(data stored in ACNUC1104 zone)

SWISSPROT: MCA_STRCO

ID   MCA_STRCO               Reviewed;         293 AA.
AC   Q9ADK0;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 87.
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=SCO4967;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [2]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=18430082; DOI=10.1111/j.1365-2958.2008.06191.x;
RA   Park J.H., Roe J.H.;
RT   "Mycothiol regulates and is regulated by a thiol-specific antisigma factor
RT   RsrA and sigma(R) in Streptomyces coelicolor.";
RL   Mol. Microbiol. 68:861-870(2008).
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       ECO:0000269|PubMed:18430082}.
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   -!- INDUCTION: Transiently induced by thiol-oxidant diamide, under direct
CC       control of SigR. Also induced when MSH is oxidized or conjugated.
CC       {ECO:0000269|PubMed:18430082}.
CC   -!- DISRUPTION PHENOTYPE: Loss of amidase activity on mycothiol bimane,
CC       leading to dramatically decreased levels of N-acetylcysteinyl bimane.
CC       Increased sensitivity to a number of alkylating agents and antibiotics
CC       including N-ethylmaleimide and lincomycin.
CC       {ECO:0000269|PubMed:18430082}.
CC   -!- SIMILARITY: Belongs to the MshB deacetylase family. Mca subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01482}.
DR   EMBL; AL939122; CAD30952.1; -; Genomic_DNA.
DR   RefSeq; NP_629119.1; NC_003888.3.
DR   RefSeq; WP_003974009.1; NC_003888.3.
DR   SMR; Q9ADK0; -.
DR   STRING; 100226.SCO4967; -.
DR   EnsemblBacteria; CAD30952; CAD30952; CAD30952.
DR   GeneID; 1100408; -.
DR   KEGG; sco:SCO4967; -.
DR   PATRIC; fig|100226.15.peg.5047; -.
DR   eggNOG; ENOG4105T1M; Bacteria.
DR   eggNOG; COG2120; LUCA.
DR   HOGENOM; HOG000241173; -.
DR   InParanoid; Q9ADK0; -.
DR   KO; K18455; -.
DR   OMA; PLKLYYN; -.
DR   PhylomeDB; Q9ADK0; -.
DR   Proteomes; UP000001973; 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; IMP:UniProtKB.
DR   GO; GO:0010127; P:mycothiol-dependent detoxification; IMP:UniProtKB.
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   2: Evidence at transcript level;
DR   PRODOM; Q9ADK0.
DR   SWISS-2DPAGE; Q9ADK0.
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..293
FT                   /note="Mycothiol S-conjugate amidase"
FT                   /id="PRO_0000423188"
FT   METAL           13
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01482"
FT   METAL           16
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01482"
FT   METAL           144
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01482"
SQ   SEQUENCE   293 AA;  33164 MW;  6F5B515F0154B696 CRC64;
     MTDQLRLMAV HAHPDDESSK GAATMAKYVS EGVDVLVVTC TGGERGSILN PKLQGDAYIE
     ENIHEVRRKE MDEAREILGV GQEWLGFVDS GLPEGDPLPP LPEGCFALED VDKAAGELVR
     KIRSFRPQVI TTYDENGGYP HPDHIMTHKI TMVAFEGAAD TEKYPESEYG TAYQPLKVYY
     NQGFNRPRTE ALHHALLDRG LESPYEDWLK RWSEFERKER TLTTHVPCAD FFEIRDKALI
     AHATQIDPEG GWFRVPMEIQ KEVWPTEEYE LAKSLVETSL PEDDLFAGIR DNA
//

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