Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ferredoxin

Gene
N/A
Organism
Trichomonas vaginalis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. It links pyruvate:ferredoxin oxidoreductase to hydrogenase.

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi46Iron-sulfur (2Fe-2S)1
Metal bindingi52Iron-sulfur (2Fe-2S)1
Metal bindingi55Iron-sulfur (2Fe-2S)1
Metal bindingi85Iron-sulfur (2Fe-2S)1

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
OrganismiTrichomonas vaginalis
Taxonomic identifieri5722 [NCBI]
Taxonomic lineageiEukaryotaParabasaliaTrichomonadidaTrichomonadidaeTrichomonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Hydrogenosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000088411 – 81 Publication8
ChainiPRO_00000088429 – 100FerredoxinAdd BLAST92

Structurei

Secondary structure

1100
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 15Combined sources6
Beta strandi18 – 23Combined sources6
Helixi30 – 35Combined sources6
Turni36 – 38Combined sources3
Beta strandi47 – 52Combined sources6
Beta strandi56 – 62Combined sources7
Helixi68 – 74Combined sources7
Beta strandi81 – 83Combined sources3
Helixi84 – 86Combined sources3
Helixi91 – 93Combined sources3
Beta strandi97 – 99Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L5PX-ray2.20A/B/C9-100[»]
ProteinModelPortaliP21149.
SMRiP21149.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21149.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 1002Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST92

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
SUPFAMiSSF54292. SSF54292. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P21149-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSQVCRFGT ITAVKGGVKK QLKFEDDQTL FTVLTEAGLM SADDTCQGNK
60 70 80 90 100
ACGKCICKHV SGKVAAEDDE KEFLEDQPAN ARLACAITLS GENDGAVFEL
Length:100
Mass (Da):10,675
Last modified:May 1, 1991 - v1
Checksum:i66ADB3EDAD3F4773
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33717 Genomic DNA. Translation: AAA30324.1.
PIRiA36003.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33717 Genomic DNA. Translation: AAA30324.1.
PIRiA36003.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L5PX-ray2.20A/B/C9-100[»]
ProteinModelPortaliP21149.
SMRiP21149.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP21149.

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
SUPFAMiSSF54292. SSF54292. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFER_TRIVA
AccessioniPrimary (citable) accession number: P21149
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: November 2, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

The propeptide may play a role in the targeting of this protein to the organelle.

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.