FER_SCEFU
ID FER_SCEFU Reviewed; 94 AA.
AC P56408;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Ferredoxin;
OS Scenedesmus fuscus (Green alga) (Chlorella fusca).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Scenedesmaceae; Scenedesmus.
OX NCBI_TaxID=3073;
RN [1]
RP PARTIAL PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS), AND
RP PHOSPHORYLATION AT SER-9.
RX PubMed=10545324; DOI=10.1016/s0969-2126(00)80054-4;
RA Bes M.T., Parisini E., Inda L.A., Saraiva L.M., Peleato M.L.,
RA Sheldrick G.M.;
RT "Crystal structure determination at 1.4-A resolution of ferredoxin from the
RT green alga Chlorella fusca.";
RL Structure 7:1201-1211(1999).
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 -!- SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.
CC {ECO:0000305}.
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DR PIR; A68399; A68399.
DR PDB; 1AWD; X-ray; 1.40 A; A=1-94.
DR PDBsum; 1AWD; -.
DR AlphaFoldDB; P56408; -.
DR SMR; P56408; -.
DR iPTMnet; P56408; -.
DR EvolutionaryTrace; P56408; -.
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; Phosphoprotein;
KW Plastid; Transport.
FT CHAIN 1..94
FT /note="Ferredoxin"
FT /id="PRO_0000189314"
FT DOMAIN 1..91
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 37
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:10545324"
FT BINDING 42
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:10545324"
FT BINDING 45
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:10545324"
FT BINDING 75
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:10545324"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10545324"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1AWD"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:1AWD"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:1AWD"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:1AWD"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:1AWD"
FT HELIX 64..68
FT /evidence="ECO:0007829|PDB:1AWD"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1AWD"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1AWD"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:1AWD"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:1AWD"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:1AWD"
SQ SEQUENCE 94 AA; 10020 MW; D10A4B2FB8490409 CRC64;
YKVTLKTPSG EETIECPEDT YILDAAEEAG LDLPYSCRAG ACSSCAGKVE SGEVDQSDQS
FLDDAQMGKG FVLTCVAYPT SDVTILTHQE AALY