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Reviewed, UniProtKB/Swiss-Prot P00246 (FER_SPIPL)

Last modified November 25, 2008. Version 63. 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:
    Ferredoxin
OrganismSpirulina platensis
Taxonomic identifier118562 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatorialesArthrospira

Protein attributes

Sequence length99 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.

Cofactor

Binds 1 2Fe-2S cluster.

Sequence similarities

Belongs to the 2Fe2S plant-type ferredoxin family.

Contains 1 2Fe-2S ferredoxin-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 9998Ferredoxin
PRO_0000189371

Regions

Domain4 – 96932Fe-2S ferredoxin-type

Sites

Metal binding421Iron-sulfur (2Fe-2S)
Metal binding471Iron-sulfur (2Fe-2S)
Metal binding501Iron-sulfur (2Fe-2S)
Metal binding801Iron-sulfur (2Fe-2S)

Secondary structure

................... 99
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00246-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 71F9CA733DB03741

FASTA9910,634
        10         20         30         40         50         60 
MATYKVTLIN EAEGINETID CDDDTYILDA AEEAGLDLPY SCRAGACSTC AGTITSGTID 

        70         80         90 
QSDQSFLDDD QIEAGYVLTC VAYPTSDCTI KTHQEEGLY 

« Hide

References

[1]"The complete amino acid sequence of the Spirulina platensis ferredoxin."
Tanaka M., Haniu M., Yasunobu K.T., Rao K.K., Hall D.O.
Biochem. Biophys. Res. Commun. 69:759-765(1976) [PubMed: 817723] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-99.
[2]"X-ray analysis of a [2Fe-2S] ferrodoxin from Spirulina platensis. Main chain fold and location of side chains at 2.5-A resolution."
Tsukihara T., Fukuyama K., Nakamura M., Katsube Y., Tanaka N., Kakudo M., Wada K., Hase T., Matsubara H.
J. Biochem. 90:1763-1773(1981) [PubMed: 6801028] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[3]"Structure of S. platensis [2Fe-2S] ferredoxin and evolution of chloroplast-type ferrodoxins."
Fukuyama K., Hase T., Matsumoto S., Tsukihara T., Katsube Y., Tanaka N., Kakudo M., Wada K., Hase T., Matsubara H.
Nature 286:522-524(1980)
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRFESGAL. A00250.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
4FXCX-ray2.50A1-99[»]
ModBaseSearch...

Family and domain databases

InterProIPR006058. 2Fe2S_fd_BS.
IPR012675. b-grasp_ferredoxin-like.
IPR010241. Fdx_pln.
IPR001041. Ferredoxin.
[Graphical view]
Gene3DG3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
PfamPF00111. Fer2. 1 hit.
[Graphical view]
TIGRFAMsTIGR02008. fdx_plant. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubP00246.

Entry information

Entry nameFER_SPIPL
AccessionPrimary (citable) accession number: P00246
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 25, 2008
This is version 63 of the entry and version 2 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