ARSC2_CORGK
ID ARSC2_CORGK Reviewed; 129 AA.
AC P0DKS8; Q6M898; Q8NTP3;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Arsenate-mycothiol transferase ArsC2;
DE EC=2.8.4.2;
DE AltName: Full=Mycothiol-dependent arsenate reductase ArsC2;
GN Name=arsC2; Synonyms=arsX; OrderedLocusNames=WA5_0259;
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; CCH23480.1; -; Genomic_DNA.
DR RefSeq; WP_003863342.1; NC_020519.1.
DR AlphaFoldDB; P0DKS8; -.
DR SMR; P0DKS8; -.
DR KEGG; cgu:WA5_0259; -.
DR PATRIC; fig|1204414.5.peg.281; -.
DR HOGENOM; CLU_071415_3_3_11; -.
DR OMA; FMCVRNA; -.
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..129
FT /note="Arsenate-mycothiol transferase ArsC2"
FT /id="PRO_0000420636"
SQ SEQUENCE 129 AA; 13763 MW; 9279EF21FF0E52B8 CRC64;
MKSVLFVCVG NGGKSQMAAA LAQKYASDSV EIHSAGTKPA QGLNQLSVES IAEVGADMSQ
GIPKAIDPEL LRTVDRVVIL GDDAQVDMPE SAQGALERWS IEEPDAQGME RMRIVRDQID
NRVQALLAG