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Protein

Ferredoxin-6

Gene

fdxE

Organism
Rhodobacter capsulatus (Rhodopseudomonas capsulata)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Ferredoxins are small electron carrier proteins that participate in various redox reactions. FdVI is an essential protein required for growth of R.capsulatus. May be involved in Fe-S cluster assembly.1 Publication1 Publication

Cofactori

[2Fe-2S] cluster3 PublicationsNote: Binds 1 [2Fe-2S] cluster.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi40 – 401Iron-sulfur (2Fe-2S)2 Publications
Metal bindingi46 – 461Iron-sulfur (2Fe-2S)2 Publications
Metal bindingi49 – 491Iron-sulfur (2Fe-2S)2 Publications
Metal bindingi87 – 871Iron-sulfur (2Fe-2S)2 Publications

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-6
Alternative name(s):
Ferredoxin VI1 Publication
Short name:
FdVI1 Publication
Gene namesi
Name:fdxE1 Publication
OrganismiRhodobacter capsulatus (Rhodopseudomonas capsulata)
Taxonomic identifieri1061 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Pathology & Biotechi

Disruption phenotypei

Disruption of this gene is lethal.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 107106Ferredoxin-6PRO_0000201180Add
BLAST

Expressioni

Inductioni

Seems to be constitutively expressed. Is expressed at a similar level under N-limited and N-sufficient conditions.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi272942.RCAP_rcc02404.

Structurei

Secondary structure

1
107
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75Combined sources
Beta strandi13 – 175Combined sources
Helixi24 – 296Combined sources
Turni30 – 323Combined sources
Beta strandi41 – 466Combined sources
Beta strandi50 – 534Combined sources
Helixi55 – 584Combined sources
Helixi66 – 727Combined sources
Beta strandi75 – 773Combined sources
Turni80 – 823Combined sources
Beta strandi83 – 853Combined sources
Helixi86 – 883Combined sources
Helixi93 – 953Combined sources
Beta strandi98 – 1014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E9MX-ray2.07A2-107[»]
1UWMX-ray2.00A2-107[»]
ProteinModelPortaliP80306.
SMRiP80306. Positions 2-107.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80306.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 1061052Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the adrenodoxin/putidaredoxin family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4107Z7P. Bacteria.
COG0633. LUCA.
HOGENOMiHOG000244518.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR001055. Adrenodoxin.
IPR018298. Adrenodoxin_Fe-S_BS.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
PRINTSiPR00355. ADRENODOXIN.
SUPFAMiSSF54292. SSF54292. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS00814. ADX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P80306-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKIIFIEHN GTRHEVEAKP GLTVMEAARD NGVPGIDADC GGACACSTCH
60 70 80 90 100
AYVDPAWVDK LPKALPTETD MIDFAYEPNP ATSRLTCQIK VTSLLDGLVV

HLPEKQI
Length:107
Mass (Da):11,533
Last modified:November 26, 2014 - v2
Checksum:i64239FF7451D8D1B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11304 Genomic DNA. Translation: CAA72162.1.
PIRiS45612.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11304 Genomic DNA. Translation: CAA72162.1.
PIRiS45612.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E9MX-ray2.07A2-107[»]
1UWMX-ray2.00A2-107[»]
ProteinModelPortaliP80306.
SMRiP80306. Positions 2-107.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272942.RCAP_rcc02404.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4107Z7P. Bacteria.
COG0633. LUCA.
HOGENOMiHOG000244518.

Miscellaneous databases

EvolutionaryTraceiP80306.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR001055. Adrenodoxin.
IPR018298. Adrenodoxin_Fe-S_BS.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
PRINTSiPR00355. ADRENODOXIN.
SUPFAMiSSF54292. SSF54292. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS00814. ADX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A [2Fe-2S] ferredoxin (FdVI) is essential for growth of the photosynthetic bacterium Rhodobacter capsulatus."
    Armengaud J., Meyer C., Jouanneau Y.
    J. Bacteriol. 179:3304-3309(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, DISRUPTION PHENOTYPE.
    Strain: ATCC 33303 / B10.
  2. "Purification of a sixth ferredoxin from Rhodobacter capsulatus. Primary structure and biochemical properties."
    Naud I., Vincon M., Garin J., Gaillard J., Forest E., Jouanneau Y.
    Eur. J. Biochem. 222:933-939(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-107, COFACTOR, MASS SPECTROMETRY.
    Strain: ATCC 33303 / B10.
  3. "Crystallization and preliminary X-ray diffraction analysis of a [2Fe-2S] ferredoxin (FdVI) from Rhodobacter capsulatus."
    Armengaud J., Sainz G., Jouanneau Y., Sieker L.C.
    Acta Crystallogr. D 57:301-303(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (2FE-2S), COFACTOR.
    Strain: ATCC 33303 / B10.
  4. "Structure of a [2Fe-2S] ferredoxin from Rhodobacter capsulatus likely involved in Fe-S cluster biogenesis and conformational changes observed upon reduction."
    Sainz G., Jakoncic J., Sieker L.C., Stojanoff V., Sanishvili N., Asso M., Bertrand P., Armengaud J., Jouanneau Y.
    J. Biol. Inorg. Chem. 11:235-246(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (2FE-2S), COFACTOR.
    Strain: ATCC 33303 / B10.

Entry informationi

Entry nameiFER6_RHOCA
AccessioniPrimary (citable) accession number: P80306
Secondary accession number(s): Q9R767
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 26, 2014
Last modified: December 9, 2015
This is version 81 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, Direct protein sequencing

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.