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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

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

Manual assertion based on experiment ini

  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

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Oxidoreductase

Keywords - Biological processi

Arsenical resistance

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-10862.
BRENDAi1.20.4.1. 3352.
1.20.4.B2. 3352.
SABIO-RKP0A006.

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

Complete GO annotation...

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

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.
InterProiIPR014064. Arsenate_reductase_ArsC.
IPR023485. Ptyr_pPase_SF.
[Graphical view]
PfamiPF01451. LMWPc. 1 hit.
[Graphical view]
SMARTiSM00226. LMWPc. 1 hit.
[Graphical view]
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_000163236.1. NZ_LJBL01000027.1.
WP_000163239.1. NZ_LSBE01000012.1.
WP_000163242.1. NZ_JXZW01000001.1.
WP_000358995.1. NZ_MCFM01000022.1.
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.
28381728.
3978621.
5759819.
6155824.

Cross-referencesi

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_000163236.1. NZ_LJBL01000027.1.
WP_000163239.1. NZ_LSBE01000012.1.
WP_000163242.1. NZ_JXZW01000001.1.
WP_000358995.1. NZ_MCFM01000022.1.
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.

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...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi13874340.
13874755.
13874878.
13874905.
13875324.
13875605.
13875818.
13875891.
13875956.
13876308.
13877846.
28381728.
3978621.
5759819.
6155824.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-10862.
BRENDAi1.20.4.1. 3352.
1.20.4.B2. 3352.
SABIO-RKP0A006.

Miscellaneous databases

EvolutionaryTraceiP0A006.

Family and domain databases

CDDicd00115. LMWPc. 1 hit.
HAMAPiMF_01624. Arsenate_reduct. 1 hit.
InterProiIPR014064. Arsenate_reductase_ArsC.
IPR023485. Ptyr_pPase_SF.
[Graphical view]
PfamiPF01451. LMWPc. 1 hit.
[Graphical view]
SMARTiSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMiSSF52788. SSF52788. 1 hit.
TIGRFAMsiTIGR02691. arsC_pI258_fam. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiARSC_STAAU
AccessioniPrimary (citable) accession number: P0A006
Secondary accession number(s): P30330
, Q6Y0M0, Q6Y0M4, Q6Y0N2, Q8GQH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: February 15, 2005
Last modified: November 30, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

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

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.