ID A0A1X6WX07_9MICO Unreviewed; 557 AA.
AC A0A1X6WX07;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 08-OCT-2025, entry version 24.
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=FM110_04655 {ECO:0000313|EMBL:SLM90191.1};
OS Brachybacterium nesterenkovii.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC Dermabacteraceae; Brachybacterium.
OX NCBI_TaxID=47847 {ECO:0000313|EMBL:SLM90191.1, ECO:0000313|Proteomes:UP000195981};
RN [1] {ECO:0000313|EMBL:SLM90191.1, ECO:0000313|Proteomes:UP000195981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP104813 {ECO:0000313|EMBL:SLM90191.1,
RC ECO:0000313|Proteomes:UP000195981};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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=mycothiol S-conjugate + H2O = an N-acetyl-L-cysteine-S-
CC conjugate + 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside;
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; FWFG01000045; SLM90191.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6WX07; -.
DR Proteomes; UP000195981; Unassembled WGS sequence.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:TreeGrafter.
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:UP000195981};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01482}.
FT REGION 127..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..191
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..230
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01482"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01482"
FT BINDING 414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01482"
SQ SEQUENCE 557 AA; 60039 MW; B2872FCF31D38235 CRC64;
MCSCAPQDHV TVVDRAILHA GRGGPSQARR ARSGVRHHIG GRSGALAVDD LRGDRLALRG
DLDGVQRLRR VLRGDIDLRE AHLAARRVQR LHAAAHRGAR TGRDLERQGD RAGVGMLVGD
RVRAHRLVGE AQPHEHRGGD EDRPGDDRDD PPATPVGAAT VSGIEALGAR EIAPALGGGA
DGVIGRSGGH GASVSEPSPG DRAGRSSRPI DPERAGGGPG PRSTASGGGA RPRHSSARVQ
ARGVICRRPS PSDAPILHDP RSPVTQTATA PSAPLRMVAV HAHPDDESSK GAASMARYVH
EGVQVTVITC TGGERGDILN PKMAEDPEAL ADLPAVRRRE MARAQEILGV DHEWLGFEDS
GLPEGDPLPA LPEGSFATLE LDVAARPLVE ALRRLRPQVL TTYNENGGYP HPDHIMTHRV
SMRAVDLAAD GTFAPELGEP WEVLKVYYNN DFSRQRFAAI ARYMTEQGMG SAELDAWLER
FDERDDRLLT TRVDVRDYLA IRDEALRAHA TQVDPDGFFF AVPHDVLDAA WPTDDYELRM
SRIGVTLPET DLFAGIR
//
