Skip Header

 
Contribute Send feedback
Read comments (?) or add your own

Reviewed, UniProtKB/Swiss-Prot P82385 (SOR_PYRFU)

Last modified December 15, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Superoxide reductase
      Short name=SOR
    EC=1.15.1.2
Gene names
Name: sorA
Ordered Locus Names: PF1281
OrganismPyrococcus furiosus [Complete proteome] [HAMAP]
Taxonomic identifier2261 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length124 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Uses electrons from reduced NADP, by way of rubredoxin and an oxidoreductase, to catalyze the reduction of superoxide to hydrogen peroxide.

Catalytic activity

Reduced rubredoxin + superoxide + 2 H+ = rubredoxin + H2O2.

Cofactor

Iron.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the desulfoferrodoxin family.

Ontologies

Keywords
   Biological processElectron transport
Transport
   LigandIron
Metal-binding
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processelectron transport chain

Inferred from electronic annotation. Source: UniProtKB-KW

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioniron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

superoxide reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 124124Superoxide reductase
PRO_0000140873

Sites

Metal binding141Iron
Metal binding161Iron
Metal binding411Iron
Metal binding471Iron
Metal binding1111Iron
Metal binding1141Iron

Secondary structure

..................... 124
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P82385-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: EDD92C7E501C8048

FASTA12414,324
        10         20         30         40         50         60 
MISETIRSGD WKGEKHVPVI EYEREGELVK VKVQVGKEIP HPNTTEHHIR YIELYFLPEG 

        70         80         90        100        110        120 
ENFVYQVGRV EFTAHGESVN GPNTSDVYTE PIAYFVLKTK KKGKLYALSY CNIHGLWENE 


VTLE 

« Hide

References

« Hide 'large scale' references
[1]"Anaerobic microbes: oxygen detoxification without superoxide dismutase."
Jenney F.E. Jr., Verhagen M.F.J.M., Cui X., Adams M.W.W.
Science 286:306-309(1999) [PubMed: 10514376] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[2]"The complete sequence of the Pyrococcus furiosus genome."
Weiss R.B., Dunn D.M., Robb F.T., Brown J.R.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[3]"Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states."
Yeh A.P., Hu Y., Jenney F.E. Jr., Adams M.W.W., Rees D.C.
Biochemistry 39:2499-2508(2000) [PubMed: 10704199] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

Cross-references

Sequence databases

AF156097 Genomic DNA. Translation: AAF03229.1.
AE009950 Genomic DNA. Translation: AAL81405.1.
PIRT44571.
RefSeqNP_579010.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1DO6X-ray2.00A/B1-124[»]
1DQIX-ray1.70A/B/C/D1-124[»]
1DQKX-ray2.00A/B/C/D1-124[»]
ModBaseSearch...

Genome annotation databases

GeneID1469154.
GenomeReviewsGene locus PF1281 in contig AE009950_GR.
KEGGpfu:PF1281.
NMPDRfig|186497.1.peg.1325.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG541098.
OMAEHHIAWI.

Enzyme and pathway databases

BRENDA1.15.1.2. 321.

Family and domain databases

InterProIPR002742. Desulfoferrodoxin_Fe-bd.
[Graphical view]
PfamPF01880. Desulfoferrodox. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSOR_PYRFU
AccessionPrimary (citable) accession number: P82385
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 2000
Last modified: December 15, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents