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FER5_MAIZE
ID   FER5_MAIZE              Reviewed;         135 AA.
AC   P27789;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Ferredoxin-5, chloroplastic;
DE   AltName: Full=Ferredoxin V;
DE            Short=Fd V;
DE   Flags: Precursor;
GN   Name=FDX5; Synonyms=PFD5;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16668188; DOI=10.1104/pp.96.1.77;
RA   Hase T., Kimatsa Y., Yonekura K., Matsumura T., Sakakibara H.;
RT   "Molecular cloning and differential expression of the maize ferredoxin gene
RT   family.";
RL   Plant Physiol. 96:77-83(1991).
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   EMBL; M73828; AAA33462.1; -; mRNA.
DR   PIR; T03288; T03288.
DR   AlphaFoldDB; P27789; -.
DR   SMR; P27789; -.
DR   STRING; 4577.GRMZM2G122327_P01; -.
DR   PRIDE; P27789; -.
DR   MaizeGDB; 66392; -.
DR   eggNOG; ENOG502S3RJ; Eukaryota.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P27789; baseline and differential.
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   GO; GO:0009416; P:response to light stimulus; IEP:AgBase.
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   2: Evidence at transcript level;
KW   2Fe-2S; Chloroplast; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Plastid; Reference proteome; Transit peptide; Transport.
FT   TRANSIT         1..38
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           39..135
FT                   /note="Ferredoxin-5, chloroplastic"
FT                   /id="PRO_0000008832"
FT   DOMAIN          41..131
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         77
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         82
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         85
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         115
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ   SEQUENCE   135 AA;  14399 MW;  8FA43C41AD4CB976 CRC64;
     MATVLSSPRA PAFSFSLRAA PATTVAMTRG ASSRLRAQAT YNVKLITPEG EVELQVPDDV
     YILDYAEEEG IDLPYSCRAG SCSSCAGKVV SGSLDQSDQS FLDDSQVADG WVLTCVAYPT
     SDVVIETHKE DDLIS
 
 
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