FER_ARTPT
ID FER_ARTPT Reviewed; 99 AA.
AC P00246;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Ferredoxin;
OS Arthrospira platensis (Spirulina platensis).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Microcoleaceae; Arthrospira.
OX NCBI_TaxID=118562;
RN [1]
RP PROTEIN SEQUENCE OF 2-99.
RX PubMed=817723; DOI=10.1016/0006-291x(76)90940-2;
RA Tanaka M., Haniu M., Yasunobu K.T., Rao K.K., Hall D.O.;
RT "The complete amino acid sequence of the Spirulina platensis ferredoxin.";
RL Biochem. Biophys. Res. Commun. 69:759-765(1976).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=6801028; DOI=10.1093/oxfordjournals.jbchem.a133654;
RA Tsukihara T., Fukuyama K., Nakamura M., Katsube Y., Tanaka N., Kakudo M.,
RA Wada K., Hase T., Matsubara H.;
RT "X-ray analysis of a [2Fe-2S] ferrodoxin from Spirulina platensis. Main
RT chain fold and location of side chains at 2.5-A resolution.";
RL J. Biochem. 90:1763-1773(1981).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RA Fukuyama K., Hase T., Matsumoto S., Tsukihara T., Katsube Y., Tanaka N.,
RA Kakudo M., Wada K., Hase T., Matsubara H.;
RT "Structure of S. platensis [2Fe-2S] ferredoxin and evolution of
RT chloroplast-type ferrodoxins.";
RL Nature 286:522-524(1980).
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 -!- 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 PIR; A00250; FESGAL.
DR PDB; 4FXC; X-ray; 2.50 A; A=2-99.
DR PDBsum; 4FXC; -.
DR AlphaFoldDB; P00246; -.
DR SMR; P00246; -.
DR EvolutionaryTrace; P00246; -.
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; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:817723"
FT CHAIN 2..99
FT /note="Ferredoxin"
FT /id="PRO_0000189371"
FT DOMAIN 4..96
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 42
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 50
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT BINDING 80
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:4FXC"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:4FXC"
FT HELIX 27..33
FT /evidence="ECO:0007829|PDB:4FXC"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:4FXC"
FT STRAND 48..60
FT /evidence="ECO:0007829|PDB:4FXC"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:4FXC"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:4FXC"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:4FXC"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:4FXC"
SQ SEQUENCE 99 AA; 10634 MW; 71F9CA733DB03741 CRC64;
MATYKVTLIN EAEGINETID CDDDTYILDA AEEAGLDLPY SCRAGACSTC AGTITSGTID
QSDQSFLDDD QIEAGYVLTC VAYPTSDCTI KTHQEEGLY