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FER_BUMFI
ID   FER_BUMFI               Reviewed;          98 AA.
AC   P13106;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Ferredoxin;
OS   Bumilleriopsis filiformis (Yellow-green alga).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Xanthophyceae;
OC   Mischococcales; Centritractaceae; Bumilleriopsis.
OX   NCBI_TaxID=2835;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6418731;
RA   Inoue K., Hase T., Boeger P., Matsubara H.;
RT   "Amino acid sequence of a ferredoxin from Bumilleriopsis filiformis, a
RT   yellow-green alga: relationship with red algae, protoflorideophyceae, and
RT   filamentous blue-green algae.";
RL   J. Biochem. 94:1451-1455(1983).
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; A28857; FEBF2.
DR   AlphaFoldDB; P13106; -.
DR   SMR; P13106; -.
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; Chloroplast; Direct protein sequencing; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Plastid; Transport.
FT   CHAIN           1..98
FT                   /note="Ferredoxin"
FT                   /id="PRO_0000189311"
FT   DOMAIN          3..95
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         41
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         46
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         49
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         79
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   VARIANT         1
FT                   /note="E -> A"
SQ   SEQUENCE   98 AA;  10620 MW;  E49CCDACA01DD75E CRC64;
     ETYSVTLVNE EKNINAVIKC PDDQFILDAA EEQGIELPYS CRAGACSTCA GKVLSGTIDQ
     SEQSFLDDDQ MGAGFLLTCV AYPTSDCKVQ THAEDDLY
 
 
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