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Protein

Arsenate reductase

Gene

arsC

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)] (PubMed:1409657, PubMed:8003493, PubMed:10606519, PubMed:11862551, PubMed:12072565, PubMed:12682056, PubMed:16797027). In vitro, has also low phosphatase activity with para-nitrophenyl phosphate (pNPP) as substrate (PubMed:11573087).8 Publications

Catalytic activityi

Arsenate + thioredoxin = arsenite + thioredoxin disulfide + H2O.UniRule annotation7 Publications

Enzyme regulationi

Potassium binding stabilizes the enzyme and increases its specific activity (PubMed:12682056, PubMed:16797027). Activity is also stimulated by sulfate (PubMed:16797027). Inhibited by arsenite (mixed inhibitor) (PubMed:11862551).3 Publications

Kineticsi

kcat is 4.5 min(-1) with arsenate as substrate (at 2 µM arsenate) and kcat is 9.9 min(-1) with arsenate as substrate (at 10 mM arsenate) (PubMed:10606519). kcat is 54 min(-1) in the presence of KCl (PubMed:12682056, PubMed:16797027). kcat is 35 min(-1) in the presence of NaCl (PubMed:12682056, PubMed:16797027). kcat is 172 min(-1) in the presence of Na2SO4 (PubMed:16797027). kcat is 219 min(-1) in the presence of K2SO4 (PubMed:16797027). kcat is 0.53 min(-1) for the phosphatase activity with para-nitrophenyl phosphate as substrate (PubMed:11573087).4 Publications
  1. KM=0.8 µM for arsenate (below 1 mM arsenate)1 Publication
  2. KM=2 mM for arsenate (above 1 mM arsenate)1 Publication
  3. KM=0.066 µM for arsenate1 Publication
  4. KM=68 µM for arsenate1 Publication
  5. KM=9 µM for arsenate (in the presence of KCl)2 Publications
  6. KM=22 µM for arsenate (in the presence of NaCl)2 Publications
  7. KM=61 µM for arsenate (in the presence of Na2SO4)1 Publication
  8. KM=81 µM for arsenate (in the presence of K2SO4)1 Publication
  9. KM=146 mM for para-nitrophenyl phosphate (reduced form only)1 Publication
  1. Vmax=200 nmol/min/mg enzyme (below 1 mM arsenate)1 Publication
  2. Vmax=450 nmol/min/mg enzyme (above 1 mM arsenate)1 Publication

pH dependencei

Optimum pH is 8.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei10NucleophileUniRule annotation2 Publications1
Metal bindingi13Potassium5 Publications1
Metal bindingi36Potassium5 Publications1
Metal bindingi63Potassium5 Publications1
Metal bindingi65Potassium5 Publications1
Active sitei82NucleophileUniRule annotation2 Publications1
Active sitei89NucleophileUniRule annotation2 Publications1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processArsenical resistance
LigandMetal-binding, Potassium

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-10862.
BRENDAi1.20.4.1. 3352.
1.20.4.B2. 3352.
SABIO-RKiP0A006.

Names & Taxonomyi

Protein namesi
Recommended name:
Arsenate reductase1 PublicationUniRule annotation (EC:1.20.4.47 Publications)
Alternative name(s):
Arsenical pump modifier
Protein ArsC
Gene namesi
Name:arsC1 PublicationUniRule annotation
Encoded oniPlasmid pI2587 Publications
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Subcellular locationi

  • Cytoplasm UniRule annotation1 Publication

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Deletion of the gene leads to a complete loss of arsenate resistance, but does not affect arsenite or antimony resistance.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi10C → A: Loss of activity. 1 Publication1
Mutagenesisi10C → S: Loss of activity; when associated with A-15. 2 Publications1
Mutagenesisi13N → A: Loss of K(+) stabilization over Na(+). 1 Publication1
Mutagenesisi15C → A: 2-fold decrease in affinity for arsenate. Does not affect affinity for pNPP. Loss of activity; when associated with S-10. 2 Publications1
Mutagenesisi16R → K: Loss of activity. 1 Publication1
Mutagenesisi17S → A: 5-fold decrease in catalytic efficiency. 1 Publication1
Mutagenesisi21E → A: Decreases the thermal stabilization effect of K(+). 1 Publication1
Mutagenesisi36S → A: Strong impact on thermal stabilization. 1 Publication1
Mutagenesisi62H → Q: Uncouples the sulfate effect from the potassium effect on the kinetics. 1 Publication1
Mutagenesisi65D → A: Loss of K(+) stabilization over Na(+). 1 Publication1
Mutagenesisi82C → S: Loss of activity. 1 Publication1
Mutagenesisi89C → A: Loss of activity. 1 Publication1
Mutagenesisi89C → L: Leads to a reductase locked in the C-10/C-82 intermediate form. Decrease in affinity for pNPP. 2 Publications1
Mutagenesisi105D → A: 4-fold decrease in catalytic efficiency. 1 Publication1

Chemistry databases

DrugBankiDB02763. 5-Mercapto-2-Nitro-Benzoic Acid.
DB03138. Perchlorate Ion.
DB03352. S-Arsonocysteine.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001625231 – 131Arsenate reductaseAdd BLAST131

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi10 ↔ 82Redox-active; alternateUniRule annotationCombined sources2 Publications
Disulfide bondi82 ↔ 89Redox-active; alternateUniRule annotationCombined sources3 Publications

Post-translational modificationi

Cys-89 performs a nucleophilic attack on a Cys-10-Cys-82 intermediate, forming another disulfide intermediate with Cys-82.2 Publications

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

Induced by arsenate [As(V)], arsenite [As(III)], and antimonite [Sb(III)].1 Publication

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1131
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 15Combined sources12
Helixi16 – 27Combined sources12
Turni29 – 31Combined sources3
Beta strandi32 – 40Combined sources9
Helixi46 – 54Combined sources9
Helixi69 – 74Combined sources6
Beta strandi76 – 80Combined sources5
Helixi83 – 88Combined sources6
Beta strandi96 – 100Combined sources5
Helixi111 – 129Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JF8X-ray1.12A1-131[»]
1JFVX-ray2.00A1-131[»]
1LJLX-ray2.01A1-131[»]
1LJUX-ray1.40A1-131[»]
1LK0X-ray1.60A/B1-131[»]
1RXEX-ray1.70A1-131[»]
1RXIX-ray1.50A1-131[»]
2CD7X-ray1.50A1-131[»]
2FXIX-ray1.80A1-131[»]
ProteinModelPortaliP0A006.
SMRiP0A006.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A006.

Family & Domainsi

Sequence similaritiesi

Belongs to the low molecular weight phosphotyrosine protein phosphatase family. Thioredoxin-coupled ArsC subfamily.UniRule annotationCurated

Keywords - Domaini

Redox-active center

Family and domain databases

HAMAPiMF_01624. Arsenate_reduct. 1 hit.
InterProiView protein in InterPro
IPR014064. Arsenate_reductase_ArsC.
IPR023485. Ptyr_pPase.
IPR036196. Ptyr_pPase_sf.
PfamiView protein in Pfam
PF01451. LMWPc. 1 hit.
SMARTiView protein in SMART
SM00226. LMWPc. 1 hit.
SUPFAMiSSF52788. SSF52788. 1 hit.
TIGRFAMsiTIGR02691. arsC_pI258_fam. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A006-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKKTIYFIC TGNSCRSQMA EGWGKEILGE GWNVYSAGIE THGVNPKAIE
60 70 80 90 100
AMKEVDIDIS NHTSDLIDND ILKQSDLVVT LCSDADNNCP ILPPNVKKEH
110 120 130
WGFDDPAGKE WSEFQRVRDE IKLAIEKFKL R
Length:131
Mass (Da):14,813
Last modified:February 15, 2005 - v1
Checksum:i03871148DC433A18
GO

Mass spectrometryi

Molecular mass is 14810.5 Da from positions 1 - 131. Determined by ESI. 1 Publication
Molecular mass is 14812 Da from positions 1 - 131. Determined by ESI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti2D → T in strain: SW18, SW4, SW24 and SW1. 1
Natural varianti24 – 33GKEILGEGWN → AKQILAKDWD in strain: SW18. 10
Natural varianti24 – 31GKEILGEG → AKQILADD in strain: SW24 and SW1. 8
Natural varianti24 – 31GKEILGEG → AKQILAED in strain: SW4. 8
Natural varianti56D → G in strain: SW18, SW4, SW24 and SW1. 1
Natural varianti65D → N in strain: SW24 and SW1. 1
Natural varianti70 – 76DILKQSD → NIIKNSN in strain: SW18, SW4, SW24 and SW1. 7
Natural varianti87N → V in strain: SW18, SW4, SW24 and SW1. 1
Natural varianti91I → S in strain: SW4, SW24 and SW1. 1
Natural varianti91I → T in strain: SW18. 1
Natural varianti94P → T in strain: SW18, SW4, SW24 and SW1. 1
Natural varianti110E → P in strain: SW18, SW4, SW24 and SW1. 1
Natural varianti123L → I in strain: SW4, SW24 and SW1. 1
Natural varianti123L → V in strain: SW18. 1
Natural varianti127K → N in strain: SW18, SW4, SW24 and SW1. 1
Natural varianti130L → S in strain: SW18, SW4, SW24 and SW1. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86824 Genomic DNA. Translation: AAA25638.1.
AY194061 Genomic DNA. Translation: AAP32334.1.
AY194062 Genomic DNA. Translation: AAP32338.1.
AY194064 Genomic DNA. Translation: AAP32346.1.
AY194065 Genomic DNA. Translation: AAP32350.1.
PIRiA53641.
D41903.
RefSeqiWP_000163242.1. NZ_NAJH01000080.1.
WP_000358995.1. NZ_NMZF01000026.1.
YP_001573918.1. NC_010077.1.
YP_001715971.1. NC_010419.1.
YP_006937217.1. NC_013292.1.
YP_006937607.1. NC_013319.1.
YP_006937727.1. NC_013322.1.
YP_006937753.1. NC_013323.1.
YP_006938161.1. NC_013333.1.
YP_006938435.1. NC_013340.1.
YP_006938641.1. NC_013347.1.
YP_006938712.1. NC_013349.1.
YP_006938775.1. NC_013352.1.
YP_006939395.1. NC_018965.1.
YP_006940871.1. NC_019009.1.
YP_536862.1. NC_007931.1.

Genome annotation databases

GeneIDi13874340.
13874755.
13874878.
13874905.
13875324.
13875605.
13875818.
13875891.
13875956.
13876308.
13877846.
3978621.
5759819.
6155824.

Similar proteinsi

Entry informationi

Entry nameiARSC_STAAU
AccessioniPrimary (citable) accession number: P0A006
Secondary accession number(s): P30330
, Q6Y0M0, Q6Y0M4, Q6Y0N2, Q8GQH3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: February 15, 2005
Last modified: November 22, 2017
This is version 96 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families