FER_SILLB
ID FER_SILLB Reviewed; 146 AA.
AC P04669;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Ferredoxin, chloroplastic;
DE Flags: Precursor;
GN Name=PETF;
OS Silene latifolia subsp. alba (White campion) (Lychnis alba).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Caryophyllaceae; Sileneae; Silene;
OC Silene subgen. Behenantha; Silene sect. Melandrium.
OX NCBI_TaxID=52853;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2987875; DOI=10.1093/nar/13.9.3179;
RA Smeekens S., van Binsbergen J., Weisbeek P.J.;
RT "The plant ferredoxin precursor: nucleotide sequence of a full length cDNA
RT clone.";
RL Nucleic Acids Res. 13:3179-3194(1985).
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 -!- SUBUNIT: Forms a complex with heterodimeric ferredoxin-thioredoxin
CC reductase (FTR) and thioredoxin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X02432; CAA26281.1; -; mRNA.
DR PIR; A23011; FEQH.
DR AlphaFoldDB; P04669; -.
DR SMR; P04669; -.
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 2: Evidence at transcript level;
KW 2Fe-2S; Chloroplast; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Plastid; Transit peptide; Transport.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT CHAIN 49..146
FT /note="Ferredoxin, chloroplastic"
FT /id="PRO_0000008838"
FT DOMAIN 51..142
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 88
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 93
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 126
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 146 AA; 15351 MW; E708DAA314B1BB09 CRC64;
MASTLSTLSV SASLLPKQQP MVASSLPTNM GQALFGLKAG SRGRVTAMAT YKVTLITKES
GTVTFDCPDD VYVLDQAEEE GIDLPYSCRA GSCSSCAGKV VAGSVDQSDQ SFLDDDQIEA
GWVLTCAAYP SADVTIETHK EEELTA
