ARSC_SYNY3
ID ARSC_SYNY3 Reviewed; 131 AA.
AC P74313;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Glutaredoxin arsenate reductase;
DE EC=1.20.4.1;
DE AltName: Full=Low molecular weight protein-tyrosine-phosphatase;
DE EC=3.1.3.48;
DE AltName: Full=Protein ArsC;
DE Short=SynArsC;
DE Short=rSynArsC;
GN Name=arsC; OrderedLocusNames=slr0946;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
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;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, DISULFIDE BOND, AND
RP MUTAGENESIS OF CYS-8; CYS-13; CYS-80 AND CYS-82.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=14617642; DOI=10.1128/jb.185.23.6780-6789.2003;
RA Li R., Haile J.D., Kennelly P.J.;
RT "An arsenate reductase from Synechocystis sp. strain PCC 6803 exhibits a
RT novel combination of catalytic characteristics.";
RL J. Bacteriol. 185:6780-6789(2003).
RN [3]
RP FUNCTION.
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).
RN [4]
RP FUNCTION, MUTAGENESIS OF CYS-8; CYS-13; CYS-35; CYS-80 AND CYS-82, AND
RP REACTION MECHANISM.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=22155275; DOI=10.1016/j.bbapap.2011.11.012;
RA Kim S.G., Chung J.S., Sutton R.B., Lee J.S., Lopez-Maury L., Lee S.Y.,
RA Florencio F.J., Lin T., Zabet-Moghaddam M., Wood M.J., Nayak K., Madem V.,
RA Tripathy J.N., Kim S.K., Knaff D.B.;
RT "Redox, mutagenic and structural studies of the glutaredoxin/arsenate
RT reductase couple from the cyanobacterium Synechocystis sp. PCC 6803.";
RL Biochim. Biophys. Acta 1824:392-403(2012).
RN [5]
RP STRUCTURE BY NMR, AND DISULFIDE BOND.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=20960080; DOI=10.1007/s12104-010-9273-2;
RA Yu C., Xia B., Jin C.;
RT "1H, 13C and 15N resonance assignments of the arsenate reductase from
RT Synechocystis sp. strain PCC 6803.";
RL Biomol. NMR. Assign. 5:85-87(2011).
CC -!- FUNCTION: Reduces arsenate [As(V)] to arsenite [As(III)] using
CC glutathione and glutaredoxin as sources of reducing equivalents. GrxA
CC is the most effective electron donor in vivo compared to other
CC glutaredoxins. Constitutes the major arsenate reductase compared to
CC ArsI1 and ArsI2. Also shows weak phosphatase activity toward p-
CC nitrophenyl phosphate. {ECO:0000269|PubMed:14617642,
CC ECO:0000269|PubMed:19304854, ECO:0000269|PubMed:22155275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=77 mM for p-nitrophenyl phosphate {ECO:0000269|PubMed:14617642};
CC Vmax=3.1 umol/min/mg enzyme with arsenate as substrate
CC {ECO:0000269|PubMed:14617642};
CC Vmax=0.08 umol/min/mg enzyme with p-nitrophenyl phosphate as
CC substrate {ECO:0000269|PubMed:14617642};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14617642}.
CC -!- MISCELLANEOUS: Cys-8 probably provides the initial functional group for
CC covalent attachment of the electron-accepting substrate, arsenate, to
CC ArsC. {ECO:0000305|PubMed:22155275}.
CC -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC phosphatase family. {ECO:0000305}.
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DR EMBL; BA000022; BAA18407.1; -; Genomic_DNA.
DR PIR; S76148; S76148.
DR PDB; 2L17; NMR; -; A=1-131.
DR PDB; 2L18; NMR; -; A=1-131.
DR PDB; 2L19; NMR; -; A=1-131.
DR PDB; 2MYN; NMR; -; A=1-131.
DR PDB; 2MYP; NMR; -; A=1-131.
DR PDB; 2MYT; NMR; -; A=1-131.
DR PDB; 2MYU; NMR; -; A=1-131.
DR PDBsum; 2L17; -.
DR PDBsum; 2L18; -.
DR PDBsum; 2L19; -.
DR PDBsum; 2MYN; -.
DR PDBsum; 2MYP; -.
DR PDBsum; 2MYT; -.
DR PDBsum; 2MYU; -.
DR AlphaFoldDB; P74313; -.
DR BMRB; P74313; -.
DR SMR; P74313; -.
DR STRING; 1148.1653494; -.
DR PaxDb; P74313; -.
DR EnsemblBacteria; BAA18407; BAA18407; BAA18407.
DR KEGG; syn:slr0946; -.
DR eggNOG; COG0394; Bacteria.
DR InParanoid; P74313; -.
DR OMA; VISLCGC; -.
DR PhylomeDB; P74313; -.
DR BRENDA; 1.20.4.1; 382.
DR EvolutionaryTrace; P74313; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0008794; F:arsenate reductase (glutaredoxin) activity; IEA:UniProtKB-EC.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW.
DR InterPro; IPR014062; Arsenate_reductase_gluta.
DR InterPro; IPR023485; Ptyr_pPase.
DR InterPro; IPR036196; Ptyr_pPase_sf.
DR Pfam; PF01451; LMWPc; 1.
DR SMART; SM00226; LMWPc; 1.
DR SUPFAM; SSF52788; SSF52788; 1.
DR TIGRFAMs; TIGR02689; ars_reduc_gluta; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Arsenical resistance; Disulfide bond; Hydrolase;
KW Oxidoreductase; Redox-active center; Reference proteome.
FT CHAIN 1..131
FT /note="Glutaredoxin arsenate reductase"
FT /id="PRO_0000429130"
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT DISULFID 8..80
FT /note="Redox-active; alternate"
FT /evidence="ECO:0000269|PubMed:20960080"
FT DISULFID 80..82
FT /note="Redox-active; alternate"
FT /evidence="ECO:0000269|PubMed:20960080"
FT MUTAGEN 8
FT /note="C->S: Abolishes arsenate reductase activity."
FT /evidence="ECO:0000269|PubMed:14617642,
FT ECO:0000269|PubMed:22155275"
FT MUTAGEN 13
FT /note="C->S: Little or no effect on arsenate reductase
FT activity. Abolishes protein phosphatase activity."
FT /evidence="ECO:0000269|PubMed:14617642,
FT ECO:0000269|PubMed:22155275"
FT MUTAGEN 35
FT /note="C->A: Little or no effect on arsenate reductase
FT activity."
FT /evidence="ECO:0000269|PubMed:22155275"
FT MUTAGEN 80
FT /note="C->S: Abolishes arsenate reductase activity."
FT /evidence="ECO:0000269|PubMed:14617642,
FT ECO:0000269|PubMed:22155275"
FT MUTAGEN 82
FT /note="C->S: Abolishes arsenate reductase activity."
FT /evidence="ECO:0000269|PubMed:14617642,
FT ECO:0000269|PubMed:22155275"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2L17"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:2L17"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:2L19"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:2L17"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:2MYT"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:2L17"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:2L17"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2L19"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:2L17"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:2L17"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:2L17"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2MYN"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2MYU"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:2L17"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:2L17"
FT HELIX 109..130
FT /evidence="ECO:0007829|PDB:2L17"
SQ SEQUENCE 131 AA; 14443 MW; 7D2013D6910A18B8 CRC64;
MKKVMFVCKR NSCRSQMAEG FAKTLGAGKI AVTSCGLESS RVHPTAIAMM EEVGIDISGQ
TSDPIENFNA DDYDVVISLC GCGVNLPPEW VTQEIFEDWQ LEDPDGQSLE VFRTVRGQVK
ERVENLIAKI S
