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P00214 (FER1_AZOVI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ferredoxin-1
Alternative name(s):
Ferredoxin I
Short name=FdI
Gene names
Name:fdxA
OrganismAzotobacter vinelandii
Taxonomic identifier354 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Protein attributes

Sequence length107 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. This ferredoxin could play a role in regulating gene expression by interacting directly with DNA.

Cofactor

Binds 1 4Fe-4S cluster.

Binds 1 3Fe-4S cluster.

Sequence similarities

Contains 2 4Fe-4S ferredoxin-type domains.

Biophysicochemical properties

Redox potential:

E0 is -450 mV for the 3Fe-4S, and -645 mV for the 4Fe-4S clusters.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 107106Ferredoxin-1
PRO_0000159095

Regions

Domain2 – 30294Fe-4S ferredoxin-type 1
Domain31 – 60304Fe-4S ferredoxin-type 2

Sites

Metal binding91Iron-sulfur 1 (3Fe-4S) Ref.5
Metal binding171Iron-sulfur 1 (3Fe-4S) Ref.5
Metal binding211Iron-sulfur 2 (4Fe-4S) Ref.5
Metal binding401Iron-sulfur 2 (4Fe-4S) Ref.5
Metal binding431Iron-sulfur 2 (4Fe-4S) Ref.5
Metal binding461Iron-sulfur 2 (4Fe-4S) Ref.5
Metal binding501Iron-sulfur 1 (3Fe-4S) Ref.5

Experimental info

Sequence conflict491E → R in AAA16869. Ref.2
Sequence conflict531Q → E AA sequence Ref.3

Secondary structure

............................. 107
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00214 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 3B4B0D1A55765B2B

FASTA10712,182
        10         20         30         40         50         60 
MAFVVTDNCI KCKYTDCVEV CPVDCFYEGP NFLVIHPDEC IDCALCEPEC PAQAIFSEDE 

        70         80         90        100 
VPEDMQEFIQ LNAELAEVWP NITEKKDPLP DAEDWDGVKG KLQHLER 

« Hide

References

[1]"Azotobacter vinelandii ferredoxin I: cloning, sequencing, and mutant analysis."
Morgan T.V., Lundell D.J., Burgess B.K.
J. Biol. Chem. 263:1370-1375(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Azotobacter vinelandii mutS: nucleotide sequence and mutant analysis."
Le O., Shen B., Iismaa S.E., Burgess B.K.
J. Bacteriol. 175:7707-7710(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW.
[3]"Structure of Azotobacter vinelandii 7Fe ferredoxin. Amino acid sequence and electron density maps of residues."
Howard J.B., Lorsbach T.W., Ghosh D., Melis K., Stout C.D.
J. Biol. Chem. 258:508-522(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-107, X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).
[4]"Iron-sulfur clusters and protein structure of Azotobacter ferredoxin at 2.0-A resolution."
Ghosh D., O'Donnell S., Furey W.F. Jr., Robbins A.H., Stout C.D.
J. Mol. Biol. 158:73-109(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).
[5]"Structure of ferredoxin I from Azotobacter vinelandii."
Stout G.H., Turley S., Sieker L.C., Jensen L.H.
Proc. Natl. Acad. Sci. U.S.A. 85:1020-1022(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
[6]"Refinement of the 7 Fe ferredoxin from Azotobacter vinelandii at 1.9-A resolution."
Stout G.H.
J. Mol. Biol. 205:545-555(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[7]"Structure at pH 6.5 of ferredoxin I from Azotobacter vinelandii at 2.3-A resolution."
Merritt E.A., Stout G.H., Turley S., Sieker L.C., Jensen L.H., Orme-Johnson W.H.
Acta Crystallogr. D 49:272-281(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[8]"Structure of Azotobacter vinelandii 7Fe ferredoxin at 1.35-A resolution and determination of the [Fe-S] bonds with 0.01-A accuracy."
Stout C.D., Stura E.A., McRee D.E.
J. Mol. Biol. 278:629-639(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
[9]"Oxidized and reduced Azotobacter vinelandii ferredoxin I at 1.4-A resolution: conformational change of surface residues without significant change in the [3Fe-4S]+/0 cluster."
Schipke C.G., Goodin D.B., McRee D.E., Stout C.D.
Biochemistry 38:8228-8239(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
[10]"Alteration of the reduction potential of the [4Fe-4S](2+/+) cluster of Azotobacter vinelandii ferredoxin I."
Chen K., Tilley G.J., Sridhar V., Prasad G.S., Stout C.D., Armstrong F.A., Burgess B.K.
J. Biol. Chem. 274:36479-36487(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[11]"Does ferredoxin I (Azotobacter) represent a novel class of DNA-binding proteins that regulate gene expression in response to cellular iron(II)?"
Thomson A.J.
FEBS Lett. 285:230-236(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING.
[12]"Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: [Fe-S] cluster-driven protein rearrangement."
Martin A.E., Burgess B.K., Stout C.D., Cash V.L., Dean D.R., Jensen G.M., Stephens P.J.
Proc. Natl. Acad. Sci. U.S.A. 87:598-602(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[13]"Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I. Changes in [4Fe-4S] cluster reduction potential and reactivity."
Iismaa S.E., Vazquez A.E., Jensen G.M., Stephens P.J., Butt J.N., Armstrong F.A., Burgess B.K.
J. Biol. Chem. 266:21563-21571(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[14]"Azotobacter vinelandii ferredoxin I. Alteration of individual surface charges and the [4FE-4S]2+/+ cluster reduction potential."
Shen B., Jollie D.R., Stout C.D., Diller T.C., Armstrong F.A., Gorst C.M., la Mar G.N., Stephen P.J., Burgess B.K.
J. Biol. Chem. 269:8564-8575(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03521 Genomic DNA. Translation: AAA22125.1.
M63007 Unassigned DNA. Translation: AAA16869.1.
PIRFEAV. A29936.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A6LX-ray2.10A2-106[»]
1AXQX-ray2.10A2-106[»]
1B0TX-ray2.10A2-107[»]
1B0VX-ray2.80A/B/C/D2-107[»]
1D3WX-ray1.70A2-107[»]
1F5BX-ray1.62A4-106[»]
1F5CX-ray1.75A2-106[»]
1FD2X-ray1.90A2-107[»]
1FDAX-ray2.10A2-106[»]
1FDBX-ray2.20A2-106[»]
1FDDX-ray1.90A2-106[»]
1FERX-ray2.30A2-107[»]
1FF2X-ray2.30A2-106[»]
1FRHX-ray2.30A4-107[»]
1FRIX-ray2.10A2-107[»]
1FRJX-ray2.30A2-107[»]
1FRKX-ray2.10A2-107[»]
1FRLX-ray2.30A2-107[»]
1FRMX-ray2.30A2-107[»]
1FRXX-ray2.50A2-106[»]
1FTCX-ray2.35A/B2-106[»]
1G3OX-ray1.65A2-106[»]
1G6BX-ray1.90A2-106[»]
1GAOX-ray2.20A/B/C/D2-106[»]
1PC4X-ray1.65A1-107[»]
1PC5X-ray1.80A1-107[»]
2FD2X-ray1.90A2-106[»]
5FD1X-ray1.90A2-106[»]
6FD1X-ray1.35A2-107[»]
6FDRX-ray1.40A2-107[»]
7FD1X-ray1.30A2-107[»]
7FDRX-ray1.40A2-107[»]
ProteinModelPortalP00214.
SMRP00214. Positions 2-107.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001450. 4Fe4S-bd_dom.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR000813. 7Fe_ferredoxin.
IPR022569. Fd_C.
[Graphical view]
PfamPF11953. DUF3470. 1 hit.
PF00037. Fer4. 1 hit.
[Graphical view]
PRINTSPR00354. 7FE8SFRDOXIN.
PROSITEPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00214.

Entry information

Entry nameFER1_AZOVI
AccessionPrimary (citable) accession number: P00214
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references