ID   ARSC_NEIGO              Reviewed;         102 AA.
AC   P95354;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Putative arsenate reductase;
DE            EC=1.20.4.1 {ECO:0000250|UniProtKB:P08692};
GN   Name=arsC;
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CH811;
RX   PubMed=10819322; DOI=10.1093/dnares/7.2.75;
RA   Bernatchez S., Francis F.M., Salimnia H., Beveridge T.J., Li H.,
RA   Dillon J.-A.R.;
RT   "Genomic, transcriptional and phenotypic analysis of ftsE and ftsX of
RT   Neisseria gonorrhoeae.";
RL   DNA Res. 7:75-81(2000).
CC   -!- FUNCTION: Involved in resistance to arsenate. Catalyzes the reduction
CC       of arsenate [As(V)] to arsenite [As(III)].
CC       {ECO:0000250|UniProtKB:P08692}.
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:0000250|UniProtKB:P08692};
CC   -!- SIMILARITY: Belongs to the ArsC family. {ECO:0000305}.
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DR   EMBL; U76418; AAB36522.1; -; Genomic_DNA.
DR   AlphaFoldDB; P95354; -.
DR   SMR; P95354; -.
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   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   Arsenical resistance; Oxidoreductase.
FT   CHAIN           1..102
FT                   /note="Putative arsenate reductase"
FT                   /id="PRO_0000162540"
FT   ACT_SITE        12
FT                   /note="Nucleophile; cysteine thioarsenate intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P08692,
FT                   ECO:0000255|PROSITE-ProRule:PRU01282"
FT   SITE            8
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250|UniProtKB:P08692"
FT   SITE            61
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250|UniProtKB:P08692"
FT   SITE            95
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250|UniProtKB:P08692"
SQ   SEQUENCE   102 AA;  11413 MW;  E015371DA3FCED71 CRC64;
     MSEIKIFHNP RCSKSRAAVS LLEERGIAAE AVKYLDTPPD LSELKDIFNK LGLESARGMM
     RVKDDLYKEL GLDNPDLDND ALLRAIADHP ALLERPIVLG KR