The new UniProt website is here!
Take me to UniProt BETA
UniProtKB - P08692 (ARSC1_ECOLX)
Protein
Arsenate reductase
Gene
arsC
Organism
Escherichia coli
Status
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 PublicationsCatalytic activityi
- [glutaredoxin]-dithiol + arsenate + glutathione + H+ = arsenite + glutathionyl-S-S-[glutaredoxin] + H2O3 PublicationsEC:1.20.4.13 PublicationsThis reaction proceeds in the forward3 Publications direction.
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
Kineticsi
kcat is 0.53 sec(-1) with arsenate as substrate. kcat is 0.218 sec(-1) with Grx2 as substrate.1 Publication
- KM=8 mM for arsenate1 Publication
- KM=15.2 mM for arsenate1 Publication
- KM=32.9 nM for glutaredoxin Grx21 Publication
pH dependencei
Optimum pH is 6.3-6.8.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 8 | Important for activity. Lowers pKa of the active site Cys1 Publication | 1 | |
Active sitei | 12 | Nucleophile; cysteine thioarsenate intermediatePROSITE-ProRule annotation3 Publications | 1 | |
Sitei | 60 | Important for activity. Involved in arsenate binding and transition-state stabilization3 Publications | 1 | |
Sitei | 94 | Important for activity. Involved in arsenate binding and transition-state stabilization3 Publications | 1 | |
Sitei | 107 | Important for activity. Involved in arsenate binding and transition-state stabilization3 Publications | 1 |
GO - Molecular functioni
- arsenate reductase (glutaredoxin) activity Source: UniProtKB-EC
GO - Biological processi
- response to arsenic-containing substance Source: UniProtKB-KW
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Arsenical resistance |
Names & Taxonomyi
Protein namesi | Recommended name: Arsenate reductase1 Publication (EC:1.20.4.13 Publications)Alternative name(s): Arsenical pump modifier |
Gene namesi | Name:arsC1 Publication |
Encoded oni | Plasmid R7738 Publications |
Organismi | Escherichia coli |
Taxonomic identifieri | 562 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 8 | H → P, G or R: Loss of reductase activity. Mutant is sensitive to arsenate. 1 Publication | 1 | |
Mutagenesisi | 8 | H → S: Mutant is sensitive to arsenate. 1 Publication | 1 | |
Mutagenesisi | 12 | C → A or G: Mutant is sensitive to arsenate. 1 Publication | 1 | |
Mutagenesisi | 12 | C → S: Loss of reductase activity. Mutant is sensitive to arsenate. 1 Publication | 1 | |
Mutagenesisi | 60 | R → A: 50-fold decrease in catalytic efficiency with arsenate. Mutant is sensitive to arsenate. 1 Publication | 1 | |
Mutagenesisi | 60 | R → E: 70-fold decrease in catalytic efficiency with arsenate. Mutant is sensitive to arsenate. 1 Publication | 1 | |
Mutagenesisi | 60 | R → K: 22-fold decrease in catalytic efficiency with arsenate. Mutant shows low-level resistance to arsenate. 1 Publication | 1 | |
Mutagenesisi | 61 | K → A, E or R: Mutant retains arsenate resistance. 1 Publication | 1 | |
Mutagenesisi | 88 | H → R, S, V or W: No change in reductase activity. Mutant retains arsenate resistance. 1 Publication | 1 | |
Mutagenesisi | 94 | R → A, E or Y: Loss of reductase activity. Mutant is sensitive to arsenate. 1 Publication | 1 | |
Mutagenesisi | 94 | R → K: Loss of reductase activity. Mutant exhibits slight resistance to arsenate. 1 Publication | 1 | |
Mutagenesisi | 106 | C → G or S: Retains reductase activity. Mutant retains arsenate resistance. 1 Publication | 1 | |
Mutagenesisi | 106 | C → V: Mutant retains arsenate resistance. 1 Publication | 1 | |
Mutagenesisi | 107 | R → A, E or Y: Loss of reductase activity. Mutant is sensitive to arsenate. 1 Publication | 1 | |
Mutagenesisi | 107 | R → K: Mutant retains arsenate resistance. 1 Publication | 1 | |
Mutagenesisi | 127 | E → A: 6-fold decrease in catalytic efficiency with arsenate. Mutant is sensitive at high arsenate concentrations. 1 Publication | 1 | |
Mutagenesisi | 127 | E → D: 13-fold decrease in catalytic efficiency with arsenate. Mutant is sensitive at high arsenate concentrations. 1 Publication | 1 | |
Mutagenesisi | 127 | E → K: 17-fold decrease in catalytic efficiency with arsenate. Mutant is sensitive at high arsenate concentrations. 1 Publication | 1 | |
Mutagenesisi | 128 | D → A: 4-fold decrease in catalytic efficiency with arsenate. Mutant is relatively resistant to arsenate, but is more sensitive at higher concentrations. 1 Publication | 1 | |
Mutagenesisi | 128 | D → E: 7-fold decrease in catalytic efficiency with arsenate. Mutant is relatively resistant to arsenate, but is more sensitive at higher concentrations. 1 Publication | 1 | |
Mutagenesisi | 128 | D → K: 9-fold decrease in catalytic efficiency with arsenate. Mutant is relatively resistant to arsenate, but is more sensitive at higher concentrations. 1 Publication | 1 | |
Mutagenesisi | 130 | E → A: 3-fold decrease in catalytic efficiency with arsenate. Mutant is relatively resistant to arsenate, but is more sensitive at higher concentrations. 1 Publication | 1 | |
Mutagenesisi | 130 | E → D: 5-fold decrease in catalytic efficiency with arsenate. Mutant is relatively resistant to arsenate, but is more sensitive at higher concentrations. 1 Publication | 1 | |
Mutagenesisi | 130 | E → K: 5-fold decrease in catalytic efficiency with arsenate. Mutant is relatively resistant to arsenate, but is more sensitive at higher concentrations. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB04456, Arsenous acid DB03352, S-Arsonocysteine DB03289, Thiarsa Dihydroxy Cysteine DB01808, Thiarsahydroxy-Cysteine |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000162537 | 1 – 141 | Arsenate reductaseAdd BLAST | 141 |
Interactioni
Subunit structurei
Monomer in solution.
1 PublicationProtein-protein interaction databases
STRINGi | 585034.ECIAI1_3650 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | P08692 |
SMRi | P08692 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P08692 |
Family & Domainsi
Sequence similaritiesi
Belongs to the ArsC family.Curated
Phylogenomic databases
eggNOGi | COG1393, Bacteria |
Family and domain databases
CDDi | cd03034, ArsC_ArsC, 1 hit |
InterProi | View protein in InterPro IPR006659, Arsenate_reductase IPR006660, Arsenate_reductase-like IPR036249, Thioredoxin-like_sf |
PANTHERi | PTHR30041, PTHR30041, 1 hit |
Pfami | View protein in Pfam PF03960, ArsC, 1 hit |
SUPFAMi | SSF52833, SSF52833, 1 hit |
TIGRFAMsi | TIGR00014, arsC, 1 hit |
PROSITEi | View protein in PROSITE PS51353, ARSC, 1 hit |
i Sequence
Sequence statusi: Complete.
P08692-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J02591 Genomic DNA Translation: AAA21096.1 |
PIRi | C25937 |
RefSeqi | WP_011117598.1, NZ_VNXP01000024.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J02591 Genomic DNA Translation: AAA21096.1 |
PIRi | C25937 |
RefSeqi | WP_011117598.1, NZ_VNXP01000024.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1I9D | X-ray | 1.65 | A | 1-141 | [»] | |
1J9B | X-ray | 1.26 | A | 1-141 | [»] | |
1JZW | X-ray | 1.76 | A | 1-140 | [»] | |
1S3C | X-ray | 1.25 | A | 1-141 | [»] | |
1S3D | X-ray | 1.54 | A | 3-140 | [»] | |
1SD8 | X-ray | 1.59 | A | 1-141 | [»] | |
1SD9 | X-ray | 1.65 | A | 1-141 | [»] | |
1SJZ | X-ray | 1.80 | A | 1-140 | [»] | |
1SK0 | X-ray | 1.80 | A | 1-140 | [»] | |
1SK1 | X-ray | 1.55 | A | 1-140 | [»] | |
1SK2 | X-ray | 1.54 | A | 1-140 | [»] | |
AlphaFoldDBi | P08692 | |||||
SMRi | P08692 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 585034.ECIAI1_3650 |
Chemistry databases
DrugBanki | DB04456, Arsenous acid DB03352, S-Arsonocysteine DB03289, Thiarsa Dihydroxy Cysteine DB01808, Thiarsahydroxy-Cysteine |
Phylogenomic databases
eggNOGi | COG1393, Bacteria |
Miscellaneous databases
EvolutionaryTracei | P08692 |
Family and domain databases
CDDi | cd03034, ArsC_ArsC, 1 hit |
InterProi | View protein in InterPro IPR006659, Arsenate_reductase IPR006660, Arsenate_reductase-like IPR036249, Thioredoxin-like_sf |
PANTHERi | PTHR30041, PTHR30041, 1 hit |
Pfami | View protein in Pfam PF03960, ArsC, 1 hit |
SUPFAMi | SSF52833, SSF52833, 1 hit |
TIGRFAMsi | TIGR00014, arsC, 1 hit |
PROSITEi | View protein in PROSITE PS51353, ARSC, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ARSC1_ECOLX | |
Accessioni | P08692Primary (citable) accession number: P08692 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 1, 1988 |
Last sequence update: | January 1, 1988 | |
Last modified: | May 25, 2022 | |
This is version 117 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, PlasmidDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families