ID   ARSC1_CORGK             Reviewed;         140 AA.
AC   P0DKS6; Q6M575; Q8NQC7;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Arsenate-mycothiol transferase ArsC1;
DE            EC=2.8.4.2;
DE   AltName: Full=Mycothiol-dependent arsenate reductase ArsC1;
GN   Name=arsC1; OrderedLocusNames=WA5_1454;
OS   Corynebacterium glutamicum (strain ATCC 13032 / K051).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1204414;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / K051;
RX   PubMed=22640862; DOI=10.1186/gb-2012-13-5-r40;
RA   Binder S., Schendzielorz G., Stabler N., Krumbach K., Hoffmann K., Bott M.,
RA   Eggeling L.;
RT   "A high-throughput approach to identify genomic variants of bacterial
RT   metabolite producers at the single-cell level.";
RL   Genome Biol. 13:R40.1-R40.12(2012).
CC   -!- FUNCTION: Involved in defense against toxic arsenate. Involved in the
CC       mycothiol/myoredoxin redox pathway which uses a mycothioltransferase
CC       mechanism; facilitates adduct formation between arsenate and mycothiol
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=arsenate + mycothiol = arseno-mycothiol + H2O;
CC         Xref=Rhea:RHEA:27349, ChEBI:CHEBI:15377, ChEBI:CHEBI:16768,
CC         ChEBI:CHEBI:48597, ChEBI:CHEBI:59655; EC=2.8.4.2;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC       phosphatase family. {ECO:0000305}.
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DR   EMBL; HE802067; CCH24674.1; -; Genomic_DNA.
DR   RefSeq; WP_011014415.1; NC_020519.1.
DR   AlphaFoldDB; P0DKS6; -.
DR   SMR; P0DKS6; -.
DR   KEGG; cgu:WA5_1454; -.
DR   PATRIC; fig|1204414.5.peg.1560; -.
DR   HOGENOM; CLU_071415_3_3_11; -.
DR   OMA; IDGMERM; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0102100; F:mycothiol-arsenate ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW.
DR   InterPro; IPR023485; Ptyr_pPase.
DR   InterPro; IPR036196; Ptyr_pPase_sf.
DR   Pfam; PF01451; LMWPc; 1.
DR   SMART; SM00226; LMWPc; 1.
DR   SUPFAM; SSF52788; SSF52788; 1.
PE   3: Inferred from homology;
KW   Arsenical resistance; Cytoplasm; Transferase.
FT   CHAIN           1..140
FT                   /note="Arsenate-mycothiol transferase ArsC1"
FT                   /id="PRO_0000420635"
SQ   SEQUENCE   140 AA;  15117 MW;  8F19A3BFDC697C48 CRC64;
     MNNQPSVLFV CVGNGGKSQM AAALAKKHAG DALKVYSAGT KPGTKLNQQS LDSIAEVGAD
     MSQGFPKGID QELIKRVDRV VILGAEAQLE MPIDANGILQ RWVTDEPSER GIEGMERMRL
     VRDDIDARVQ NLVAELTQNA