ID   ARSC_NEIMA              Reviewed;         117 AA.
AC   P63621; A1IP98; Q9JQU0;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Arsenate reductase;
DE            EC=1.20.4.1 {ECO:0000250|UniProtKB:P08692};
GN   Name=arsC; OrderedLocusNames=NMA0252;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(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; AL157959; CAM07558.1; -; Genomic_DNA.
DR   RefSeq; WP_002225750.1; NC_003116.1.
DR   AlphaFoldDB; P63621; -.
DR   SMR; P63621; -.
DR   EnsemblBacteria; CAM07558; CAM07558; NMA0252.
DR   KEGG; nma:NMA0252; -.
DR   HOGENOM; CLU_116644_0_1_4; -.
DR   OMA; MVTHPKL; -.
DR   BioCyc; NMEN122587:NMA_RS01310-MON; -.
DR   Proteomes; UP000000626; 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   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..117
FT                   /note="Arsenate reductase"
FT                   /id="PRO_0000162541"
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"
FT   SITE            108
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250|UniProtKB:P08692"
SQ   SEQUENCE   117 AA;  12869 MW;  C834075A7941EBE5 CRC64;
     MPEIKIFHNP RCSKSRAALS LLEERGIAAE VVKYLDTPPD LSELKDIFNK LGLASARGMM
     RVKDDLYKEL GLDNPNLDND ALLRAIADHP ALLERPIVLA NGKAAVGRPL ENIEAVL