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Protein

Ferredoxin-1, chloroplastic

Gene

FDX1

Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: Annotation score: 5 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

Manual assertion based on experiment ini

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi91Iron-sulfur (2Fe-2S)1
Metal bindingi96Iron-sulfur (2Fe-2S)1
Metal bindingi99Iron-sulfur (2Fe-2S)1
Metal bindingi129Iron-sulfur (2Fe-2S)1

GO - Molecular functioni

  • 2 iron, 2 sulfur cluster binding Source: AgBase
  • electron carrier activity Source: AgBase
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • electron transport chain Source: AgBase
  • response to light stimulus Source: AgBase

Keywordsi

Biological processElectron transport, Transport
Ligand2Fe-2S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

SABIO-RKiP27787.

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 cladePanicoideaeAndropogonodaeAndropogoneaeTripsacinaeZea
Proteomesi
  • UP000007305 Componenti: Unplaced

Organism-specific databases

MaizeGDBi66392.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: AgBase
  • chloroplast stroma Source: AgBase

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi117D → N: Decreased affinity for Fd-NADP(+) oxidoreductase and decreased electron-transfer activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 52Chloroplast1 PublicationAdd BLAST52
ChainiPRO_000000883053 – 150Ferredoxin-1, chloroplasticAdd BLAST98

Proteomic databases

PaxDbiP27787.
ProMEXiP27787.

Expressioni

Tissue specificityi

Expressed almost exclusively in mesophyll cells.1 Publication

Interactioni

Protein-protein interaction databases

IntActiP27787. 1 interactor.
STRINGi4577.GRMZM2G122337_P01.

Structurei

Secondary structure

1150
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi54 – 61Combined sources8
Beta strandi64 – 71Combined sources8
Beta strandi72 – 74Combined sources3
Helixi76 – 82Combined sources7
Beta strandi90 – 94Combined sources5
Beta strandi100 – 106Combined sources7
Helixi118 – 122Combined sources5
Beta strandi125 – 127Combined sources3
Helixi128 – 130Combined sources3
Beta strandi132 – 140Combined sources9
Helixi144 – 147Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GAQX-ray2.59B53-150[»]
3B2FX-ray1.70A/B53-150[»]
3W5UX-ray2.70B/D/F/H53-150[»]
3W5VX-ray3.81B/D53-150[»]
5H8YX-ray2.20E/F53-150[»]
5H92X-ray2.08C53-150[»]
ProteinModelPortaliP27787.
SMRiP27787.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27787.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini55 – 1452Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST91

Sequence similaritiesi

Belongs to the 2Fe2S plant-type ferredoxin family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IYGQ. Eukaryota.
COG0633. LUCA.
HOGENOMiHOG000217152.
KOiK02639.

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di3.10.20.30. 1 hit.
InterProiView protein in InterPro
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR010241. Fd_pln.
PfamiView protein in Pfam
PF00111. Fer2. 1 hit.
SUPFAMiSSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR02008. fdx_plant. 1 hit.
PROSITEiView protein in PROSITE
PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.

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.

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.

Entry informationi

Entry nameiFER1_MAIZE
AccessioniPrimary (citable) accession number: P27787
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: February 15, 2017
This is version 123 of the entry and version 1 of the sequence. See 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