ID FER_ARCLA Reviewed; 97 AA.
AC P00223;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 13-SEP-2023, entry version 104.
DE RecName: Full=Ferredoxin;
OS Arctium lappa (Greater burdock) (Lappa major).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC Arctiinae; Arctium.
OX NCBI_TaxID=4217;
RN [1]
RP PROTEIN SEQUENCE.
RA Takruri I.A.H., Gilroy J., Boulter D.;
RT "Amino acid sequence of ferredoxin from Arctium lappa.";
RL Phytochemistry 21:325-327(1982).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 [2Fe-2S] cluster.;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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DR PIR; A00230; FEBQ.
DR AlphaFoldDB; P00223; -.
DR SMR; P00223; -.
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 GO; GO:0006124; P:ferredoxin metabolic process; IEA:UniProt.
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 NCBIfam; TIGR02008; fdx_plant; 1.
DR PANTHER; PTHR43112; FERREDOXIN; 1.
DR PANTHER; PTHR43112:SF3; FERREDOXIN-2, CHLOROPLASTIC; 1.
DR Pfam; PF00111; Fer2; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Chloroplast; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Plastid; Transport.
FT CHAIN 1..97
FT /note="Ferredoxin"
FT /id="PRO_0000189308"
FT DOMAIN 3..93
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 39
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 44
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 77
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT VARIANT 63
FT /note="Y -> F"
SQ SEQUENCE 97 AA; 10425 MW; 7F0063AC7EF40CAD CRC64;
ATYKVTLITP EGKQEFEVPD DVYILDHAAE EVGDLPYSCR AGSCSSCAGK VTAGSVDQSD
GSYLDDDQME AGWVLTCVAY PTSDVTIETH KEEELTA
//
