FER_CHLRE
ID FER_CHLRE Reviewed; 126 AA.
AC P07839;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Ferredoxin, chloroplastic;
DE Flags: Precursor;
GN Name=PETF;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8278553; DOI=10.1104/pp.102.4.1349;
RA Stein M., Jacquot J.-P., Miginiac-Maslow M.;
RT "A cDNA clone encoding Chlamydomonas reinhardtii preferredoxin.";
RL Plant Physiol. 102:1349-1350(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RA Stein M., Chedozeau B., Jacquot J.-P.;
RT "Cloning and sequencing of a ferredoxin gene from Chlamydomonas
RT reinhardtii.";
RL (er) Plant Gene Register PGR95-065(1995).
RN [3]
RP PROTEIN SEQUENCE OF 33-126.
RX PubMed=3350005; DOI=10.1111/j.1432-1033.1988.tb13901.x;
RA Schmitter J.-M., Jacquot J.-P., Lamotte-Guery F., Beauvallet C., Dutka S.,
RA Gadal P., Decottignies P.;
RT "Purification, properties and complete amino acid sequence of the
RT ferredoxin from a green alga, Chlamydomonas reinhardtii.";
RL Eur. J. Biochem. 172:405-412(1988).
RN [4]
RP STRUCTURE BY NMR OF 1-32.
RX PubMed=8174712; DOI=10.1016/0014-5793(94)80568-7;
RA Lancelin J.-M., Bally I., Arlaud G.J., Blackledge M., Gans P., Stein M.,
RA Jacquot J.-P.;
RT "NMR structures of ferredoxin chloroplastic transit peptide from
RT Chlamydomonas reinhardtii promoted by trifluoroethanol in aqueous
RT solution.";
RL FEBS Lett. 343:261-266(1994).
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}.
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DR EMBL; U29516; AAC49171.1; -; Genomic_DNA.
DR EMBL; L10349; AAA33085.1; -; mRNA.
DR PIR; T08054; FEKM.
DR RefSeq; XP_001692808.1; XM_001692756.1.
DR PDB; 1FCT; NMR; -; A=1-32.
DR PDB; 2MH7; NMR; -; A=33-126.
DR PDB; 2N0S; NMR; -; B=33-126.
DR PDB; 6KUM; X-ray; 1.40 A; A/B=32-126.
DR PDB; 6KV0; X-ray; 1.40 A; A/B=32-126.
DR PDB; 6LK1; X-ray; 0.90 A; A/B=32-126.
DR PDB; 7AKT; X-ray; 1.11 A; A=33-126.
DR PDBsum; 1FCT; -.
DR PDBsum; 2MH7; -.
DR PDBsum; 2N0S; -.
DR PDBsum; 6KUM; -.
DR PDBsum; 6KV0; -.
DR PDBsum; 6LK1; -.
DR PDBsum; 7AKT; -.
DR AlphaFoldDB; P07839; -.
DR BMRB; P07839; -.
DR SMR; P07839; -.
DR STRING; 3055.EDP03827; -.
DR EnsemblPlants; PNW73294; PNW73294; CHLRE_14g626700v5.
DR GeneID; 5718285; -.
DR Gramene; PNW73294; PNW73294; CHLRE_14g626700v5.
DR KEGG; cre:CHLRE_14g626700v5; -.
DR eggNOG; ENOG502S3RJ; Eukaryota.
DR HOGENOM; CLU_082632_1_1_1; -.
DR OMA; GTCITCV; -.
DR OrthoDB; 1557921at2759; -.
DR EvolutionaryTrace; P07839; -.
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:0051536; F:iron-sulfur cluster binding; IDA:UniProtKB.
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 InterPro; IPR023383; Ferredoxin_transit_pept.
DR Pfam; PF11591; 2Fe-2S_Ferredox; 1.
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..32
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:3350005"
FT CHAIN 33..126
FT /note="Ferredoxin, chloroplastic"
FT /id="PRO_0000008828"
FT DOMAIN 33..123
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 69
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 74
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 77
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 107
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:1FCT"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:1FCT"
FT TURN 19..22
FT /evidence="ECO:0007829|PDB:1FCT"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1FCT"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:6LK1"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:6LK1"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2N0S"
FT HELIX 54..60
FT /evidence="ECO:0007829|PDB:6LK1"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:6KUM"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:6LK1"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:6LK1"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:2N0S"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:6LK1"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:6LK1"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:6LK1"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:6LK1"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:6LK1"
SQ SEQUENCE 126 AA; 13232 MW; 155AFEA9E6F6E411 CRC64;
MAMAMRSTFA ARVGAKPAVR GARPASRMSC MAYKVTLKTP SGDKTIECPA DTYILDAAEE
AGLDLPYSCR AGACSSCAGK VAAGTVDQSD QSFLDDAQMG NGFVLTCVAY PTSDCTIQTH
QEEALY
