(data stored in ACNUC7421 zone)

SWISSPROT: Q47ST0_THEFY

ID   Q47ST0_THEFY            Unreviewed;       290 AA.
AC   Q47ST0;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 78.
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   OrderedLocusNames=Tfu_0449 {ECO:0000313|EMBL:AAZ54487.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54487.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: A mycothiol (MSH, N-acetylcysteinyl-glucosaminyl-
CC       inositol) S-conjugate amidase, it recycles conjugated MSH to the
CC       N-acetyl cysteine conjugate (AcCys S-conjugate, a mercapturic
CC       acid) and the MSH precursor. Involved in MSH-dependent
CC       detoxification of a number of alkylating agents and antibiotics.
CC       {ECO:0000256|HAMAP-Rule:MF_01482}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + mycothiol S-conjugate = 1D-myo-inositol 2-amino-2-
CC         deoxy-alpha-D-glucopyranoside + an N-acetyl-L-cysteine-S-
CC         conjugate; Xref=Rhea:RHEA:36543, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:58718, ChEBI:CHEBI:58886, ChEBI:CHEBI:59633;
CC         EC=3.5.1.115; Evidence={ECO:0000256|HAMAP-Rule:MF_01482};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01482};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       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; CP000088; AAZ54487.1; -; Genomic_DNA.
DR   STRING; 269800.Tfu_0449; -.
DR   EnsemblBacteria; AAZ54487; AAZ54487; Tfu_0449.
DR   KEGG; tfu:Tfu_0449; -.
DR   eggNOG; ENOG4105T1M; Bacteria.
DR   eggNOG; COG2120; LUCA.
DR   HOGENOM; HOG000241173; -.
DR   KO; K18455; -.
DR   OMA; PLKLYYN; -.
DR   BioCyc; TFUS269800:G1G4Q-456-MONOMER; -.
DR   Proteomes; UP000000434; 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;
DR   PRODOM; Q47ST0.
DR   SWISS-2DPAGE; Q47ST0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01482};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01482};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01482}.
FT   METAL        13     13       Zinc. {ECO:0000256|HAMAP-Rule:MF_01482}.
FT   METAL        16     16       Zinc. {ECO:0000256|HAMAP-Rule:MF_01482}.
FT   METAL       143    143       Zinc. {ECO:0000256|HAMAP-Rule:MF_01482}.
SQ   SEQUENCE   290 AA;  33175 MW;  992F5B0ACCF92F18 CRC64;
     MSERLRLMAV HAHPDDESSK GAATMARYVN EGAEVLVVTL TGGERGSILN PAMDRPEIRE
     NIAEVRRKEM EEARRILGVR QVFVGFIDSG LPEGDPPPPL PEGCFALQPL EVAAEPVVRL
     VREFRPHVMI TYDEQGGYPH PDHIMCHKVS VEAFEAAADP ERYPGTGEPW QTSKLYYHVS
     FPLERFEAIA KVLSDRGMEN PYADWMKRLE KRDTRRWEIT TRVECGEYFE VRDRALLAHA
     TQIDPNSFWF AVPNDIQREA WPTEDYHLAR SFVDTELPED DLFAGIRDKV
//

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