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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)DescriptionActionsGraphical viewLength
Metal bindingi40Iron-sulfur (2Fe-2S)2 Publications1
Metal bindingi46Iron-sulfur (2Fe-2S)2 Publications1
Metal bindingi49Iron-sulfur (2Fe-2S)2 Publications1
Metal bindingi87Iron-sulfur (2Fe-2S)2 Publications1

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002011802 – 107Ferredoxin-6Add BLAST106

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

1107
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 7Combined sources5
Beta strandi13 – 17Combined sources5
Helixi24 – 29Combined sources6
Turni30 – 32Combined sources3
Beta strandi41 – 46Combined sources6
Beta strandi50 – 53Combined sources4
Helixi55 – 58Combined sources4
Helixi66 – 72Combined sources7
Beta strandi75 – 77Combined sources3
Turni80 – 82Combined sources3
Beta strandi83 – 85Combined sources3
Helixi86 – 88Combined sources3
Helixi93 – 95Combined sources3
Beta strandi98 – 101Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP80306.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 1062Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST105

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

CDDicd00207. fer2. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E9MX-ray2.07A2-107[»]
1UWMX-ray2.00A2-107[»]
ProteinModelPortaliP80306.
SMRiP80306.
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

CDDicd00207. fer2. 1 hit.
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...

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: November 2, 2016
This is version 84 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.