAMYA AHGVDVLVVT CTGGERGDVL NPSYGEVEGG
IEGMRAVRTA EMAAAAEALG VRQHWLGFVD SGLPEGDPLP PLPEGCFALQ PLEVASAPLV
ELVREFRPHV ITTYDPSGGY PHPDHIMCHR VAYEAYHAAG DPERYRDRGE PWTPLKLYYN
HGFSMKRMRA MHDALVAAGR ESPFGDWIDS RQAREIPERT ATTFVPVADF FPQRDAALRA
HATQIDPDGF FFAIPREIEL AQWPTEEYEL AHSHVPTTTP EDDLFAGIAR VVGA
//
