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UniProtKB - P08692 (ARSC1_ECOLX)

Entry version 115 (29 Sep 2021)
Sequence version 1 (01 Jan 1988)
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Protein

Arsenate reductase

Gene

arsC

Organism
Escherichia coli
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

Involved in resistance to arsenate (PubMed:3021763, PubMed:8003492, PubMed:7577935).

Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)] (PubMed:8003492, PubMed:7577935, PubMed:14592722).

The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable).

Curated4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_section">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

Inhibited by the thiol reagents iodoacetate (IAA) and N-ethylmaleimide (NEM) (PubMed:7577935). Activity is rapidly inactivated by the histidine-modifying reagent diethylpyrocarbonate (DEPC) (PubMed:8969183).2 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 0.53 sec(-1) with arsenate as substrate. kcat is 0.218 sec(-1) with Grx2 as substrate.1 Publication
  1. KM=8 mM for arsenate1 Publication
  2. KM=15.2 mM for arsenate1 Publication
  3. KM=32.9 nM for glutaredoxin Grx21 Publication

pH dependencei

Optimum pH is 6.3-6.8.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei8Important for activity. Lowers pKa of the active site Cys1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei12Nucleophile; cysteine thioarsenate intermediatePROSITE-ProRule annotation3 Publications1
Sitei60Important for activity. Involved in arsenate binding and transition-state stabilization3 Publications1
Sitei94Important for activity. Involved in arsenate binding and transition-state stabilization3 Publications1
Sitei107Important for activity. Involved in arsenate binding and transition-state stabilization3 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

<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_and_taxonomy_section">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 Publication (EC:1.20.4.13 Publications)
Alternative name(s):
Arsenical pump modifier
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 R7738 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiEscherichia coli
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri562 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi8H → P, G or R: Loss of reductase activity. Mutant is sensitive to arsenate. 1 Publication1
Mutagenesisi8H → S: Mutant is sensitive to arsenate. 1 Publication1
Mutagenesisi12C → A or G: Mutant is sensitive to arsenate. 1 Publication1
Mutagenesisi12C → S: Loss of reductase activity. Mutant is sensitive to arsenate. 1 Publication1
Mutagenesisi60R → A: 50-fold decrease in catalytic efficiency with arsenate. Mutant is sensitive to arsenate. 1 Publication1
Mutagenesisi60R → E: 70-fold decrease in catalytic efficiency with arsenate. Mutant is sensitive to arsenate. 1 Publication1
Mutagenesisi60R → K: 22-fold decrease in catalytic efficiency with arsenate. Mutant shows low-level resistance to arsenate. 1 Publication1
Mutagenesisi61K → A, E or R: Mutant retains arsenate resistance. 1 Publication1
Mutagenesisi88H → R, S, V or W: No change in reductase activity. Mutant retains arsenate resistance. 1 Publication1
Mutagenesisi94R → A, E or Y: Loss of reductase activity. Mutant is sensitive to arsenate. 1 Publication1
Mutagenesisi94R → K: Loss of reductase activity. Mutant exhibits slight resistance to arsenate. 1 Publication1
Mutagenesisi106C → G or S: Retains reductase activity. Mutant retains arsenate resistance. 1 Publication1
Mutagenesisi106C → V: Mutant retains arsenate resistance. 1 Publication1
Mutagenesisi107R → A, E or Y: Loss of reductase activity. Mutant is sensitive to arsenate. 1 Publication1
Mutagenesisi107R → K: Mutant retains arsenate resistance. 1 Publication1
Mutagenesisi127E → A: 6-fold decrease in catalytic efficiency with arsenate. Mutant is sensitive at high arsenate concentrations. 1 Publication1
Mutagenesisi127E → D: 13-fold decrease in catalytic efficiency with arsenate. Mutant is sensitive at high arsenate concentrations. 1 Publication1
Mutagenesisi127E → K: 17-fold decrease in catalytic efficiency with arsenate. Mutant is sensitive at high arsenate concentrations. 1 Publication1
Mutagenesisi128D → A: 4-fold decrease in catalytic efficiency with arsenate. Mutant is relatively resistant to arsenate, but is more sensitive at higher concentrations. 1 Publication1
Mutagenesisi128D → E: 7-fold decrease in catalytic efficiency with arsenate. Mutant is relatively resistant to arsenate, but is more sensitive at higher concentrations. 1 Publication1
Mutagenesisi128D → K: 9-fold decrease in catalytic efficiency with arsenate. Mutant is relatively resistant to arsenate, but is more sensitive at higher concentrations. 1 Publication1
Mutagenesisi130E → A: 3-fold decrease in catalytic efficiency with arsenate. Mutant is relatively resistant to arsenate, but is more sensitive at higher concentrations. 1 Publication1
Mutagenesisi130E → D: 5-fold decrease in catalytic efficiency with arsenate. Mutant is relatively resistant to arsenate, but is more sensitive at higher concentrations. 1 Publication1
Mutagenesisi130E → K: 5-fold decrease in catalytic efficiency with arsenate. Mutant is relatively resistant to arsenate, but is more sensitive at higher concentrations. 1 Publication1

Chemistry databases

Drug and drug target database

More...DrugBanki		DB04456, Arsenous acid
DB03352, S-Arsonocysteine
DB03289, Thiarsa Dihydroxy Cysteine
DB01808, Thiarsahydroxy-Cysteine

<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_00001625371 – 141Arsenate reductaseAdd BLAST141

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer in solution.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		481805.EcolC_0213

<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

1141
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P08692

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		P08692

<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 ArsC family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG1393, Bacteria

Family and domain databases

Conserved Domains Database

More...CDDi		cd03034, ArsC_ArsC, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR006659, Arsenate_reductase
IPR006660, Arsenate_reductase-like
IPR036249, Thioredoxin-like_sf

The PANTHER Classification System

More...PANTHERi		PTHR30041, PTHR30041, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF03960, ArsC, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52833, SSF52833, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00014, arsC, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51353, ARSC, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P08692-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSNITIYHNP ACGTSRNTLE MIRNSGTEPT IILYLENPPS RDELVKLIAD 
        60         70         80         90        100
MGISVRALLR KNVEPYEQLG LAEDKFTDDQ LIDFMLQHPI LINRPIVVTP 
       110        120        130        140 
LGTRLCRPSE VVLDILQDAQ KGAFTKEDGE KVVDEAGKRL K
Length:141
Mass (Da):15,830
Last modified:January 1, 1988 - 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:i240F4105487E2FBF
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
J02591 Genomic DNA Translation: AAA21096.1

Protein sequence database of the Protein Information Resource

More...PIRi		C25937

NCBI Reference Sequences

More...RefSeqi		WP_011117598.1, NZ_VNXP01000024.1

<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
J02591 Genomic DNA Translation: AAA21096.1
PIRiC25937
RefSeqiWP_011117598.1, NZ_VNXP01000024.1

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
1I9DX-ray1.65A1-141[»]
1J9BX-ray1.26A1-141[»]
1JZWX-ray1.76A1-140[»]
1S3CX-ray1.25A1-141[»]
1S3DX-ray1.54A3-140[»]
1SD8X-ray1.59A1-141[»]
1SD9X-ray1.65A1-141[»]
1SJZX-ray1.80A1-140[»]
1SK0X-ray1.80A1-140[»]
1SK1X-ray1.55A1-140[»]
1SK2X-ray1.54A1-140[»]
SMRiP08692
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi481805.EcolC_0213

Chemistry databases

DrugBankiDB04456, Arsenous acid
DB03352, S-Arsonocysteine
DB03289, Thiarsa Dihydroxy Cysteine
DB01808, Thiarsahydroxy-Cysteine

Phylogenomic databases

eggNOGiCOG1393, Bacteria

Miscellaneous databases

EvolutionaryTraceiP08692

Family and domain databases

CDDicd03034, ArsC_ArsC, 1 hit
InterProiView protein in InterPro
IPR006659, Arsenate_reductase
IPR006660, Arsenate_reductase-like
IPR036249, Thioredoxin-like_sf
PANTHERiPTHR30041, PTHR30041, 1 hit
PfamiView protein in Pfam
PF03960, ArsC, 1 hit
SUPFAMiSSF52833, SSF52833, 1 hit
TIGRFAMsiTIGR00014, arsC, 1 hit
PROSITEiView protein in PROSITE
PS51353, ARSC, 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 nameiARSC1_ECOLX
<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: P08692
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: September 29, 2021
This is version 115 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, Direct protein sequencing, 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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