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Protein

Ferredoxin-2, chloroplastic

Gene

FD2

Organism
Arabidopsis thaliana (Mouse-ear cress)
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.

Cofactori

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

Redox potential

E0 is -433 mV.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi91 – 911Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi96 – 961Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi99 – 991Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi129 – 1291Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • photosynthetic acclimation Source: TAIR
  • photosynthetic electron transport chain Source: TAIR
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-2, chloroplastic
Short name:
AtFd2
Gene namesi
Name:FD2
Synonyms:PETF, PETF1
Ordered Locus Names:At1g60950
ORF Names:T7P1.9
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G60950.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5252ChloroplastAdd
BLAST
Chaini53 – 14896Ferredoxin-2, chloroplasticPRO_0000008825Add
BLAST

Proteomic databases

PaxDbiP16972.
PRIDEiP16972.

Expressioni

Tissue specificityi

Expressed in leaves. Not detected in roots.1 Publication

Gene expression databases

GenevisibleiP16972. AT.

Interactioni

Subunit structurei

Interacts with PGRL1A and PGRL1B.1 Publication

Protein-protein interaction databases

BioGridi27610. 9 interactions.
IntActiP16972. 3 interactions.
STRINGi3702.AT1G60950.1.

Structurei

3D structure databases

ProteinModelPortaliP16972.
SMRiP16972. Positions 53-148.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiENOG410IYGQ. Eukaryota.
COG0633. LUCA.
HOGENOMiHOG000217152.
InParanoidiP16972.
KOiK02639.
OMAiLEVECDD.
PhylomeDBiP16972.

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.

P16972-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTALSSAI VGTSFIRRSP APISLRSLPS ANTQSLFGLK SGTARGGRVT
60 70 80 90 100
AMATYKVKFI TPEGELEVEC DDDVYVLDAA EEAGIDLPYS CRAGSCSSCA
110 120 130 140
GKVVSGSVDQ SDQSFLDDEQ IGEGFVLTCA AYPTSDVTIE THKEEDIV
Length:148
Mass (Da):15,539
Last modified:August 1, 1990 - v1
Checksum:i0E7EF445BEB23F62
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51370 Genomic DNA. Translation: CAA35754.1.
M35868 mRNA. Translation: AAA32790.1.
AC018908 Genomic DNA. Translation: AAG51652.1.
CP002684 Genomic DNA. Translation: AEE33752.1.
AF324706 mRNA. Translation: AAG40057.1.
AF326885 mRNA. Translation: AAG41467.1.
AF339705 mRNA. Translation: AAK00387.1.
AY093034 mRNA. Translation: AAM13033.1.
AY128936 mRNA. Translation: AAM91336.1.
AK226379 mRNA. Translation: BAE98526.1.
PIRiS09979.
RefSeqiNP_176291.1. NM_104775.2.
UniGeneiAt.47579.

Genome annotation databases

EnsemblPlantsiAT1G60950.1; AT1G60950.1; AT1G60950.
GeneIDi842386.
GrameneiAT1G60950.1; AT1G60950.1; AT1G60950.
KEGGiath:AT1G60950.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51370 Genomic DNA. Translation: CAA35754.1.
M35868 mRNA. Translation: AAA32790.1.
AC018908 Genomic DNA. Translation: AAG51652.1.
CP002684 Genomic DNA. Translation: AEE33752.1.
AF324706 mRNA. Translation: AAG40057.1.
AF326885 mRNA. Translation: AAG41467.1.
AF339705 mRNA. Translation: AAK00387.1.
AY093034 mRNA. Translation: AAM13033.1.
AY128936 mRNA. Translation: AAM91336.1.
AK226379 mRNA. Translation: BAE98526.1.
PIRiS09979.
RefSeqiNP_176291.1. NM_104775.2.
UniGeneiAt.47579.

3D structure databases

ProteinModelPortaliP16972.
SMRiP16972. Positions 53-148.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi27610. 9 interactions.
IntActiP16972. 3 interactions.
STRINGi3702.AT1G60950.1.

Proteomic databases

PaxDbiP16972.
PRIDEiP16972.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G60950.1; AT1G60950.1; AT1G60950.
GeneIDi842386.
GrameneiAT1G60950.1; AT1G60950.1; AT1G60950.
KEGGiath:AT1G60950.

Organism-specific databases

TAIRiAT1G60950.

Phylogenomic databases

eggNOGiENOG410IYGQ. Eukaryota.
COG0633. LUCA.
HOGENOMiHOG000217152.
InParanoidiP16972.
KOiK02639.
OMAiLEVECDD.
PhylomeDBiP16972.

Miscellaneous databases

PROiP16972.

Gene expression databases

GenevisibleiP16972. AT.

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

« Hide 'large scale' publications
  1. "Tissue-specific expression directed by an Arabidopsis thaliana pre-ferredoxin promoter in transgenic tobacco plants."
    Vorst O., van Dam F., Oosterhoff-Teertstra R., Smeekens S., Weisbeek P.
    Plant Mol. Biol. 14:491-499(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Columbia.
  2. "Isolation and characterization of a ferredoxin gene from Arabidopsis thaliana."
    Somers D.E., Caspar T., Quail P.H.
    Plant Physiol. 93:572-577(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  7. "A post genomic characterization of Arabidopsis ferredoxins."
    Hanke G.T., Kimata-Ariga Y., Taniguchi I., Hase T.
    Plant Physiol. 134:255-264(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, GENE FAMILY, NOMENCLATURE.
  8. "A complex containing PGRL1 and PGR5 is involved in the switch between linear and cyclic electron flow in Arabidopsis."
    DalCorso G., Pesaresi P., Masiero S., Aseeva E., Schuenemann D., Finazzi G., Joliot P., Barbato R., Leister D.
    Cell 132:273-285(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PGRL1A AND PGRL1B.
    Strain: cv. Columbia.

Entry informationi

Entry nameiFER2_ARATH
AccessioniPrimary (citable) accession number: P16972
Secondary accession number(s): Q0WWH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: June 8, 2016
This is version 132 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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  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.