ID   MRX1_CORGK              Reviewed;          79 AA.
AC   P0DKT0; Q6M6U4; Q8NS40;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Mycoredoxin 1;
DE            EC=1.20.4.3;
GN   Name=mrx1; OrderedLocusNames=WA5_0808;
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; 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 (By similarity). {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR   EMBL; HE802067; CCH24028.1; -; Genomic_DNA.
DR   RefSeq; WP_011013923.1; NC_020519.1.
DR   AlphaFoldDB; P0DKT0; -.
DR   SMR; P0DKT0; -.
DR   KEGG; cgu:WA5_0808; -.
DR   PATRIC; fig|1204414.5.peg.868; -.
DR   HOGENOM; CLU_026126_11_1_11; -.
DR   OMA; EGIAYTE; -.
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   3: Inferred from homology;
KW   Arsenical resistance; Cytoplasm; Oxidoreductase.
FT   CHAIN           1..79
FT                   /note="Mycoredoxin 1"
FT                   /id="PRO_0000420637"
FT   DOMAIN          1..79
FT                   /note="Glutaredoxin"
SQ   SEQUENCE   79 AA;  8717 MW;  DC60300C420A629E CRC64;
     MSNVTIYATD WCPYCRSLLK GLDGQEYDLI DVDQDEEAGE WVKSVNDGNR IVPTVRYSDG
     THATNPLAAE VIAKIEALA