FER1_SPIOL
ID FER1_SPIOL Reviewed; 147 AA.
AC P00221;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Ferredoxin-1, chloroplastic;
DE AltName: Full=Ferredoxin I;
DE Short=Fd I;
DE Flags: Precursor;
GN Name=PETF;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wedel N., Bartling D., Herrmann R.G.;
RT "Analysis of cDNA clones encoding the entire ferredoxin I precursor
RT polypeptide from spinach.";
RL Bot. Acta 101:295-300(1988).
RN [2]
RP PROTEIN SEQUENCE OF 51-147.
RX PubMed=5651327; DOI=10.1016/s0021-9258(18)93507-6;
RA Matsubara H., Sasaki R.M.;
RT "Spinach ferredoxin. II. Typtic, chymotryptic, and thermolytic peptides,
RT and complete amino acid sequence.";
RL J. Biol. Chem. 243:1732-1757(1968).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANT LYS-142.
RX PubMed=10089511; DOI=10.1107/s0907444998005137;
RA Binda C., Coda A., Aliverti A., Zanetti G., Mattevi A.;
RT "Structure of the mutant E92K of [2Fe-2S] ferredoxin I from Spinacia
RT oleracea at 1.7-A resolution.";
RL Acta Crystallogr. D 54:1353-1358(1998).
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 -!- INTERACTION:
CC P00221; P00455: PETH; NbExp=3; IntAct=EBI-864933, EBI-865079;
CC P00221; P12353: psaD; NbExp=2; IntAct=EBI-864933, EBI-864919;
CC P00221; P39458: narB; Xeno; NbExp=2; IntAct=EBI-864933, EBI-932578;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- MISCELLANEOUS: There may be variants with Lys-81 and Met-83 and a
CC possible deletion of Lys-141.
CC -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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DR EMBL; M35660; AAA34028.1; -; mRNA.
DR PIR; S00437; FESP1.
DR PDB; 1A70; X-ray; 1.70 A; A=51-147.
DR PDBsum; 1A70; -.
DR AlphaFoldDB; P00221; -.
DR SMR; P00221; -.
DR IntAct; P00221; 4.
DR OrthoDB; 1557921at2759; -.
DR SABIO-RK; P00221; -.
DR EvolutionaryTrace; P00221; -.
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..50
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:5651327"
FT CHAIN 51..147
FT /note="Ferredoxin-1, chloroplastic"
FT /id="PRO_0000008839"
FT DOMAIN 53..143
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 89
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 94
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 97
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 127
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:1A70"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:1A70"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:1A70"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:1A70"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:1A70"
FT HELIX 116..121
FT /evidence="ECO:0007829|PDB:1A70"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1A70"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1A70"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:1A70"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:1A70"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:1A70"
SQ SEQUENCE 147 AA; 15658 MW; 76045050A0AA8697 CRC64;
MAATTTTMMG MATTFVPKPQ APPMMAALPS NTGRSLFGLK TGSRGGRMTM AAYKVTLVTP
TGNVEFQCPD DVYILDAAEE EGIDLPYSCR AGSCSSCAGK LKTGSLNQDD QSFLDDDQID
EGWVLTCAAY PVSDVTIETH KEEELTA
