FER1_HYONI
ID FER1_HYONI Reviewed; 97 AA.
AC P84873;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Ferredoxin-1;
DE AltName: Full=Major ferredoxin;
OS Hyoscyamus niger (Black henbane).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Hyoscyameae;
OC Hyoscyamus.
OX NCBI_TaxID=4079;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RC TISSUE=Leaf {ECO:0000269|PubMed:16079510};
RX PubMed=16079510; DOI=10.1248/bpb.28.1535;
RA Mino Y., Yukita M., Hiratsuka N., Wariishi H.;
RT "Amino acid sequences of ferredoxins from Atropa belladonna and Hyoscyamus
RT niger: their similarities to those in other tropane-alkaloid-containing
RT plants.";
RL Biol. Pharm. Bull. 28:1535-1538(2005).
CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons
CC in a wide variety of metabolic reactions. {ECO:0000305}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000255}.
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DR AlphaFoldDB; P84873; -.
DR SMR; P84873; -.
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 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; Chloroplast; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Plastid; Transport.
FT CHAIN 1..97
FT /note="Ferredoxin-1"
FT /id="PRO_0000245100"
FT DOMAIN 3..93
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000250|UniProtKB:P0A3C8,
FT ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 39
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A3C8,
FT ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 44
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A3C8,
FT ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A3C8,
FT ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 77
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A3C8,
FT ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 97 AA; 10393 MW; 55AAA3D0F458D39C CRC64;
ATYKVKLVTP DGPVEFNCPD DVYILDQAEE EGHELPYSCR AGSCSSCAGK VSAGTVDQSD
GNFLDDDQIA DGFVLTCVAY PQSDVTIETH KEEDLTG
