ARSC_RHIME
ID ARSC_RHIME Reviewed; 140 AA.
AC Q92R44;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Arsenate reductase {ECO:0000303|PubMed:16199569};
DE EC=1.20.4.1 {ECO:0000269|PubMed:16199569};
GN Name=arsC {ECO:0000303|PubMed:16199569};
GN ORFNames=SMc02649 {ECO:0000312|EMBL:CAC45654.1};
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=1021;
RX PubMed=16199569; DOI=10.1128/jb.187.20.6991-6997.2005;
RA Yang H.C., Cheng J., Finan T.M., Rosen B.P., Bhattacharjee H.;
RT "Novel pathway for arsenic detoxification in the legume symbiont
RT Sinorhizobium meliloti.";
RL J. Bacteriol. 187:6991-6997(2005).
CC -!- FUNCTION: Involved in resistance to arsenate. Catalyzes the reduction
CC of arsenate [As(V)] to arsenite [As(III)]. The resulting arsenite is
CC then extruded from the cell via the aquaglyceroporin AqpS. Does not
CC display antimonate reductase activity. {ECO:0000269|PubMed:16199569}.
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:16199569};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25 mM for arsenate {ECO:0000269|PubMed:16199569};
CC Vmax=100 nmol/min/mg enzyme {ECO:0000269|PubMed:16199569};
CC -!- DISRUPTION PHENOTYPE: Disruption mutant shows selective sensitivity to
CC arsenate. Does not affect sensitivity to antimonate [Sb(V)].
CC {ECO:0000269|PubMed:16199569}.
CC -!- SIMILARITY: Belongs to the ArsC family. {ECO:0000255|PROSITE-
CC ProRule:PRU01282}.
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DR EMBL; AL591688; CAC45654.1; -; Genomic_DNA.
DR RefSeq; NP_385181.1; NC_003047.1.
DR RefSeq; WP_010969024.1; NC_003047.1.
DR AlphaFoldDB; Q92R44; -.
DR SMR; Q92R44; -.
DR STRING; 266834.SMc02649; -.
DR EnsemblBacteria; CAC45654; CAC45654; SMc02649.
DR GeneID; 61602535; -.
DR KEGG; sme:SMc02649; -.
DR PATRIC; fig|266834.11.peg.2481; -.
DR eggNOG; COG1393; Bacteria.
DR HOGENOM; CLU_116644_0_0_5; -.
DR OMA; HYLENPP; -.
DR BioCyc; MetaCyc:MON-21683; -.
DR Proteomes; UP000001976; 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 1: Evidence at protein level;
KW Arsenical resistance; Oxidoreductase; Reference proteome.
FT CHAIN 1..140
FT /note="Arsenate reductase"
FT /id="PRO_0000453040"
FT ACT_SITE 11
FT /note="Nucleophile; cysteine thioarsenate intermediate"
FT /evidence="ECO:0000250|UniProtKB:P08692,
FT ECO:0000255|PROSITE-ProRule:PRU01282"
FT SITE 7
FT /note="Important for activity. Lowers pKa of the active
FT site Cys"
FT /evidence="ECO:0000250|UniProtKB:P08692"
FT SITE 59
FT /note="Important for activity. Involved in arsenate binding
FT and transition-state stabilization"
FT /evidence="ECO:0000250|UniProtKB:P08692"
FT SITE 93
FT /note="Important for activity. Involved in arsenate binding
FT and transition-state stabilization"
FT /evidence="ECO:0000250|UniProtKB:P08692"
FT SITE 106
FT /note="Important for activity. Involved in arsenate binding
FT and transition-state stabilization"
FT /evidence="ECO:0000250|UniProtKB:P08692"
SQ SEQUENCE 140 AA; 15112 MW; 6ED4FF71FC93D79C CRC64;
MTVTIYHNPA CGTSRNTLAM IRNAGIEPTV VEYLKNPPSR AELEAMIAAA GLTVRQAIRE
KGTPFAELGL GDPSRSDEEL LDAMLEHPIL INRPFVVAPL GTRLCRPSEV VLDILPDTHK
GPFSKEDGEA VLDAGGKRIV
