ID A0A088QU86_9CORY Unreviewed; 267 AA.
AC A0A088QU86;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:AIN81316.1};
GN ORFNames=DR71_508 {ECO:0000313|EMBL:AIN81316.1};
OS Corynebacterium sp. ATCC 6931.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1487956 {ECO:0000313|EMBL:AIN81316.1, ECO:0000313|Proteomes:UP000029247};
RN [1] {ECO:0000313|EMBL:AIN81316.1, ECO:0000313|Proteomes:UP000029247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6931 {ECO:0000313|Proteomes:UP000029247};
RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA Scholz M.B., Teshima H., Xu Y.;
RL Submitted (JUL-2014) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01482}.
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DR EMBL; CP008913; AIN81316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A088QU86; -.
DR STRING; 1487956.DR71_508; -.
DR KEGG; coa:DR71_508; -.
DR eggNOG; COG2120; Bacteria.
DR HOGENOM; CLU_049311_2_2_11; -.
DR Proteomes; UP000029247; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000029247};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01482}.
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01482"
SQ SEQUENCE 267 AA; 29983 MW; 1C99B20206BA27CA CRC64;
MARYAAEGHR VKVVTCTGGE AGSILNPAMD RPEVRENIAA VRVHEMAAAA ETLGVEHEWL
GFTDSGLPAG NPVPVLSHGV FARQSVEDAT KPLIRAIREF RPHVIITYDE NGGYPHPDHI
MTHIVSMRAW LESGTDKYPE LGEPWEISKL YYTHGFIKAR LIALDNYYRD NGLESPLAES
FRRWTKTPGD IMTRVTTQVE CGDYFQQRDQ ALLAHATQID PNGPFFAVPV DIQQRVWPTE
EFELARTRVQ TELPETDLFA GIDPDAE
//
