ID   ARSI1_SYNY3             Reviewed;         144 AA.
AC   Q6ZEM6;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Arsenate reductase ArsI1;
DE            EC=1.20.4.1 {ECO:0000269|PubMed:19304854};
GN   Name=arsI1 {ECO:0000303|PubMed:19304854}; OrderedLocusNames=sll5104;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OG   Plasmid pSYSM.
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa; PLASMID=pSYSM;
RX   PubMed=14686584; DOI=10.1093/dnares/10.5.221;
RA   Kaneko T., Nakamura Y., Sasamoto S., Watanabe A., Kohara M., Matsumoto M.,
RA   Shimpo S., Yamada M., Tabata S.;
RT   "Structural analysis of four large plasmids harboring in a unicellular
RT   cyanobacterium, Synechocystis sp. PCC 6803.";
RL   DNA Res. 10:221-228(2003).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=19304854; DOI=10.1128/jb.01798-08;
RA   Lopez-Maury L., Sanchez-Riego A.M., Reyes J.C., Florencio F.J.;
RT   "The glutathione/glutaredoxin system is essential for arsenate reduction in
RT   Synechocystis sp. strain PCC 6803.";
RL   J. Bacteriol. 191:3534-3543(2009).
CC   -!- FUNCTION: Catalyzes the reduction of arsenate [As(V)] to arsenite
CC       [As(III)]. Does not constitute the major arsenate reductase in cells:
CC       essential only in the absence of ArsC (AC P74313).
CC       {ECO:0000269|PubMed:19304854}.
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:0000269|PubMed:19304854};
CC   -!- SIMILARITY: Belongs to the ArsC family. {ECO:0000305}.
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DR   EMBL; AP004310; BAD01874.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6ZEM6; -.
DR   SMR; Q6ZEM6; -.
DR   EnsemblBacteria; BAD01874; BAD01874; BAD01874.
DR   KEGG; syn:sll5104; -.
DR   InParanoid; Q6ZEM6; -.
DR   OMA; MQRPIVT; -.
DR   PhylomeDB; Q6ZEM6; -.
DR   Proteomes; UP000001425; Plasmid pSYSM.
DR   GO; GO:0008794; F:arsenate reductase (glutaredoxin) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046685; P:response to arsenic-containing substance; IBA:GO_Central.
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   PROSITE; PS51353; ARSC; 1.
PE   1: Evidence at protein level;
KW   Oxidoreductase; Plasmid; Reference proteome.
FT   CHAIN           1..144
FT                   /note="Arsenate reductase ArsI1"
FT                   /id="PRO_0000429128"
FT   ACT_SITE        14
FT                   /note="Nucleophile; cysteine thioarsenate intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P08692,
FT                   ECO:0000255|PROSITE-ProRule:PRU01282"
FT   SITE            10
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250|UniProtKB:P08692"
FT   SITE            62
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250|UniProtKB:P08692"
FT   SITE            96
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250|UniProtKB:P08692"
FT   SITE            109
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250|UniProtKB:P08692"
SQ   SEQUENCE   144 AA;  16033 MW;  A3003659452CDFBE CRC64;
     MTENMIVIYH NPDCGTSRNV LQLIEAAGYL PQVIEYVKEG WTKPQLLGLF AAADLTPRSA
     LRTTKSPAAE LNLLEETVTD AQILDAMVEY PILVNRPIVC TPKGVRLCRP SEVVLDLLDH
     WPSGPFAKED GELIIDERGN RVYT