arsC

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

Catalytic activityⁱ

[glutaredoxin]-dithiol
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Search chemical reactions in Rhea for this molecule.
+
arsenate
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See the description of this molecule in ChEBI.
+
glutathione
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See the description of this molecule in ChEBI.
+
H⁺
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=
arsenite
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See the description of this molecule in ChEBI.
+
glutathionyl-S-S-[glutaredoxin]
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+
H₂O
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See the description of this molecule in ChEBI.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.4
  "Properties of the arsenate reductase of plasmid R773."
  Gladysheva T.B., Oden K.L., Rosen B.P.
  Biochemistry 33:7288-7293(1994) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Ref.5
  "Identification of an essential cysteinyl residue in the ArsC arsenate reductase of plasmid R773."
  Liu J., Gladysheva T.B., Lee L., Rosen B.P.
  Biochemistry 34:13472-13476(1995) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, ACTIVE SITE, MUTAGENESIS OF CYS-12 AND CYS-106.
- Ref.7
  "Identification of a triad of arginine residues in the active site of the ArsC arsenate reductase of plasmid R773."
  Shi J., Mukhopadhyay R., Rosen B.P.
  FEMS Microbiol. Lett. 227:295-301(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-60; LYS-61; ARG-94; ARG-107; GLU-127; ASP-128 AND GLU-130.
EC:
1.20.4.1
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.4
  "Properties of the arsenate reductase of plasmid R773."
  Gladysheva T.B., Oden K.L., Rosen B.P.
  Biochemistry 33:7288-7293(1994) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Ref.5
  "Identification of an essential cysteinyl residue in the ArsC arsenate reductase of plasmid R773."
  Liu J., Gladysheva T.B., Lee L., Rosen B.P.
  Biochemistry 34:13472-13476(1995) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, ACTIVE SITE, MUTAGENESIS OF CYS-12 AND CYS-106.
- Ref.7
  "Identification of a triad of arginine residues in the active site of the ArsC arsenate reductase of plasmid R773."
  Shi J., Mukhopadhyay R., Rosen B.P.
  FEMS Microbiol. Lett. 227:295-301(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-60; LYS-61; ARG-94; ARG-107; GLU-127; ASP-128 AND GLU-130.
This reaction proceeds in the
forward
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
3 Publications
Manual assertion based on experiment inⁱ
- Ref.4
  "Properties of the arsenate reductase of plasmid R773."
  Gladysheva T.B., Oden K.L., Rosen B.P.
  Biochemistry 33:7288-7293(1994) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
- Ref.5
  "Identification of an essential cysteinyl residue in the ArsC arsenate reductase of plasmid R773."
  Liu J., Gladysheva T.B., Lee L., Rosen B.P.
  Biochemistry 34:13472-13476(1995) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, ACTIVE SITE, MUTAGENESIS OF CYS-12 AND CYS-106.
- Ref.7
  "Identification of a triad of arginine residues in the active site of the ArsC arsenate reductase of plasmid R773."
  Shi J., Mukhopadhyay R., Rosen B.P.
  FEMS Microbiol. Lett. 227:295-301(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-60; LYS-61; ARG-94; ARG-107; GLU-127; ASP-128 AND GLU-130.
direction.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
[glutaredoxin]-dithiol
L-cysteine residue
Position: n
zoom
L-cysteine residue
Position: n+3
zoom
+
arsenate
zoom
+
glutathione
zoom
+
H⁺
=
arsenite
zoom
+
glutathionyl-S-S-[glutaredoxin]
L-cysteine residue
Position: n+3
zoom
S-(S-glutathionyl)-L-cysteine residue
Position: n
zoom
+
H₂O

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

pH dependenceⁱ

Optimum pH is 6.3-6.8.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	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

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

response to arsenic-containing substance Source: UniProtKB-KW

Complete GO annotation on QuickGO ...

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	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	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

Drug and drug target database More...DrugBankⁱ	DB04456, Arsenous acid DB03352, S-Arsonocysteine DB03289, Thiarsa Dihydroxy Cysteine DB01808, Thiarsahydroxy-Cysteine

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 Publication

Protein-protein interaction databases

STRINGⁱ	585034.ECIAI1_3650

STRINGⁱ

585034.ECIAI1_3650

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	5 – 7	Combined sources	3
Helixⁱ	13 – 24	Combined sources	12
Beta strandⁱ	30 – 32	Combined sources	3
Turnⁱ	34 – 36	Combined sources	3
Helixⁱ	41 – 51	Combined sources	11
Helixⁱ	55 – 58	Combined sources	4
Beta strandⁱ	61 – 63	Combined sources	3
Helixⁱ	64 – 68	Combined sources	5
Turnⁱ	69 – 72	Combined sources	4
Helixⁱ	78 – 87	Combined sources	10
Helixⁱ	89 – 91	Combined sources	3
Beta strandⁱ	96 – 99	Combined sources	4
Beta strandⁱ	102 – 105	Combined sources	4
Helixⁱ	109 – 114	Combined sources	6
Beta strandⁱ	131 – 133	Combined sources	3

Show more details

3D structure databases

AlphaFoldDBⁱ	P08692
SMRⁱ	P08692
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P08692

EvolutionaryTraceⁱ

P08692

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the ArsC family.Curated

Phylogenomic databases

eggNOGⁱ	COG1393, Bacteria

eggNOGⁱ

COG1393, Bacteria

Family and domain databases

Conserved Domains Database More...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
Pfam protein domain database More...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

Sequenceⁱ

Sequence statusⁱ: Complete.

P08692-1 [UniParc]FASTA Add 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

Checksum:ⁱ240F4105487E2FBF

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J02591 Genomic DNA Translation: AAA21096.1
PIRⁱ	C25937
NCBI Reference Sequences More...RefSeqⁱ	WP_011117598.1, NZ_VNXP01000024.1

Protein	Similar proteins		Species	Score	Length	Source
P08692	Arsenate reductase		SALER		141	UniRef100_P08692
Arsenate reductase		Salmonella enterica subsp. enterica serovar Kentucky		141
Arsenate reductase		ECOLX		141
Arsenate reductase		CITKO		141
Arsenate reductase		SALTM		141
+2

Protein	Similar proteins		Species	Score	Length	Source
P08692	Arsenate reductase		ECOLI		141	UniRef90_P08692
Arsenate reductase		SHIFL		141
Arsenate reductase		SALER		141
Arsenate reductase		Salmonella enterica subsp. enterica serovar Kentucky		141
Arsenate reductase		ECOLX		141
+313

Protein	Similar proteins		Species	Score	Length	Source
P08692	Arsenate reductase		ECOLI		141	UniRef50_P08692
Arsenate reductase		SHIFL		141
Arsenate reductase		ACIMA		141
Arsenate reductase		SALER		141
Arsenate reductase		Salmonella enterica subsp. enterica serovar Kentucky		141
+965

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: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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

STRINGⁱ

585034.ECIAI1_3650

Chemistry databases

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

DrugBankⁱ

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

Phylogenomic databases

eggNOGⁱ	COG1393, Bacteria

eggNOGⁱ

COG1393, Bacteria

Miscellaneous databases

EvolutionaryTraceⁱ	P08692

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

UniProtKB

UniParc

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Supporting data

UniProtKB - P08692 (ARSC1_ECOLX)

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Arsenate reductase

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<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

<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 '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

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<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>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 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

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<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

<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

Protein-protein interaction databases

<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

3D structure databases

Miscellaneous databases

<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

Phylogenomic databases

Family and domain databases

Sequence databases

<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

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

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Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

pH dependenceⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ