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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi46 – 461Iron-sulfur (2Fe-2S)
Metal bindingi52 – 521Iron-sulfur (2Fe-2S)
Metal bindingi55 – 551Iron-sulfur (2Fe-2S)
Metal bindingi85 – 851Iron-sulfur (2Fe-2S)

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)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 881 PublicationPRO_0000008841
Chaini9 – 10092FerredoxinPRO_0000008842Add
BLAST

Structurei

Secondary structure

1
100
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 156Combined sources
Beta strandi18 – 236Combined sources
Helixi30 – 356Combined sources
Turni36 – 383Combined sources
Beta strandi47 – 526Combined sources
Beta strandi56 – 627Combined sources
Helixi68 – 747Combined sources
Beta strandi81 – 833Combined sources
Helixi84 – 863Combined sources
Helixi91 – 933Combined sources
Beta strandi97 – 993Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L5PX-ray2.20A/B/C9-100[»]
ProteinModelPortaliP21149.
SMRiP21149. Positions 9-100.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21149.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 100922Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Family and domain databases

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1L5PX-ray2.20A/B/C9-100[»]
ProteinModelPortaliP21149.
SMRiP21149. Positions 9-100.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP21149.

Family and domain databases

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...

Publicationsi

  1. "Molecular analysis of the hydrogenosomal ferredoxin of the anaerobic protist Trichomonas vaginalis."
    Johnson P.J., D'Oliveira C.E., Gorrell T.E., Mueller M.
    Proc. Natl. Acad. Sci. U.S.A. 87:6097-6101(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 9-100.
    Strain: ATCC 30001 / NIH-C1.
  2. "The crystal structure of Trichomonas vaginalis ferredoxin provides insight into metronidazole activation."
    Crossnoe C.R., Germanas J.P., LeMagueres P., Mustata G., Krause K.L.
    J. Mol. Biol. 318:503-518(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 9-100.

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: December 9, 2015
This is version 82 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.