Reviewed, UniProtKB/Swiss-Prot O04090 (FER1_ARATH)

Names and origin

Protein names

Recommended name:
    Ferredoxin-1, chloroplastic
      Short name=AtFd1

Gene names

Name:	FD1
Synonyms:	PETF2
Ordered Locus Names:	At1g10960
ORF Names:	T19D16.12

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	148 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Cofactor	Binds 1 2Fe-2S cluster.
Subcellular location	Plastid › chloroplast.
Tissue specificity	Expressed in leaves. Not detected in roots. Ref.4
Sequence similarities	Belongs to the 2Fe2S plant-type ferredoxin family. Contains 1 2Fe-2S ferredoxin-type domain.
Biophysicochemical properties	Redox potential: E0 is -425 mV.
Sequence caution	The sequence AAL24214.1 differs from that shown. Reason: Erroneous termination at position 119. Translated as Glu.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast stroma Inferred from direct assay. Source: TAIR
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRX3	Q42403	1	EBI-449441,EBI-449157

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 52	52	Chloroplast
	Chain	53 – 148	96	Ferredoxin-1, chloroplastic		PRO_0000008826
Regions
	Domain	55 – 145	91	2Fe-2S ferredoxin-type
Sites
	Metal binding	91	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	96	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	99	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	129	1	Iron-sulfur (2Fe-2S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	O04090-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 9B2809F103FADCEF	FASTA	148	15,897
	10 20 30 40 50 60 MASTALSSAI VSTSFLRRQQ TPISLRSLPF ANTQSLFGLK SSTARGGRVT AMATYKVKFI 70 80 90 100 110 120 TPEGEQEVEC EEDVYVLDAA EEAGLDLPYS CRAGSCSSCA GKVVSGSIDQ SDQSFLDDEQ 130 140 MSEGYVLTCV AYPTSDVVIE THKEEAIM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"A post genomic characterization of Arabidopsis ferredoxins." Hanke G.T., Kimata-Ariga Y., Taniguchi I., Hase T. Plant Physiol. 134:255-264(2004) [PubMed: 14684843] [Abstract] Cited for: TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, GENE FAMILY, NOMENCLATURE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U95973 Genomic DNA. Translation: AAB65481.1. AY058106 mRNA. Translation: AAL24214.1. Sequence problems. AY127948 mRNA. Translation: AAM91047.1. AY086012 mRNA. Translation: AAM63221.1.
IPI	IPI00522921.
PIR	E86243.
RefSeq	NP_172565.1.
UniGene	At.21590 At.71247
3D structure databases
HSSP	HSSP built from PDB template 1GAQ based on UniProtKB P27787.
SMR	O04090. Positions 53-148.
ModBase	Search...
Protein-protein interaction databases
IntAct	O04090. 1 interaction.
Proteomic databases
PRIDE	O04090.
Genome annotation databases
GeneID	837639.
GenomeReviews	Gene locus AT1G10960 in contig CT485782_GR.
KEGG	ath:AT1G10960.
NMPDR	fig|3702.1.peg.1345.
Organism-specific databases
TAIR	At1g10960.
Phylogenomic databases
OMA	O04090. TYKVTLV.
Gene expression databases
ArrayExpress	O04090.
GermOnline	AT1G10960. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR012675. b-grasp_ferredoxin-like. IPR010241. Fdx_pln. IPR001041. Ferredoxin. [Graphical view]
Gene3D	G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
Pfam	PF00111. Fer2. 1 hit. [Graphical view]
TIGRFAMs	TIGR02008. fdx_plant. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FER1_ARATH

Accession

Primary (citable) accession number: O04090
Secondary accession number(s): Q93Z60

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 1, 1997
Last modified:	June 16, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)