Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutaredoxin arsenate reductase

Gene

arsC

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Reduces arsenate [As(V)] to arsenite [As(III)] using glutathione and glutaredoxin as sources of reducing equivalents. GrxA is the most effective electron donor in vivo compared to other glutaredoxins. Constitutes the major arsenate reductase compared to ArsI1 and ArsI2. Also shows weak phosphatase activity toward p-nitrophenyl phosphate.3 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Arsenate + glutaredoxin = arsenite + glutaredoxin disulfide + H2O.

Kineticsi

  1. KM=77 mM for p-nitrophenyl phosphate1 Publication
  1. Vmax=3.1 µmol/min/mg enzyme with arsenate as substrate1 Publication
  2. Vmax=0.08 µmol/min/mg enzyme with p-nitrophenyl phosphate as substrate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei8 – 81NucleophileBy similarity
Active sitei80 – 801NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Oxidoreductase

Keywords - Biological processi

Arsenical resistance

Enzyme and pathway databases

BRENDAi1.20.4.1. 382.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaredoxin arsenate reductase (EC:1.20.4.1)
Alternative name(s):
Low molecular weight protein-tyrosine-phosphatase (EC:3.1.3.48)
Protein ArsC
Short name:
SynArsC
Short name:
rSynArsC
Gene namesi
Name:arsC
Ordered Locus Names:slr0946
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
Proteomesi
  • UP000001425 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81C → S: Abolishes arsenate reductase activity. 2 Publications
Mutagenesisi13 – 131C → S: Little or no effect on arsenate reductase activity. Abolishes protein phosphatase activity. 2 Publications
Mutagenesisi35 – 351C → A: Little or no effect on arsenate reductase activity. 1 Publication
Mutagenesisi80 – 801C → S: Abolishes arsenate reductase activity. 2 Publications
Mutagenesisi82 – 821C → S: Abolishes arsenate reductase activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 131131Glutaredoxin arsenate reductasePRO_0000429130Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi8 ↔ 80Redox-active; alternate1 Publication
Disulfide bondi80 ↔ 82Redox-active; alternate1 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
131
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Helixi13 – 2513Combined sources
Turni26 – 294Combined sources
Beta strandi30 – 356Combined sources
Beta strandi36 – 394Combined sources
Helixi44 – 518Combined sources
Turni52 – 543Combined sources
Helixi58 – 603Combined sources
Helixi65 – 673Combined sources
Helixi70 – 723Combined sources
Beta strandi74 – 785Combined sources
Beta strandi80 – 823Combined sources
Helixi83 – 853Combined sources
Helixi89 – 924Combined sources
Beta strandi93 – 986Combined sources
Helixi109 – 13022Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L17NMR-A1-131[»]
2L18NMR-A1-131[»]
2L19NMR-A1-131[»]
2MYNNMR-A1-131[»]
2MYPNMR-A1-131[»]
2MYTNMR-A1-131[»]
2MYUNMR-A1-131[»]
ProteinModelPortaliP74313.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP74313.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

HOGENOMiHOG000273093.
InParanoidiP74313.
KOiK03741.
OMAiKRVMFVC.
PhylomeDBiP74313.

Family and domain databases

CDDicd00115. LMWPc. 1 hit.
InterProiIPR014062. Arsenate_reductase_gluta.
IPR023485. Ptyr_pPase_SF.
[Graphical view]
PfamiPF01451. LMWPc. 1 hit.
[Graphical view]
SMARTiSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMiSSF52788. SSF52788. 1 hit.
TIGRFAMsiTIGR02689. ars_reduc_gluta. 1 hit.

Sequencei

Sequence statusi: Complete.

P74313-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKVMFVCKR NSCRSQMAEG FAKTLGAGKI AVTSCGLESS RVHPTAIAMM
60 70 80 90 100
EEVGIDISGQ TSDPIENFNA DDYDVVISLC GCGVNLPPEW VTQEIFEDWQ
110 120 130
LEDPDGQSLE VFRTVRGQVK ERVENLIAKI S
Length:131
Mass (Da):14,443
Last modified:February 1, 1997 - v1
Checksum:i7D2013D6910A18B8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA18407.1.
PIRiS76148.

Genome annotation databases

EnsemblBacteriaiBAA18407; BAA18407; BAA18407.
KEGGisyn:slr0946.
PATRICi23840936. VBISynSp132158_2022.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA18407.1.
PIRiS76148.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L17NMR-A1-131[»]
2L18NMR-A1-131[»]
2L19NMR-A1-131[»]
2MYNNMR-A1-131[»]
2MYPNMR-A1-131[»]
2MYTNMR-A1-131[»]
2MYUNMR-A1-131[»]
ProteinModelPortaliP74313.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA18407; BAA18407; BAA18407.
KEGGisyn:slr0946.
PATRICi23840936. VBISynSp132158_2022.

Phylogenomic databases

HOGENOMiHOG000273093.
InParanoidiP74313.
KOiK03741.
OMAiKRVMFVC.
PhylomeDBiP74313.

Enzyme and pathway databases

BRENDAi1.20.4.1. 382.

Miscellaneous databases

EvolutionaryTraceiP74313.

Family and domain databases

CDDicd00115. LMWPc. 1 hit.
InterProiIPR014062. Arsenate_reductase_gluta.
IPR023485. Ptyr_pPase_SF.
[Graphical view]
PfamiPF01451. LMWPc. 1 hit.
[Graphical view]
SMARTiSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMiSSF52788. SSF52788. 1 hit.
TIGRFAMsiTIGR02689. ars_reduc_gluta. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiARSC_SYNY3
AccessioniPrimary (citable) accession number: P74313
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 14, 2014
Last sequence update: February 1, 1997
Last modified: September 7, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Cys-8 probably provides the initial functional group for covalent attachment of the electron-accepting substrate, arsenate, to ArsC.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

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.