ID   A0A5P8RRJ8_YERPE        Unreviewed;       118 AA.
AC   A0A5P8RRJ8;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   03-AUG-2022, entry version 4.
DE   RecName: Full=Arsenate reductase {ECO:0000256|RuleBase:RU362029};
DE            EC=1.20.4.1 {ECO:0000256|RuleBase:RU362029};
GN   Name=arsC {ECO:0000313|EMBL:QFR84653.1};
GN   ORFNames=DJY80_06915 {ECO:0000313|EMBL:QFR84653.1};
OS   Yersinia pestis subsp. pestis bv. Medievalis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=1234662 {ECO:0000313|EMBL:QFR84653.1, ECO:0000313|Proteomes:UP000326807};
RN   [1] {ECO:0000313|EMBL:QFR84653.1, ECO:0000313|Proteomes:UP000326807}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCPM-O-B-6530 {ECO:0000313|EMBL:QFR84653.1,
RC   ECO:0000313|Proteomes:UP000326807};
RA   Bogun A., Kislichkina A., Mayskaya N., Platonov M., Sizova A., Skryabin Y.,
RA   Solomentsev V., Ivanov S., Shaikhutdinova R., Dentovskaya S., Anisimov A.;
RL   Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[glutaredoxin]-dithiol + arsenate + glutathione + H(+) =
CC         arsenite + glutathionyl-S-S-[glutaredoxin] + H2O;
CC         Xref=Rhea:RHEA:22016, Rhea:RHEA-COMP:10729, Rhea:RHEA-COMP:17668,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29242,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:48597, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:146199; EC=1.20.4.1;
CC         Evidence={ECO:0000256|RuleBase:RU362029};
CC   -!- SIMILARITY: Belongs to the ArsC family. {ECO:0000256|ARBA:ARBA00007198,
CC       ECO:0000256|PROSITE-ProRule:PRU01282, ECO:0000256|RuleBase:RU362029}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP045158; QFR84653.1; -; Genomic_DNA.
DR   RefSeq; WP_002208565.1; NZ_CP045158.1.
DR   SMR; A0A5P8RRJ8; -.
DR   GeneID; 66844785; -.
DR   Proteomes; UP000326807; Chromosome.
DR   GO; GO:0008794; F:arsenate reductase (glutaredoxin) activity; IEA:UniProtKB-UniRule.
DR   CDD; cd03034; ArsC_ArsC; 1.
DR   InterPro; IPR006659; Arsenate_reductase.
DR   InterPro; IPR006660; Arsenate_reductase-like.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR30041; PTHR30041; 1.
DR   Pfam; PF03960; ArsC; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR00014; arsC; 1.
DR   PROSITE; PS51353; ARSC; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362029,
KW   ECO:0000313|EMBL:QFR84653.1}.
SQ   SEQUENCE   118 AA;  13481 MW;  881FF5331AA4F57C CRC64;
     MKDVTIYHNP RCSKSRETLA LVEQQGITPQ VVLYLETPPS VDKLKELLQQ LGFSDARQLM
     RTKEDLYKTL NLDDRGLTQD QLLQAMADNP KLIERPIVVT QGKARIGRPP EQVLEILK
//