ID   MRX1_CORGL              Reviewed;          79 AA.
AC   P0DKS9; Q6M6U4; Q8NS40;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Mycoredoxin 1;
DE            EC=1.20.4.3;
GN   Name=mrx1; OrderedLocusNames=cg0964, Cgl0842;
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   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-12 AND CYS-15.
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; functions as a monothiol mixed disulfide reductase and is
CC       recycled by a second mycothiol forming mycothione which in turn is
CC       reduced in a NADPH-dependent manner. {ECO:0000269|PubMed:19286650}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[mycoredoxin]-L-cysteine + arseno-mycothiol + H(+) =
CC         [mycoredoxin]-S-mycothiol-L-cysteine + arsenite;
CC         Xref=Rhea:RHEA:54036, Rhea:RHEA-COMP:13766, Rhea:RHEA-COMP:13767,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29242, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:59655, ChEBI:CHEBI:138035; EC=1.20.4.3;
CC         Evidence={ECO:0000269|PubMed:19286650};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR   EMBL; BA000036; BAB98235.1; -; Genomic_DNA.
DR   EMBL; BX927150; CAF19548.1; -; Genomic_DNA.
DR   RefSeq; NP_600071.1; NC_003450.3.
DR   RefSeq; WP_011013923.1; NC_006958.1.
DR   AlphaFoldDB; P0DKS9; -.
DR   SMR; P0DKS9; -.
DR   STRING; 196627.cg0964; -.
DR   KEGG; cgb:cg0964; -.
DR   KEGG; cgl:Cgl0842; -.
DR   PATRIC; fig|196627.13.peg.826; -.
DR   eggNOG; COG0695; Bacteria.
DR   HOGENOM; CLU_026126_11_1_11; -.
DR   OMA; EGIAYTE; -.
DR   BioCyc; MetaCyc:G18NG-10412-MON; -.
DR   Proteomes; UP000000582; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW.
DR   InterPro; IPR011915; GlrX_actino.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR02200; GlrX_actino; 1.
PE   1: Evidence at protein level;
KW   Arsenical resistance; Cytoplasm; Oxidoreductase; Reference proteome.
FT   CHAIN           1..79
FT                   /note="Mycoredoxin 1"
FT                   /id="PRO_0000418726"
FT   DOMAIN          1..79
FT                   /note="Glutaredoxin"
FT   MUTAGEN         12
FT                   /note="C->A: Abolishes activity."
FT                   /evidence="ECO:0000269|PubMed:19286650"
FT   MUTAGEN         15
FT                   /note="C->A: No effect on activity."
FT                   /evidence="ECO:0000269|PubMed:19286650"
SQ   SEQUENCE   79 AA;  8717 MW;  DC60300C420A629E CRC64;
     MSNVTIYATD WCPYCRSLLK GLDGQEYDLI DVDQDEEAGE WVKSVNDGNR IVPTVRYSDG
     THATNPLAAE VIAKIEALA