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Protein

Ferredoxin-1

Gene

petF

Organism
Nostoc sp. (strain PCC 7120 / UTEX 2576)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Cofactori

[2Fe-2S] clusterNote: Binds 1 [2Fe-2S] cluster.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi42 – 421Iron-sulfur (2Fe-2S)
Metal bindingi47 – 471Iron-sulfur (2Fe-2S)
Metal bindingi50 – 501Iron-sulfur (2Fe-2S)
Metal bindingi80 – 801Iron-sulfur (2Fe-2S)

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ferredoxin-1
Alternative name(s):
Ferredoxin I
Gene namesi
Name:petF
Synonyms:fdxV
Ordered Locus Names:all4148
OrganismiNostoc sp. (strain PCC 7120 / UTEX 2576)
Taxonomic identifieri103690 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeNostoc
Proteomesi
  • UP000002483 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi43 – 431R → A, E or H: No effect on electron transfer. 1 Publication
Mutagenesisi49 – 491T → A: No effect on electron transfer. 1 Publication
Mutagenesisi66 – 661F → A or I: 1000-fold decrease in electron transfer. 1 Publication
Mutagenesisi69 – 691D → K: Small effect on electron transfer. 1 Publication
Mutagenesisi70 – 701D → K: Small effect on electron transfer. 1 Publication
Mutagenesisi95 – 951E → K: 20000-fold decrease in electron transfer. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 9998Ferredoxin-1PRO_0000189300Add
BLAST

Interactioni

Subunit structurei

Forms a complex with heterodimeric ferredoxin-thioredoxin reductase (FTR) and thioredoxin.By similarity

Protein-protein interaction databases

STRINGi103690.all4148.

Structurei

Secondary structure

1
99
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108Combined sources
Turni11 – 144Combined sources
Beta strandi15 – 228Combined sources
Helixi27 – 337Combined sources
Beta strandi41 – 488Combined sources
Beta strandi51 – 577Combined sources
Helixi69 – 735Combined sources
Beta strandi76 – 783Combined sources
Helixi79 – 813Combined sources
Beta strandi83 – 864Combined sources
Beta strandi88 – 914Combined sources
Helixi95 – 973Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FXAX-ray2.50A/B2-99[»]
1J7AX-ray1.80A2-99[»]
1J7BX-ray1.80A2-99[»]
1J7CX-ray1.80A2-99[»]
1QOAX-ray1.70A/B2-99[»]
1QOBX-ray1.80A/B2-99[»]
1QOFX-ray1.80A/B2-99[»]
1QOGX-ray1.80A/B2-99[»]
ProteinModelPortaliP0A3C7.
SMRiP0A3C7. Positions 2-99.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A3C7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 96932Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2Fe2S plant-type ferredoxin family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410811Q. Bacteria.
COG0633. LUCA.
HOGENOMiHOG000217152.
KOiK02639.
OMAiCTIITHQ.
OrthoDBiEOG6GJC0W.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR010241. Fd_pln.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
SUPFAMiSSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR02008. fdx_plant. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A3C7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATFKVTLIN EAEGTKHEIE VPDDEYILDA AEEQGYDLPF SCRAGACSTC
60 70 80 90
AGKLVSGTVD QSDQSFLDDD QIEAGYVLTC VAYPTSDVVI QTHKEEDLY
Length:99
Mass (Da):10,830
Last modified:January 23, 2007 - v2
Checksum:i874FD6365346BFFF
GO

Mass spectrometryi

Molecular mass is 10921 Da from positions 2 - 99. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14737 Genomic DNA. Translation: AAA22021.1.
BA000019 Genomic DNA. Translation: BAB75847.1.
PIRiAE2324.
S25233.
RefSeqiWP_010998287.1. NC_003272.1.

Genome annotation databases

EnsemblBacteriaiBAB75847; BAB75847; BAB75847.
KEGGiana:all4148.
PATRICi22778851. VBINosSp37423_4874.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14737 Genomic DNA. Translation: AAA22021.1.
BA000019 Genomic DNA. Translation: BAB75847.1.
PIRiAE2324.
S25233.
RefSeqiWP_010998287.1. NC_003272.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FXAX-ray2.50A/B2-99[»]
1J7AX-ray1.80A2-99[»]
1J7BX-ray1.80A2-99[»]
1J7CX-ray1.80A2-99[»]
1QOAX-ray1.70A/B2-99[»]
1QOBX-ray1.80A/B2-99[»]
1QOFX-ray1.80A/B2-99[»]
1QOGX-ray1.80A/B2-99[»]
ProteinModelPortaliP0A3C7.
SMRiP0A3C7. Positions 2-99.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi103690.all4148.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB75847; BAB75847; BAB75847.
KEGGiana:all4148.
PATRICi22778851. VBINosSp37423_4874.

Phylogenomic databases

eggNOGiENOG410811Q. Bacteria.
COG0633. LUCA.
HOGENOMiHOG000217152.
KOiK02639.
OMAiCTIITHQ.
OrthoDBiEOG6GJC0W.

Miscellaneous databases

EvolutionaryTraceiP0A3C7.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR010241. Fd_pln.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
SUPFAMiSSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR02008. fdx_plant. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 7120 / UTEX 2576.
  3. Singh H., Rajaram H., Apte S.K.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 6-16, MASS SPECTROMETRY.
  4. "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] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  5. "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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  6. "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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  7. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), IRON-SULFUR CLUSTER-BINDING SITES CYS-42; CYS-47; CYS-50 AND CYS-80.
  8. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Entry informationi

Entry nameiFER1_NOSS1
AccessioniPrimary (citable) accession number: P0A3C7
Secondary accession number(s): P06543
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: December 9, 2015
This is version 80 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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.