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P27787

- FER1_MAIZE

UniProt

P27787 - FER1_MAIZE

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Protein

Ferredoxin-1, chloroplastic

Gene

FDX1

Organism
Zea mays (Maize)
Status
Reviewed - 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.

Cofactori

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

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

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. electron carrier activity Source: InterPro
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. electron transport chain Source: InterPro
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, chloroplastic
Alternative name(s):
Ferredoxin I
Short name:
Fd I
Gene namesi
Name:FDX1
Synonyms:PFD1
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Organism-specific databases

GrameneiP27787.
MaizeGDBi66392.

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

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

Proteomic databases

ProMEXiP27787.

Interactioni

Protein-protein interaction databases

IntActiP27787. 1 interaction.

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 .
PIRi T03286.
RefSeqi NP_001105345.1. NM_001111875.1.
UniGenei Zm.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GAQ X-ray 2.59 B 53-150 [» ]
3B2F X-ray 1.70 A/B 53-150 [» ]
3W5U X-ray 2.70 B/D/F/H 53-150 [» ]
3W5V X-ray 3.81 B/D 53-150 [» ]
ProteinModelPortali P27787.
SMRi P27787. Positions 53-150.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P27787. 1 interaction.

Proteomic databases

ProMEXi P27787.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 542275.
KEGGi zma:542275.

Organism-specific databases

Gramenei P27787.
MaizeGDBi 66392.

Phylogenomic databases

HOGENOMi HOG000217152.
KOi K02639.

Miscellaneous databases

EvolutionaryTracei P27787.

Family and domain databases

Gene3Di 3.10.20.30. 1 hit.
InterProi IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR010241. Fd_pln.
[Graphical view ]
Pfami PF00111. Fer2. 1 hit.
[Graphical view ]
SUPFAMi SSF54292. SSF54292. 1 hit.
TIGRFAMsi TIGR02008. fdx_plant. 1 hit.
PROSITEi PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].
  2. "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: November 26, 2014
This is version 107 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

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