FER1_PEA
ID FER1_PEA Reviewed; 149 AA.
AC P09911;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Ferredoxin-1, chloroplastic;
DE AltName: Full=Ferredoxin I;
DE Flags: Precursor;
GN Name=PETF; Synonyms=FED1;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Alaska;
RX PubMed=2535518; DOI=10.2307/3868958;
RA Elliott R.C., Pedersen T.J., Fristensky B.W., White M.J., Dickey L.F.,
RA Thompson W.F.;
RT "Characterization of a single copy gene encoding ferredoxin I from pea.";
RL Plant Cell 1:681-690(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-135.
RC STRAIN=cv. Alaska;
RA Dobres M.S., Elliott R.C., Watson J.C., Thompson W.F.;
RT "A phytochrome regulated pea transcript encodes ferredoxin I.";
RL Plant Mol. Biol. 8:53-59(1987).
RN [3]
RP PROTEIN SEQUENCE OF 53-89, AND FUNCTION.
RC STRAIN=cv. Onward;
RX DOI=10.1093/jxb/31.2.379;
RA Dutton J.E., Rogers L.J., Haslett B.G., Takruri I.A.H., Gleaves J.T.,
RA Boulter D.;
RT "Comparative studies on the properties of two ferredoxins from Pisum
RT sativum L.";
RL J. Exp. Bot. 31:379-391(1980).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions. {ECO:0000269|Ref.3}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 [2Fe-2S] cluster.;
CC -!- SUBUNIT: Forms a complex with heterodimeric ferredoxin-thioredoxin
CC reductase (FTR) and thioredoxin. {ECO:0000250}.
CC -!- INTERACTION:
CC P09911; P10933: PETH; NbExp=3; IntAct=EBI-931449, EBI-931306;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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DR EMBL; M31713; AAA33665.1; -; Genomic_DNA.
DR EMBL; M17107; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S11495; FEPM1.
DR PDB; 6YAC; EM; 2.50 A; N=53-149.
DR PDB; 6YEZ; EM; 2.70 A; N=53-149.
DR PDBsum; 6YAC; -.
DR PDBsum; 6YEZ; -.
DR AlphaFoldDB; P09911; -.
DR SMR; P09911; -.
DR DIP; DIP-384N; -.
DR IntAct; P09911; 2.
DR MINT; P09911; -.
DR EnsemblPlants; Psat3g090040.1; Psat3g090040.1.cds1; Psat3g090040.
DR Gramene; Psat3g090040.1; Psat3g090040.1.cds1; Psat3g090040.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR010241; Fd_pln.
DR Pfam; PF00111; Fer2; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR TIGRFAMs; TIGR02008; fdx_plant; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Chloroplast; Direct protein sequencing;
KW Electron transport; Iron; Iron-sulfur; Metal-binding; Plastid;
KW Transit peptide; Transport.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 53..149
FT /note="Ferredoxin-1, chloroplastic"
FT /id="PRO_0000008836"
FT DOMAIN 55..145
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 91
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 96
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 99
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 129
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT VARIANT 59
FT /note="L -> I (in strain: cv. Onward)"
FT VARIANT 85
FT /note="I -> L (in strain: cv. Onward)"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:6YAC"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:6YAC"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:6YAC"
FT STRAND 92..101
FT /evidence="ECO:0007829|PDB:6YAC"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:6YAC"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:6YEZ"
FT TURN 118..122
FT /evidence="ECO:0007829|PDB:6YAC"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:6YAC"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:6YAC"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:6YAC"
SQ SEQUENCE 149 AA; 15804 MW; 517ECE23CA85DC48 CRC64;
MATTPALYGT AVSTSFLRTQ PMPMSVTTTK AFSNGFLGLK TSLKRGDLAV AMASYKVKLV
TPDGTQEFEC PSDVYILDHA EEVGIDLPYS CRAGSCSSCA GKVVGGEVDQ SDGSFLDDEQ
IEAGFVLTCV AYPTSDVVIE THKEEDLTA
