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 03-AUG-2022, entry version 95.
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}.
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DR EMBL; AL939122; CAD30952.1; -; Genomic_DNA.
DR RefSeq; NP_629119.1; NC_003888.3.
DR RefSeq; WP_003974009.1; NC_003888.3.
DR AlphaFoldDB; Q9ADK0; -.
DR SMR; Q9ADK0; -.
DR STRING; 100226.SCO4967; -.
DR GeneID; 1100408; -.
DR KEGG; sco:SCO4967; -.
DR PATRIC; fig|100226.15.peg.5047; -.
DR eggNOG; COG2120; Bacteria.
DR HOGENOM; CLU_049311_2_2_11; -.
DR InParanoid; Q9ADK0; -.
DR OMA; PLKLYYN; -.
DR PhylomeDB; Q9ADK0; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
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;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..293
FT /note="Mycothiol S-conjugate amidase"
FT /id="PRO_0000423188"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01482"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01482"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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
