ID   ARSC1_CORGL             Reviewed;         140 AA.
AC   P0DKS5; Q6M575; Q8NQC7;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 1.
DT   03-AUG-2022, entry version 44.
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=cg1706, Cgl1511;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
RN   [3]
RP   INDUCTION.
RX   PubMed=16204540; DOI=10.1128/aem.71.10.6206-6215.2005;
RA   Ordonez E., Letek M., Valbuena N., Gil J.A., Mateos L.M.;
RT   "Analysis of genes involved in arsenic resistance in Corynebacterium
RT   glutamicum ATCC 13032.";
RL   Appl. Environ. Microbiol. 71:6206-6215(2005).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=19286650; DOI=10.1074/jbc.m900877200;
RA   Ordonez E., Van Belle K., Roos G., De Galan S., Letek M., Gil J.A.,
RA   Wyns L., Mateos L.M., Messens J.;
RT   "Arsenate reductase, mycothiol, and mycoredoxin concert thiol/disulfide
RT   exchange.";
RL   J. Biol. Chem. 284:15107-15116(2009).
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       {ECO:0000269|PubMed:19286650}.
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         Evidence={ECO:0000269|PubMed:19286650};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=82 mM for arsenate in the presence of mycoredoxin 1, mycothiol,
CC         mycothione reductase and NADPH {ECO:0000269|PubMed:19286650};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: By arsenite. {ECO:0000269|PubMed:16204540}.
CC   -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC       phosphatase family. {ECO:0000305}.
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DR   EMBL; BA000036; BAB98904.1; -; Genomic_DNA.
DR   EMBL; BX927152; CAF21520.1; -; Genomic_DNA.
DR   RefSeq; NP_600727.2; NC_003450.3.
DR   RefSeq; WP_011014415.1; NC_006958.1.
DR   AlphaFoldDB; P0DKS5; -.
DR   SMR; P0DKS5; -.
DR   STRING; 196627.cg1706; -.
DR   KEGG; cgb:cg1706; -.
DR   KEGG; cgl:Cgl1511; -.
DR   PATRIC; fig|196627.13.peg.1479; -.
DR   eggNOG; COG0394; Bacteria.
DR   HOGENOM; CLU_071415_3_3_11; -.
DR   OMA; IDGMERM; -.
DR   BRENDA; 1.20.4.4; 960.
DR   BRENDA; 2.8.4.2; 960.
DR   SABIO-RK; P0DKS5; -.
DR   Proteomes; UP000000582; Chromosome.
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   1: Evidence at protein level;
KW   Arsenical resistance; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..140
FT                   /note="Arsenate-mycothiol transferase ArsC1"
FT                   /id="PRO_0000418724"
SQ   SEQUENCE   140 AA;  15117 MW;  8F19A3BFDC697C48 CRC64;
     MNNQPSVLFV CVGNGGKSQM AAALAKKHAG DALKVYSAGT KPGTKLNQQS LDSIAEVGAD
     MSQGFPKGID QELIKRVDRV VILGAEAQLE MPIDANGILQ RWVTDEPSER GIEGMERMRL
     VRDDIDARVQ NLVAELTQNA