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Entry version 119 (02 Jun 2021)
Sequence version 1 (15 Feb 2005)
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Protein

Arsenate reductase

Gene

arsC

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei10NucleophileUniRule annotation2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi13Potassium5 Publications1
Metal bindingi36Potassium5 Publications1
Metal bindingi63Potassium5 Publications1
Metal bindingi65Potassium5 Publications1
Active sitei82NucleophileUniRule annotation2 Publications1
Active sitei89NucleophileUniRule annotation2 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processArsenical resistance
LigandMetal-binding, Potassium

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-10862

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.20.4.1, 3352
1.20.4.4, 3352

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P0A006

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Arsenate reductase1 PublicationUniRule annotation (EC:1.20.4.47 Publications)
Alternative name(s):
Arsenical pump modifier
Protein ArsC
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:arsC1 PublicationUniRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates if the gene coding for the protein originates from the hydrogenosome, the mitochondrion, the nucleomorph, different plastids or a plasmid. The absence of this section means that the gene is located in one of the main chromosomal element(s).<p><a href='/help/encoded_on' target='_top'>More...</a></p>Encoded oniPlasmid pI2587 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiStaphylococcus aureus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1280 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4523173

Drug and drug target database

More...
DrugBanki
DB02763, 5-Mercapto-2-Nitro-Benzoic Acid
DB03138, Perchlorate
DB03352, S-Arsonocysteine

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001625231 – 131Arsenate reductaseAdd BLAST131

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi10 ↔ 82Redox-active; alternateUniRule annotationCombined sources2 Publications
Disulfide bondi82 ↔ 89Redox-active; alternateUniRule annotationCombined sources3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1131
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
P0A006

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0A006

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0A006

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>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

HAMAP database of protein families

More...
HAMAPi
MF_01624, Arsenate_reduct, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR014064, Arsenate_reductase_ArsC
IPR023485, Ptyr_pPase
IPR036196, Ptyr_pPase_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01451, LMWPc, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00226, LMWPc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52788, SSF52788, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02691, arsC_pI258_fam, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i03871148DC433A18
GO

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 14810.5 Da. Determined by ESI. 1 Publication
Molecular mass is 14812 Da. Determined by ESI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
PIRi
A53641
D41903

NCBI Reference Sequences

More...
RefSeqi
WP_000163242.1, NZ_WKIT01000072.1
WP_000358995.1, NZ_WWCF01000102.1
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

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
59698368

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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_000163242.1, NZ_WKIT01000072.1
WP_000358995.1, NZ_WWCF01000102.1
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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]
BMRBiP0A006
SMRiP0A006
ModBaseiSearch...
PDBe-KBiSearch...

Chemistry databases

ChEMBLiCHEMBL4523173
DrugBankiDB02763, 5-Mercapto-2-Nitro-Benzoic Acid
DB03138, Perchlorate
DB03352, S-Arsonocysteine

Genome annotation databases

GeneIDi59698368

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-10862
BRENDAi1.20.4.1, 3352
1.20.4.4, 3352
SABIO-RKiP0A006

Miscellaneous databases

EvolutionaryTraceiP0A006

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

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiARSC_STAAU
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A006
Secondary accession number(s): P30330
, Q6Y0M0, Q6Y0M4, Q6Y0N2, Q8GQH3
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: February 15, 2005
Last modified: June 2, 2021
This is version 119 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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
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