ARSC2_CORGL
ID ARSC2_CORGL Reviewed; 129 AA.
AC P0DKS7; Q6M898; Q8NTP3;
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 ArsC2;
DE EC=2.8.4.2;
DE AltName: Full=Mycothiol-dependent arsenate reductase ArsC2;
GN Name=arsC2; Synonyms=arsX; OrderedLocusNames=cg0319, Cgl0263;
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS).
RX PubMed=22032722; DOI=10.1111/j.1365-2958.2011.07882.x;
RA Villadangos A.F., Van Belle K., Wahni K., Dufe V.T., Freitas S., Nur H.,
RA De Galan S., Gil J.A., Collet J.F., Mateos L.M., Messens J.;
RT "Corynebacterium glutamicum survives arsenic stress with arsenate
RT reductases coupled to two distinct redox mechanisms.";
RL Mol. Microbiol. 82:998-1014(2011).
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=142 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; BAB97656.1; -; Genomic_DNA.
DR EMBL; BX927148; CAF18834.1; -; Genomic_DNA.
DR RefSeq; NP_599516.1; NC_003450.3.
DR RefSeq; WP_003863342.1; NC_006958.1.
DR PDB; 3RH0; X-ray; 1.72 A; A/B=1-129.
DR PDBsum; 3RH0; -.
DR AlphaFoldDB; P0DKS7; -.
DR SMR; P0DKS7; -.
DR STRING; 196627.cg0319; -.
DR PRIDE; P0DKS7; -.
DR KEGG; cgb:cg0319; -.
DR KEGG; cgl:Cgl0263; -.
DR PATRIC; fig|196627.13.peg.267; -.
DR eggNOG; COG0394; Bacteria.
DR HOGENOM; CLU_071415_3_3_11; -.
DR OMA; FMCVRNA; -.
DR BRENDA; 2.8.4.2; 960.
DR SABIO-RK; P0DKS7; -.
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 3D-structure; Arsenical resistance; Cytoplasm; Reference proteome;
KW Transferase.
FT CHAIN 1..129
FT /note="Arsenate-mycothiol transferase ArsC2"
FT /id="PRO_0000418725"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:3RH0"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:3RH0"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:3RH0"
FT HELIX 45..53
FT /evidence="ECO:0007829|PDB:3RH0"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:3RH0"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:3RH0"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:3RH0"
FT HELIX 108..127
FT /evidence="ECO:0007829|PDB:3RH0"
SQ SEQUENCE 129 AA; 13763 MW; 9279EF21FF0E52B8 CRC64;
MKSVLFVCVG NGGKSQMAAA LAQKYASDSV EIHSAGTKPA QGLNQLSVES IAEVGADMSQ
GIPKAIDPEL LRTVDRVVIL GDDAQVDMPE SAQGALERWS IEEPDAQGME RMRIVRDQID
NRVQALLAG
