Ferredoxin - Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

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P29603 (FER_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 106. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ferredoxin

Gene names

Name:	fdxA
Ordered Locus Names:	PF1909

Organism

Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) [Reference proteome] [HAMAP]

Taxonomic identifier

186497 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus ›

Protein attributes

Sequence length	67 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 4Fe-4S cluster which readily converts to a stable 3Fe-4S form.
Subunit structure	Homodimer Potential. Ref.15
Sequence similarities	Contains 2 4Fe-4S ferredoxin-type domains.

Ontologies

Keywords
Biological process	Electron transport Transport
Domain	Repeat
Ligand	3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 67

Ferredoxin

PRO_0000159199

Regions

Domain

3 – 31

4Fe-4S ferredoxin-type 1

Domain

36 – 67

4Fe-4S ferredoxin-type 2

Sites

Metal binding

Iron-sulfur (4Fe-4S)

Metal binding

Iron-sulfur (4Fe-4S)

Metal binding

Iron-sulfur (4Fe-4S)

Metal binding

Iron-sulfur (4Fe-4S)

Amino acid modifications

Disulfide bond

22 ↔ 49

Ref.10 Ref.11

Experimental info

Mutagenesis

D → C: No effect on the efficiency of electron transfer. Ref.3 Ref.5 Ref.12 Ref.13

Mutagenesis

D → S: The efficiency of electron transfer is compromised. Ref.3 Ref.5 Ref.12 Ref.13

Mutagenesis

A → C: The mixed spin cluster is converted into a homogeneous spin cluster (S=3/2). Ref.4 Ref.5 Ref.6

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P29603 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: AF9B062690B34420
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FASTA

7,298

        10         20         30         40         50         60 
MAWKVSVDQD TCIGDAICAS LCPDVFEMND EGKAQPKVEV IEDEELYNCA KEAMEACPVS 


AITIEEA

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, expression, and molecular characterization of the gene encoding an extremely thermostable [4Fe-4S] ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus." Heltzel A., Smith E.T., Zhou Z.H., Blamey J.M., Adams M.W.W. J. Bacteriol. 176:4790-4793(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[2]	"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences." Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T. Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[3]	"Site-directed mutations of the 4Fe-ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus: role of the cluster-coordinating aspartate in physiological electron transfer reactions." Zhou Z.H., Adams M.W.W. Biochemistry 36:10892-10900(1997) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ASP-15, CIRCULAR DICHROISM ANALYSIS, EPR SPECTROSCOPY.
[4]	"Spectroscopic evidence for a new type of [Fe3S4] cluster in a mutant form of Pyrococcus furiosus ferredoxin." Duderstadt R.E., Brereton P.S., Adams M.W.W., Johnson M.K. J. Am. Chem. Soc. 120:8525-8526(1998) Cited for: MUTAGENESIS OF ALA-34, MAGNETIC CIRCULAR DICHROISM, EPR SPECTROSCOPY, RESONANCE RAMAN SPECTROSCOPY OF (3FE--4S) FORM.
[5]	"Effect of serinate ligation at each of the iron sites of the [Fe4S4] cluster of Pyrococcus furiosus ferredoxin on the redox, spectroscopic, and biological properties." Brereton P.S., Duderstadt R.E., Staples C.R., Johnson M.K., Adams M.W.W. Biochemistry 38:10594-10605(1999) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYSTEINE RESIDUES, MAGNETIC CIRCULAR DICHROISM, EPR SPECTROSCOPY, RESONANCE RAMAN SPECTROSCOPY.
[6]	"A pure S=3/2 [Fe4S4]+ cluster in the A33Y variant of Pyrococcus furiosus ferredoxin." Duderstadt R.E., Brereton P.S., Adams M.W.W., Johnson M.K. FEBS Lett. 454:21-26(1999) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ALA-34, MAGNETIC CIRCULAR DICHROISM, EPR SPECTROSCOPY, RESONANCE RAMAN SPECTROSCOPY.
[7]	"Proton NMR investigation of the oxidized three-iron clusters in the ferredoxins from the hyperthermophilic archae Pyrococcus furiosus and Thermococcus litoralis." Busse S.C., la Mar G.N., Yu L.P., Howard J.B., Smith E.T., Zhou Z.H., Adams M.W.W. Biochemistry 31:11952-11962(1992) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[8]	"Solution 1H NMR determination of secondary structure for the three-iron form of ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus." Teng Q., Zhou Z.H., Smith E.T., Busse S.C., Howard J.B., Adams M.W.W., La Mar G.N. Biochemistry 33:6316-6326(1994) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 3FE--4S FORM.
[9]	"1H NMR investigation of the electronic and molecular structure of the four-iron cluster ferredoxin from the hyperthermophile Pyrococcus furiosus. Identification of Asp 14 as a cluster ligand in each of the four redox states." Calzolai L., Gorst C.M., Zhou Z.H., Teng Q., Adams M.W.W., La Mar G.N. Biochemistry 34:11373-11384(1995) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[10]	"1H NMR investigation of the paramagnetic cluster environment in Pyrococcus furiosus three-iron ferredoxin: sequence-specific assignment of ligated cysteines independent of tertiary structure." Gorst C.M., Yeh Y.-H., Teng Q., Calzolai L., Zhou Z.H., Adams M.W.W., La Mar G.N. Biochemistry 34:600-610(1995) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 3FE--4S FORM.
[11]	"Participation of the disulfide bridge in the redox cycle of the ferredoxin from the hyperthermophile Pyrococcus furiosus: 1H nuclear magnetic resonance time resolution of the four redox states at ambient temperature." Gorst C.M., Zhou Z.H., Teng Q., Howard J.B., Adams M.W.W., La Mar G.N. Biochemistry 34:8788-8795(1995) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR, DISULFIDE BOND.
[12]	"Role of cluster-ligated aspartate in gating electron transfer in the four-iron ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus." Calzolai L., Zhou Z.H., Adams M.W.W., La Mar G.N. J. Am. Chem. Soc. 118:2513-2514(1996) Cited for: STRUCTURE BY NMR, MUTAGENESIS OF ASP-15.
[13]	"Solution NMR study of the electronic structure and magnetic properties of cluster ligation mutants of the four-iron ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus." Calzolai L., Gorst C.M., Bren K.L., Zhou Z.H., Adams M.W.W., La Mar G.N. J. Am. Chem. Soc. 119:9341-9350(1997) Cited for: STRUCTURE BY NMR, MUTAGENESIS OF ASP-15.
[14]	"Solution NMR characterization of the thermodynamics of the disulfide bond orientational isomerism and its effect of cluster electronic properties for the hyperthermostable three-iron cluster ferredoxin from the archaeon Pyrococcus furiosus." Webba da Silva M., Sham S., Gorst C.M., Calzolai L., Brereton P.S., Adams M.W.W., La Mar G.N. Biochemistry 40:12575-12583(2001) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 3FE--4S FORM.
[15]	"The 1.5 A resolution crystal structure of [Fe3S4]-ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus." Nielsen M.S., Harris P., Ooi B.L., Christensen H.E. Biochemistry 43:5188-5194(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR CLUSTER, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X79502 Genomic DNA. Translation: CAA56040.1.
AE009950 Genomic DNA. Translation: AAL82033.1.

PIR

A44203.

RefSeq

NP_579638.1. NC_003413.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SIZ	X-ray	2.25	A/C	2-67	[»]
1SJ1	X-ray	1.50	A/B	2-67	[»]
2Z8Q	X-ray	1.70	A/B	2-67	[»]
3PNI	X-ray	2.80	A/B	2-67	[»]
4DHV	X-ray	1.95	A/B	2-67	[»]

ProteinModelPortal

P29603.

SMR

P29603. Positions 2-67.

ModBase

Search...

Protein-protein interaction databases

STRING

186497.PF1909.

Proteomic databases

PRIDE

P29603.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAL82033; AAL82033; PF1909.

GeneID

1469789.

KEGG

pfu:PF1909.

Phylogenomic databases

eggNOG

COG1141.

HOGENOM

HOG000044619.

K05337.

OMA

DAICASL.

ProtClustDB

CLSK253682.

Family and domain databases

InterPro

IPR001080. 3Fe4S_ferredoxin.
IPR017896. 4Fe4S_Fe-S-bd.
[Graphical view]

PRINTS

PR00352. 3FE4SFRDOXIN.

PROSITE

PS00198. 4FE4S_FER_1. False negative.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P29603.

Entry information

Entry name

FER_PYRFU

Accession

Primary (citable) accession number: P29603

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents