FER1_RAPSA
ID FER1_RAPSA Reviewed; 98 AA.
AC P14936;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Ferredoxin, root R-B1;
OS Raphanus sativus (Radish) (Raphanus raphanistrum var. sativus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Raphanus.
OX NCBI_TaxID=3726;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=cv. Acantiformis Miyashige; TISSUE=White-root;
RX PubMed=2760019; DOI=10.1093/oxfordjournals.jbchem.a122714;
RA Wada K., Onda M., Matsubara H.;
RT "Amino acid sequences of ferredoxin isoproteins from radish roots.";
RL J. Biochem. 105:619-625(1989).
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 -!- MISCELLANEOUS: In radish there are 4 ferredoxins: 2 are root-specific
CC (R-B1 and R-B2), one is present in both leaves and roots (L-A), and
CC there is a minor form which is leaf specific (L-B).
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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DR PIR; JX0084; JX0084.
DR AlphaFoldDB; P14936; -.
DR SMR; P14936; -.
DR PRIDE; P14936; -.
DR Proteomes; UP000504610; Unplaced.
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; Chloroplast; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Plastid; Reference proteome; Transport.
FT CHAIN 1..98
FT /note="Ferredoxin, root R-B1"
FT /id="PRO_0000189358"
FT DOMAIN 4..95
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 41
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 46
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 49
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 79
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT VARIANT 9
FT /note="I -> V"
FT VARIANT 19
FT /note="D -> E"
SQ SEQUENCE 98 AA; 10783 MW; 24D6F2660CB3CF8D CRC64;
SAVYKVKLIG PDGQENEFDV PDDQYILDAA EEAGVDLPYS CRAGACSTCA GKIEKGQVDQ
SDGSFLEDHH FEKGYVLTCV AYPQSDLVIH THKEEELF
