ID   ARSC_NEIMB              Reviewed;         117 AA.
AC   P63622; Q9JQU0;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Arsenate reductase;
DE            EC=1.20.4.1 {ECO:0000250|UniProtKB:P08692};
GN   Name=arsC; OrderedLocusNames=NMB0005;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(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; AE002098; AAF40484.1; -; Genomic_DNA.
DR   PIR; C81247; C81247.
DR   RefSeq; NP_273071.1; NC_003112.2.
DR   RefSeq; WP_002225750.1; NC_003112.2.
DR   AlphaFoldDB; P63622; -.
DR   SMR; P63622; -.
DR   STRING; 122586.NMB0005; -.
DR   PaxDb; P63622; -.
DR   EnsemblBacteria; AAF40484; AAF40484; NMB0005.
DR   KEGG; nme:NMB0005; -.
DR   PATRIC; fig|122586.8.peg.5; -.
DR   HOGENOM; CLU_116644_0_1_4; -.
DR   OMA; MVTHPKL; -.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..117
FT                   /note="Arsenate reductase"
FT                   /id="PRO_0000162542"
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