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Protein

Protein ArsC

Gene

arsC

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

Functioni

Reduces arsenate [As(V)] to arsenite [As(III)] and dephosphorylates tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Could switch between different functions in different circumstances.6 Publications

Miscellaneous

Cys-10 is essential for both reductase and phosphatase reactions.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.2 Publications
Arsenate + thioredoxin = arsenite + thioredoxin disulfide + H2O.6 Publications

Enzyme regulationi

Inhibited by arsenite (mixed inhibitor).

Kineticsi

Arsenate is the physiological substrate. Kcat is 0.53 min(-1) for the phosphatase activity with para-nitrophenyl phosphate as substrate.1 Publication
  1. KM=146 mM for para-nitrophenyl phosphate (reduced form only)5 Publications
  2. KM=68 µM for arsenate5 Publications
  3. KM=0.8 µM for arsenate (below 1 mM arsenate)5 Publications
  4. KM=2 mM for arsenate (above 1 mM arsenate)5 Publications
  5. KM=13 mM for selenate5 Publications
  1. Vmax=200 nmol/min/mg enzyme (below 1 mM arsenate)5 Publications
  2. Vmax=450 nmol/min/mg enzyme (above 1 mM arsenate)5 Publications

pH dependencei

Optimum pH is 8.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei10Nucleophile; for reductase activity and phosphatase activity2 Publications1
Active sitei82Nucleophile; for reductase activity2 Publications1
Active sitei89Nucleophile; for reductase activity2 Publications1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Oxidoreductase
Biological processArsenical resistance

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:
Protein ArsC
Alternative name(s):
Arsenate reductase (EC:1.20.4.-6 Publications)
Arsenical pump modifier
Low molecular weight protein-tyrosine-phosphatase (EC:3.1.3.482 Publications)
Gene namesi
Name:arsC
Encoded oniPlasmid pI2587 Publications
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi10C → S: Loss of reductase and phosphatase activities. Loss of reductase and phosphatase activities; when associated with A-15. 2 Publications1
Mutagenesisi15C → A: Decrease in substrate affinity of reductase. Substrate affinity of phosphatase identical to wild-type. Loss of reductase and phosphatase activities; when associated with S-10. 2 Publications1
Mutagenesisi16R → K: Loss of reductase activity. 1 Publication1
Mutagenesisi17S → A: 5-fold decrease in catalytic efficiency. 1 Publication1
Mutagenesisi82C → S: Loss of reductase activity. Increase in substrate affinity of phosphatase. 1 Publication1
Mutagenesisi89C → A: Loss of reductase activity. 2 Publications1
Mutagenesisi89C → L: Decrease in substrate affinity of phosphatase. Leads to a reductase locked in the C-10/C-82 intermediate form. 2 Publications1
Mutagenesisi105D → A: 55-fold decrease in substrate affinity of reductase. 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 – 131Protein ArsCAdd BLAST131

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi10 ↔ 82Redox-active; alternate2 Publications
Disulfide bondi82 ↔ 89Redox-active; alternate2 Publications

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond

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

Keywords - Domaini

Redox-active center

Family and domain databases

CDDicd00115. LMWPc. 1 hit.
HAMAPiMF_01624. Arsenate_reduct. 1 hit.
InterProiView protein in InterPro
IPR014064. Arsenate_reductase_ArsC.
IPR023485. 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_NAJD01000043.1.
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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

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: July 5, 2017
This is version 92 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