Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot P0A3C7 (FER1_ANASP)

Last modified July 22, 2008. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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-1
Alternative name(s):
    Ferredoxin I
Gene names
Name: petF
Synonyms: fdxV
Ordered Locus Names: all4148
OrganismAnabaena sp. (strain PCC 7120) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

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.

Ontologies

Keywords

   Biological processElectron transport
Transport
   Ligand2Fe-2S
Iron
Iron-sulfur
Metal-binding
   Technical term3D-structure
Complete proteome

Gene Ontology (GO)

None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 9998Ferredoxin-1

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)

Experimental info

Mutagenesis431R → A, E or H: No effect on electron transfer
Mutagenesis491T → A: No effect on electron transfer
Mutagenesis661F → A or I: 1000-fold decrease in electron transfer
Mutagenesis691D → K: Small effect on electron transfer
Mutagenesis701D → K: Small effect on electron transfer
Mutagenesis951E → K: 20000-fold decrease in electron transfer

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A3C7-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 874FD6365346BFFF

FASTA9910,830
        10         20         30         40         50         60 
MATFKVTLIN EAEGTKHEIE VPDDEYILDA AEEQGYDLPF SCRAGACSTC AGKLVSGTVD 

        70         80         90 
QSDQSFLDDD QIEAGYVLTC VAYPTSDVVI QTHKEEDLY 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and sequence of the gene for ferredoxin I from the cyanobacterium Anabaena sp. strain PCC 7120."
Alam J., Whitaker R.A., Krogmann D.W., Curtis S.E.
J. Bacteriol. 168:1265-1271(1986) [PubMed: 2430949] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Amino acid residues in Anabaena ferredoxin crucial to interaction with ferredoxin-NADP+ reductase: site-directed mutagenesis and laser flash photolysis."
Hurley J.K., Salamon Z., Meyer T.E., Fitch J.C., Cusanovich M.A., Markley J.L., Cheng H., Xia B., Chae Y.K., Medina M., Gomez-Moreno C., Tollin G.
Biochemistry 32:9346-9354(1993) [PubMed: 8369305] [Abstract]
Cited for: MUTAGENESIS.
[4]"Multinuclear magnetic resonance studies of the 2Fe.2S* ferredoxin from Anabaena species strain PCC 7120. 1. Sequence-specific hydrogen-1 resonance assignments and secondary structure in solution of the oxidized form."
Oh B.-H., Markley J.L.
Biochemistry 29:3993-4004(1990) [PubMed: 2354171] [Abstract]
Cited for: STRUCTURE BY NMR.
[5]"Multinuclear magnetic resonance studies of the 2Fe.2S* ferredoxin from Anabaena species strain PCC 7120. 2. Sequence-specific carbon-13 and nitrogen-15 resonance assignments of the oxidized form."
Oh B.-H., Mooberry E.S., Markley J.L.
Biochemistry 29:4004-4011(1990) [PubMed: 2354172] [Abstract]
Cited for: STRUCTURE BY NMR.
[6]"Crystallization and structure determination to 2.5-A resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120."
Rypniewski W.R., Breiter D.R., Benning M.M., Wesenberg G., Oh B.-H., Markley J.L., Rayment I., Holden H.M.
Biochemistry 30:4126-4131(1991) [PubMed: 1902376] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), IRON-SULFUR CLUSTER-BINDING SITES CYS-42; CYS-47; CYS-50 AND CYS-80.
[7]"Structure-function relationships in Anabaena ferredoxin: correlations between X-ray crystal structures, reduction potentials, and rate constants of electron transfer to ferredoxin:NADP+ reductase for site-specific ferredoxin mutants."
Hurley J.K., Weber-Main A.M., Stankovich M.T., Benning M.M., Thoden J.B., Vanhooke J.L., Holden H.M., Chae Y.K., Xia B., Cheng H., Markley J.L., Martinez-Julvez M., Gomez-Moreno C., Schmeits J.L., Tollin G.
Biochemistry 36:11100-11117(1997) [PubMed: 9287153] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Cross-references

Sequence databases

M14737 Genomic DNA. Translation: AAA22021.1.
BA000019 Genomic DNA. Translation: BAB75847.1.
PIRAE2324.
S25233.
RefSeqNP_488188.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1FXAX-ray2.50A/B1-99[»]
1J7AX-ray1.80A1-99[»]
1J7BX-ray1.80A1-99[»]
1J7CX-ray1.80A1-99[»]
1QOAX-ray1.70A/B1-99[»]
1QOBX-ray1.80A/B1-99[»]
1QOFX-ray1.80A/B1-99[»]
1QOGX-ray1.80A/B1-99[»]
ModBaseSearch...

Genome annotation databases

GeneID1107750.
GenomeReviewsGene locus all4148 in contig BA000019_GR.
KEGGana:all4148.
NMPDRfig|103690.1.peg.4455.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP0A3C7.

Enzyme and pathway databases

BioCycNSP103690:ALL4148-MON.

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]
ProDomP0A3C7.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

LinkHubP0A3C7.
ProtoNetSearch...

Entry information

Entry nameFER1_ANASP
AccessionPrimary (citable) accession number: P0A3C7
Secondary accession number(s): P06543
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: July 22, 2008
This is version 30 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

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

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