ID FER3_MAIZE Reviewed; 152 AA.
AC P27788;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 27-MAR-2024, entry version 145.
DE RecName: Full=Ferredoxin-3, chloroplastic;
DE AltName: Full=Ferredoxin III;
DE Short=Fd III;
DE Flags: Precursor;
GN Name=FDX3; Synonyms=PFD3;
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.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9399441; DOI=10.1093/oxfordjournals.pcp.a029102;
RA Nakano R., Matsumura T., Sakakibara H., Sugiyama T., Hase T.;
RT "Cloning of maize ferredoxin III gene: presence of a unique repetitive
RT nucleotide sequence within an intron found in the 5'-untranslated region.";
RL Plant Cell Physiol. 38:1167-1170(1997).
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}.
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 EMBL; M73831; AAA33461.1; -; mRNA.
DR EMBL; AB001387; BAA19251.1; -; Genomic_DNA.
DR PIR; T02881; T02881.
DR RefSeq; NP_001105346.1; NM_001111876.1.
DR RefSeq; XP_008648612.1; XM_008650390.1.
DR PDB; 5H57; X-ray; 2.50 A; A/B/C/D/E/F=56-152.
DR PDB; 5H5J; X-ray; 2.50 A; B=56-152.
DR PDBsum; 5H57; -.
DR PDBsum; 5H5J; -.
DR AlphaFoldDB; P27788; -.
DR SMR; P27788; -.
DR STRING; 4577.P27788; -.
DR EnsemblPlants; Zm00001eb063710_T001; Zm00001eb063710_P001; Zm00001eb063710.
DR EnsemblPlants; Zm00001eb063710_T002; Zm00001eb063710_P002; Zm00001eb063710.
DR Gramene; Zm00001eb063710_T001; Zm00001eb063710_P001; Zm00001eb063710.
DR Gramene; Zm00001eb063710_T002; Zm00001eb063710_P002; Zm00001eb063710.
DR MaizeGDB; 66392; -.
DR HOGENOM; CLU_082632_1_2_1; -.
DR InParanoid; P27788; -.
DR OMA; CALFKSP; -.
DR OrthoDB; 312286at2759; -.
DR SABIO-RK; P27788; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; P27788; baseline and differential.
DR Genevisible; P27788; ZM.
DR GO; GO:0009507; C:chloroplast; TAS:AgBase.
DR GO; GO:0009570; C:chloroplast stroma; IDA:AgBase.
DR GO; GO:0009578; C:etioplast stroma; IDA:AgBase.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:AgBase.
DR GO; GO:0009055; F:electron transfer activity; IDA:AgBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022900; P:electron transport chain; IDA: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 NCBIfam; TIGR02008; fdx_plant; 1.
DR PANTHER; PTHR43112; FERREDOXIN; 1.
DR PANTHER; PTHR43112:SF30; FERREDOXIN-3, CHLOROPLASTIC; 1.
DR Pfam; PF00111; Fer2; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 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; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Plastid; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 56..152
FT /note="Ferredoxin-3, chloroplastic"
FT /id="PRO_0000008831"
FT DOMAIN 58..149
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 95
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 100
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 103
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 133
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:5H57"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:5H57"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:5H57"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:5H57"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:5H57"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:5H57"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:5H57"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:5H57"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:5H57"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:5H57"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:5H57"
SQ SEQUENCE 152 AA; 16123 MW; 3D6CBC4B8238EFA0 CRC64;
MSTSTFATSC TLLGNVRTTQ ASQTAVKSPS SLSFFSQVTK VPSLKTSKKL DVSAMAVYKV
KLVGPEGEEH EFDAPDDAYI LDAAETAGVE LPYSCRAGAC STCAGKIESG SVDQSDGSFL
DDGQQEEGYV LTCVSYPKSD CVIHTHKEGD LY
//
