FER_APHSA
ID FER_APHSA Reviewed; 97 AA.
AC P00250;
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-1;
DE AltName: Full=Ferredoxin I;
OS Aphanothece sacrum.
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Aphanothecaceae; Aphanothece.
OX NCBI_TaxID=1122;
RN [1]
RP PROTEIN SEQUENCE OF 2-97.
RX PubMed=818078; DOI=10.1093/oxfordjournals.jbchem.a131076;
RA Hase T., Wada K., Matsubara H.;
RT "Amino acid sequence of the major component of Aphanothece sacrum
RT ferredoxin.";
RL J. Biochem. 79:329-343(1976).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=2123937; DOI=10.1016/s0022-2836(05)80330-4;
RA Tsukihara T., Fukuyama K., Mizushima M., Harioka T., Kusunoki M.,
RA Katsube Y., Hase T., Matsubara H.;
RT "Structure of the [2Fe-2S] ferredoxin I from the blue-green alga
RT Aphanothece sacrum at 2.2-A resolution.";
RL J. Mol. Biol. 216:399-410(1990).
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}.
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DR PIR; A00254; FEAH.
DR PDB; 1FXI; X-ray; 2.20 A; A/B/C/D=2-97.
DR PDB; 3AV8; X-ray; 1.46 A; A/B/C/D=2-97.
DR PDBsum; 1FXI; -.
DR PDBsum; 3AV8; -.
DR AlphaFoldDB; P00250; -.
DR SMR; P00250; -.
DR EvolutionaryTrace; P00250; -.
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:818078"
FT CHAIN 2..97
FT /note="Ferredoxin-1"
FT /id="PRO_0000189306"
FT DOMAIN 4..94
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 40
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:2123937"
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:2123937"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:2123937"
FT BINDING 78
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465,
FT ECO:0000269|PubMed:2123937"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:3AV8"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:3AV8"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:3AV8"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:3AV8"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:3AV8"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1FXI"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:3AV8"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:3AV8"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3AV8"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:3AV8"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:3AV8"
SQ SEQUENCE 97 AA; 10440 MW; 425B51114348F549 CRC64;
MASYKVTLKT PDGDNVITVP DDEYILDVAE EEGLDLPYSC RAGACSTCAG KLVSGPAPDE
DQSFLDDDQI QAGYILTCVA YPTGDCVIET HKEEALY