ID   MCA_MYCTO               Reviewed;         288 AA.
AC   P9WJN0; L7N5N8;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Mycothiol S-conjugate amidase {ECO:0000255|HAMAP-Rule:MF_01482};
DE            EC=3.5.1.115 {ECO:0000255|HAMAP-Rule:MF_01482};
GN   Name=mca {ECO:0000255|HAMAP-Rule:MF_01482}; OrderedLocusNames=MT1113;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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:0000255|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:0000255|HAMAP-Rule:MF_01482};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01482};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01482};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01482}.
CC   -!- SIMILARITY: Belongs to the MshB deacetylase family. Mca subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01482}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK45369.1; -; Genomic_DNA.
DR   PIR; H70894; H70894.
DR   RefSeq; WP_003405746.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WJN0; -.
DR   SMR; P9WJN0; -.
DR   EnsemblBacteria; AAK45369; AAK45369; MT1113.
DR   GeneID; 45425055; -.
DR   KEGG; mtc:MT1113; -.
DR   PATRIC; fig|83331.31.peg.1198; -.
DR   HOGENOM; CLU_049311_2_2_11; -.
DR   Proteomes; UP000001020; 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; -; 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   PANTHER; PTHR12993; PTHR12993; 1.
DR   PANTHER; PTHR12993:SF16; PTHR12993:SF16; 1.
DR   Pfam; PF02585; PIG-L; 1.
DR   SUPFAM; SSF102588; SSF102588; 1.
DR   TIGRFAMs; TIGR03446; mycothiol_Mca; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..288
FT                   /note="Mycothiol S-conjugate amidase"
FT                   /id="PRO_0000427801"
FT   BINDING         12
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01482"
FT   BINDING         15
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01482"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01482"
SQ   SEQUENCE   288 AA;  32732 MW;  C19E3AAA882892DE CRC64;
     MSELRLMAVH AHPDDESSKG AATLARYADE GHRVLVVTLT GGERGEILNP AMDLPDVHGR
     IAEIRRDEMT KAAEILGVEH TWLGFVDSGL PKGDLPPPLP DDCFARVPLE VSTEALVRVV
     REFRPHVMTT YDENGGYPHP DHIRCHQVSV AAYEAAGDFC RFPDAGEPWT VSKLYYVHGF
     LRERMQMLQD EFARHGQRGP FEQWLAYWDP DHDFLTSRVT TRVECSKYFS QRDDALRAHA
     TQIDPNAEFF AAPLAWQERL WPTEEFELAR SRIPARPPET ELFAGIEP