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Protein

Ferredoxin-1, chloroplastic

Gene

FDX1

Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Occupies a key position both for transferring the photoreducing power to Fd-NADP+ oxidoreductase (FNR), hence the formation of NADPH, and for mediating the cyclic electron flow around photosystem I (PSI).1 Publication

Cofactori

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

Redox potential

E0 is -423 mV.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi91 – 911Iron-sulfur (2Fe-2S)
Metal bindingi96 – 961Iron-sulfur (2Fe-2S)
Metal bindingi99 – 991Iron-sulfur (2Fe-2S)
Metal bindingi129 – 1291Iron-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-1, chloroplasticCurated
Alternative name(s):
Ferredoxin I1 Publication
Short name:
Fd I1 Publication
Gene namesi
Name:FDX1Curated
Synonyms:pFD11 Publication
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea
ProteomesiUP000007305 Componenti: Unplaced

Organism-specific databases

GrameneiP27787.
MaizeGDBi66392.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi117 – 1171D → N: Decreased affinity for Fd-NADP(+) oxidoreductase and decreased electron-transfer activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5252Chloroplast1 PublicationAdd
BLAST
Chaini53 – 15098Ferredoxin-1, chloroplasticPRO_0000008830Add
BLAST

Proteomic databases

ProMEXiP27787.

Expressioni

Tissue specificityi

Expressed almost exclusively in mesophyll cells.1 Publication

Interactioni

Protein-protein interaction databases

IntActiP27787. 1 interaction.
STRINGi4577.GRMZM2G122337_P01.

Structurei

Secondary structure

1
150
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi54 – 618Combined sources
Beta strandi64 – 718Combined sources
Beta strandi72 – 743Combined sources
Helixi76 – 827Combined sources
Beta strandi90 – 945Combined sources
Beta strandi100 – 1067Combined sources
Helixi118 – 1225Combined sources
Beta strandi125 – 1273Combined sources
Helixi128 – 1303Combined sources
Beta strandi132 – 1409Combined sources
Helixi144 – 1474Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GAQX-ray2.59B53-150[»]
3B2FX-ray1.70A/B53-150[»]
3W5UX-ray2.70B/D/F/H53-150[»]
3W5VX-ray3.81B/D53-150[»]
ProteinModelPortaliP27787.
SMRiP27787. Positions 53-150.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27787.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 145912Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 2Fe2S plant-type ferredoxin family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000217152.
KOiK02639.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR010241. Fd_pln.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
SUPFAMiSSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR02008. fdx_plant. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P27787-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVLGSPRA PAFFFSSSSL RAAPAPTAVA LPAAKVGIMG RSASSRRRLR
60 70 80 90 100
AQATYNVKLI TPEGEVELQV PDDVYILDQA EEDGIDLPYS CRAGSCSSCA
110 120 130 140 150
GKVVSGSVDQ SDQSYLDDGQ IADGWVLTCH AYPTSDVVIE THKEEELTGA
Length:150
Mass (Da):15,838
Last modified:August 1, 1992 - v1
Checksum:i1AF43354A9BC1D3F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73829 mRNA. Translation: AAA33459.1.
M73830 mRNA. Translation: AAA33460.1.
PIRiT03286.
RefSeqiNP_001105345.1. NM_001111875.1.
UniGeneiZm.2.

Genome annotation databases

GeneIDi542275.
KEGGizma:542275.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73829 mRNA. Translation: AAA33459.1.
M73830 mRNA. Translation: AAA33460.1.
PIRiT03286.
RefSeqiNP_001105345.1. NM_001111875.1.
UniGeneiZm.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GAQX-ray2.59B53-150[»]
3B2FX-ray1.70A/B53-150[»]
3W5UX-ray2.70B/D/F/H53-150[»]
3W5VX-ray3.81B/D53-150[»]
ProteinModelPortaliP27787.
SMRiP27787. Positions 53-150.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP27787. 1 interaction.
STRINGi4577.GRMZM2G122337_P01.

Proteomic databases

ProMEXiP27787.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi542275.
KEGGizma:542275.

Organism-specific databases

GrameneiP27787.
MaizeGDBi66392.

Phylogenomic databases

HOGENOMiHOG000217152.
KOiK02639.

Miscellaneous databases

EvolutionaryTraceiP27787.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR010241. Fd_pln.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
SUPFAMiSSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR02008. fdx_plant. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and differential expression of the maize ferredoxin gene family."
    Hase T., Kimatsa Y., Yonekura K., Matsumura T., Sakakibara H.
    Plant Physiol. 96:77-83(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 53-76.
  2. "Complementary DNA cloning and characterization of ferredoxin localized in bundle-sheath cells of maize leaves."
    Matsumura T., Kimata-Ariga Y., Sakakibara H., Sugiyama T., Murata H., Takao T., Shimonishi Y., Hase T.
    Plant Physiol. 119:481-488(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-117, SUBCELLULAR LOCATION.
    Strain: cv. Golden cross Bantam T51.
  3. "Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP+ reductase."
    Kurisu G., Kusunoki M., Katoh E., Yamazaki T., Teshima K., Onda Y., Kimata-Ariga Y., Hase T.
    Nat. Struct. Biol. 8:117-121(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

Entry informationi

Entry nameiFER1_MAIZE
AccessioniPrimary (citable) accession number: P27787
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: July 22, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.