P16972 (FER2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ferredoxin-2, chloroplastic
Short name=AtFd2

Gene names

Name:	FD2
Synonyms:	PETF, PETF1
Ordered Locus Names:	At1g60950
ORF Names:	T7P1.9

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › 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.
Subunit structure	Interacts with PGRL1A and PGRL1B. Ref.8
Subcellular location	Plastid › chloroplast.
Tissue specificity	Expressed in leaves. Not detected in roots. Ref.7
Sequence similarities	Belongs to the 2Fe2S plant-type ferredoxin family. Contains 1 2Fe-2S ferredoxin-type domain.
Biophysicochemical properties	Redox potential: E0 is -433 mV. Ref.7

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 Reference proteome
Gene Ontology (GO)
Biological process	photosynthetic electron transport chain Inferred from mutant phenotype. Source: TAIR transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast 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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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-2, chloroplastic		PRO_0000008825
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)
	P16972 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 0E7EF445BEB23F62	FASTA	148	15,539
	10 20 30 40 50 60 MASTALSSAI VGTSFIRRSP APISLRSLPS ANTQSLFGLK SGTARGGRVT AMATYKVKFI 70 80 90 100 110 120 TPEGELEVEC DDDVYVLDAA EEAGIDLPYS CRAGSCSSCA GKVVSGSVDQ SDQSFLDDEQ 130 140 IGEGFVLTCA AYPTSDVTIE THKEEDIV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2102830] [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: 16667505] [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: 11130712] [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: 14593172] [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: 14684843] [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: 18243102] [Abstract] Cited for: INTERACTION WITH PGRL1A AND PGRL1B. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00540057.
PIR	S09979.
RefSeq	NP_176291.1. NM_104775.2.
UniGene	At.47579. At.71517. At.71534. At.71943.
3D structure databases
ProteinModelPortal	P16972.
SMR	P16972. Positions 53-148.
ModBase	Search...
Protein-protein interaction databases
IntAct	P16972. 3 interactions.
STRING	P16972.
Proteomic databases
PRIDE	P16972.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G60950.1; AT1G60950.1; AT1G60950.
GeneID	842386.
GenomeReviews	Gene locus AT1G60950 in contig CT485782_GR.
KEGG	ath:AT1G60950.
Organism-specific databases
TAIR	At1g60950.
Phylogenomic databases
eggNOG	euNOG12256.
GeneTree	EPGT00050000007894.
HOGENOM	HBG748855.
InParanoid	P16972.
OMA	TYKVTLI.
PhylomeDB	P16972.
ProtClustDB	PLN03136.
Gene expression databases
ArrayExpress	P16972.
Genevestigator	P16972.
GermOnline	AT1G60950. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR012675. Beta-grasp_ferredoxin-type. IPR010241. Fd_pln. IPR001041. Ferredoxin. [Graphical view]
Gene3D	G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
KO	K02639.
Pfam	PF00111. Fer2. 1 hit. [Graphical view]
SUPFAM	SSF54292. Ferredoxin. 1 hit.
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

FER2_ARATH

Accession

Primary (citable) accession number: P16972
Secondary accession number(s): Q0WWH2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	December 14, 2011
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program