ID   ARSCL_ECOLI             Reviewed;         104 AA.
AC   P0CF87; P52136; P76606; P77012;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Putative arsenate reductase;
DE            EC=1.20.4.1;
DE   AltName: Full=Arsenical pump modifier;
GN   Name=yfjU; OrderedLocusNames=JW2619;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
CC   -!- FUNCTION: Reduction of arsenate [As(V)] to arsenite [As(III)]. This
CC       protein expands the substrate specificity of ArsAB pump which can
CC       extrude arsenite and antimonite to allow for arsenate pumping and
CC       resistance (By similarity). {ECO:0000250}.
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   -!- MISCELLANEOUS: Is missing about 40 C-terminal residues compared to
CC       paralogs. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ArsC family. {ECO:0000305}.
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DR   EMBL; U36840; AAA79806.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16506.1; -; Genomic_DNA.
DR   PIR; T08649; T08649.
DR   RefSeq; WP_000065803.1; NZ_LN832404.1.
DR   AlphaFoldDB; P0CF87; -.
DR   SMR; P0CF87; -.
DR   BioGRID; 4260630; 11.
DR   PRIDE; P0CF87; -.
DR   EnsemblBacteria; BAA16506; BAA16506; BAA16506.
DR   KEGG; ecj:JW2619; -.
DR   PRO; PR:P0CF87; -.
DR   Proteomes; UP000000318; Chromosome.
DR   GO; GO:0008794; F:arsenate reductase (glutaredoxin) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW.
DR   InterPro; IPR006660; Arsenate_reductase-like.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR30041; PTHR30041; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51353; ARSC; 1.
PE   3: Inferred from homology;
KW   Arsenical resistance; Oxidoreductase.
FT   CHAIN           1..104
FT                   /note="Putative arsenate reductase"
FT                   /id="PRO_0000394134"
FT   ACT_SITE        12
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01282"
SQ   SEQUENCE   104 AA;  11824 MW;  D4C8B18493C8146B CRC64;
     MSNITIYHNP ACGTSRNTLE MLHNNGNEPT IINYLDMPPT RDELIKLISD IFSDKIIECI
     REQCHLMPAL SLNVIGHVDI RSIHSYLFNF NEKVSPSHGF IKNG