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<entry dataset="Swiss-Prot" created="1986-07-21" modified="2005-05-10">
  <accession>P00221</accession>
  <name>FER1_SPIOL</name>
  <protein>
    <name>Ferredoxin I, chloroplast precursor</name>
    <name>Fd I</name>
  </protein>
  <gene>
    <name type="primary">PETF</name>
  </gene>
  <organism key="1">
    <name type="scientific">Spinacia oleracea</name>
    <name type="common">Spinach</name>
    <dbReference type="NCBI Taxonomy" id="3562" key="2"/>
    <lineage>
      <taxon>Eukaryota</taxon>
      <taxon>Viridiplantae</taxon>
      <taxon>Streptophyta</taxon>
      <taxon>Embryophyta</taxon>
      <taxon>Tracheophyta</taxon>
      <taxon>Spermatophyta</taxon>
      <taxon>Magnoliophyta</taxon>
      <taxon>eudicotyledons</taxon>
      <taxon>core eudicotyledons</taxon>
      <taxon>Caryophyllales</taxon>
      <taxon>Amaranthaceae</taxon>
      <taxon>Spinacia</taxon>
    </lineage>
  </organism>
  <reference key="3">
    <citation type="journal article" date="1988" name="Bot. Acta" volume="101" first="295" last="300">
      <title>Analysis of cDNA clones encoding the entire ferredoxin I precursor polypeptide from spinach.</title>
      <authorList>
        <person name="Wedel N."/>
        <person name="Bartling D."/>
        <person name="Herrmann R.G."/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE.</scope>
  </reference>
  <reference key="4">
    <citation type="journal article" date="1968" name="J. Biol. Chem." volume="243" first="1732" last="1757">
      <title>Spinach ferredoxin. II. Typtic, chymotryptic, and thermolytic peptides, and complete amino acid sequence.</title>
      <authorList>
        <person name="Matsubara H."/>
        <person name="Sasaki R.M."/>
      </authorList>
      <dbReference type="PubMed" id="5651327" key="5"/>
      <dbReference type="MEDLINE" id="68243193" key="6"/>
    </citation>
    <scope>PROTEIN SEQUENCE OF 51-147.</scope>
  </reference>
  <reference key="7">
    <citation type="journal article" date="1998" name="Acta Crystallogr. D" volume="54" first="1353" last="1358">
      <title>Structure of the mutant E92K of [2Fe-2S] ferredoxin I from Spinacia oleracea at 1.7-A resolution.</title>
      <authorList>
        <person name="Binda C."/>
        <person name="Coda A."/>
        <person name="Aliverti A."/>
        <person name="Zanetti G."/>
        <person name="Mattevi A."/>
      </authorList>
      <dbReference type="PubMed" id="10089511" key="8"/>
      <dbReference type="MEDLINE" id="99192680" key="9"/>
      <dbReference type="DOI" id="10.1107/S0907444998005137" key="10"/>
    </citation>
    <scope>X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANT LYS-142.</scope>
  </reference>
  <comment type="function">
    <text>Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions</text>
  </comment>
  <comment type="cofactor">
    <text>Binds 1 2Fe-2S cluster</text>
  </comment>
  <comment type="subcellular location">
    <text>Chloroplast</text>
  </comment>
  <comment type="miscellaneous">
    <text>There may be variants with Lys-81 and Met-83 and a possible deletion of Lys-141</text>
  </comment>
  <comment type="similarity">
    <text>Belongs to the 2Fe2S plant-type ferredoxin family</text>
  </comment>
  <comment type="similarity">
    <text>Contains 1 2Fe-2S ferredoxin-type domain</text>
  </comment>
  <dbReference type="EMBL" id="M35660" key="11">
    <property type="protein sequence ID" value="AAA34028.1"/>
    <property type="molecule type" value="mRNA"/>
  </dbReference>
  <dbReference type="PIR" id="S00437" key="12">
    <property type="entry name" value="FESP1"/>
  </dbReference>
  <dbReference type="PDB" id="1A70" key="13">
    <property type="method" value="X-ray"/>
    <property type="chains" value="@=51-147"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006057" key="14">
    <property type="entry name" value="2Fe2S"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006058" key="15">
    <property type="entry name" value="2Fe2S_fd_BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010241" key="16">
    <property type="entry name" value="Fdx_plant"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001041" key="17">
    <property type="entry name" value="Ferredoxin"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00111" key="18">
    <property type="entry name" value="Fer2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00159" key="19">
    <property type="entry name" value="2FE2SFRDOXIN"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02008" key="20">
    <property type="entry name" value="fdx_plant"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00197" key="21">
    <property type="entry name" value="2FE2S_FER_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51085" key="22">
    <property type="entry name" value="2FE2S_FER_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <keyword id="KW-0001">2Fe-2S</keyword>
  <keyword id="KW-0002">3D-structure</keyword>
  <keyword id="KW-0150">Chloroplast</keyword>
  <keyword id="KW-0903">Direct protein sequencing</keyword>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0809">Transit peptide</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="transit peptide" description="Chloroplast">
    <location>
      <begin position="1"/>
      <end position="50"/>
    </location>
  </feature>
  <feature type="chain" description="Ferredoxin I">
    <location>
      <begin position="51"/>
      <end position="147"/>
    </location>
  </feature>
  <feature type="domain" description="2Fe-2S ferredoxin-type">
    <location>
      <begin position="53"/>
      <end position="143"/>
    </location>
  </feature>
  <feature type="metal ion-binding site" description="Iron-sulfur (2Fe-2S)">
    <location>
      <position position="89"/>
    </location>
  </feature>
  <feature type="metal ion-binding site" description="Iron-sulfur (2Fe-2S)">
    <location>
      <position position="94"/>
    </location>
  </feature>
  <feature type="metal ion-binding site" description="Iron-sulfur (2Fe-2S)">
    <location>
      <position position="97"/>
    </location>
  </feature>
  <feature type="metal ion-binding site" description="Iron-sulfur (2Fe-2S)">
    <location>
      <position position="127"/>
    </location>
  </feature>
  <feature type="strand">
    <location>
      <begin position="52"/>
      <end position="59"/>
    </location>
  </feature>
  <feature type="turn">
    <location>
      <begin position="60"/>
      <end position="61"/>
    </location>
  </feature>
  <feature type="strand">
    <location>
      <begin position="62"/>
      <end position="69"/>
    </location>
  </feature>
  <feature type="turn">
    <location>
      <begin position="70"/>
      <end position="71"/>
    </location>
  </feature>
  <feature type="helix">
    <location>
      <begin position="74"/>
      <end position="80"/>
    </location>
  </feature>
  <feature type="turn">
    <location>
      <begin position="81"/>
      <end position="82"/>
    </location>
  </feature>
  <feature type="turn">
    <location>
      <begin position="96"/>
      <end position="97"/>
    </location>
  </feature>
  <feature type="strand">
    <location>
      <begin position="98"/>
      <end position="103"/>
    </location>
  </feature>
  <feature type="strand">
    <location>
      <begin position="106"/>
      <end position="107"/>
    </location>
  </feature>
  <feature type="turn">
    <location>
      <begin position="109"/>
      <end position="110"/>
    </location>
  </feature>
  <feature type="helix">
    <location>
      <begin position="116"/>
      <end position="121"/>
    </location>
  </feature>
  <feature type="turn">
    <location>
      <position position="122"/>
    </location>
  </feature>
  <feature type="strand">
    <location>
      <begin position="123"/>
      <end position="125"/>
    </location>
  </feature>
  <feature type="helix">
    <location>
      <begin position="126"/>
      <end position="128"/>
    </location>
  </feature>
  <feature type="strand">
    <location>
      <begin position="130"/>
      <end position="131"/>
    </location>
  </feature>
  <feature type="strand">
    <location>
      <begin position="135"/>
      <end position="138"/>
    </location>
  </feature>
  <feature type="helix">
    <location>
      <begin position="142"/>
      <end position="144"/>
    </location>
  </feature>
  <sequence length="147" mass="15658" checksum="76045050A0AA8697" modified="1991-08-01">
MAATTTTMMGMATTFVPKPQAPPMMAALPSNTGRSLFGLKTGSRGGRMTM
AAYKVTLVTPTGNVEFQCPDDVYILDAAEEEGIDLPYSCRAGSCSSCAGK
LKTGSLNQDDQSFLDDDQIDEGWVLTCAAYPVSDVTIETHKEEELTA
</sequence>
</entry>
<copyright>
This Swiss-Prot entry is copyright. It is produced through a collaboration
between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
the European Bioinformatics Institute.  There are no  restrictions on  its
use as long as its content is in no way modified and this statement is not
removed.</copyright>
</uniprot>
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<entry dataset="Swiss-Prot" created="2003-10-10" modified="2005-05-10">
  <accession>Q9ZTS2</accession>
  <name>FER_CAPAN</name>
  <protein>
    <name>Ferredoxin, chloroplast precursor</name>
    <name>PFLP</name>
  </protein>
  <gene>
    <name type="primary">AP1</name>
  </gene>
  <organism key="1">
    <name type="scientific">Capsicum annuum</name>
    <name type="common">Bell pepper</name>
    <dbReference type="NCBI Taxonomy" id="4072" key="2"/>
    <lineage>
      <taxon>Eukaryota</taxon>
      <taxon>Viridiplantae</taxon>
      <taxon>Streptophyta</taxon>
      <taxon>Embryophyta</taxon>
      <taxon>Tracheophyta</taxon>
      <taxon>Spermatophyta</taxon>
      <taxon>Magnoliophyta</taxon>
      <taxon>eudicotyledons</taxon>
      <taxon>core eudicotyledons</taxon>
      <taxon>asterids</taxon>
      <taxon>lamiids</taxon>
      <taxon>Solanales</taxon>
      <taxon>Solanaceae</taxon>
      <taxon>Capsicum</taxon>
    </lineage>
  </organism>
  <reference key="3">
    <citation type="journal article" date="2003" name="Plant Mol. Biol." volume="51" first="913" last="924">
      <title>Ferredoxin from sweet pepper (Capsicum annuum L.) intensifying harpin(pss)-mediated hypersensitive response shows an enhanced production of active oxygen species (AOS).</title>
      <authorList>
        <person name="Dayakar B.V."/>
        <person name="Lin H.-J."/>
        <person name="Chen C.-H."/>
        <person name="Ger M.-J."/>
        <person name="Lee B.-H."/>
        <person name="Pai C.-H."/>
        <person name="Chow D."/>
        <person name="Huang H.-E."/>
        <person name="Hwang S.-Y."/>
        <person name="Chung M.-C."/>
        <person name="Feng T.-Y."/>
      </authorList>
      <dbReference type="PubMed" id="12777051" key="4"/>
      <dbReference type="MEDLINE" id="22661206" key="5"/>
      <dbReference type="DOI" id="10.1023/A:1023061303755" key="6"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION SITE THR-136.</scope>
    <source>
      <strain>cv. ECW</strain>
      <tissue>Leaf</tissue>
    </source>
  </reference>
  <comment type="function" status="By similarity">
    <text>Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions</text>
  </comment>
  <comment type="function">
    <text>Delays the harpin-mediated hypersensitive response</text>
  </comment>
  <comment type="cofactor" status="By similarity">
    <text>Binds 1 2Fe-2S cluster</text>
  </comment>
  <comment type="subcellular location">
    <text>Chloroplast</text>
  </comment>
  <comment type="similarity">
    <text>Belongs to the 2Fe2S plant-type ferredoxin family</text>
  </comment>
  <comment type="similarity">
    <text>Contains 1 2Fe-2S ferredoxin-type domain</text>
  </comment>
  <dbReference type="EMBL" id="AF039662" key="7">
    <property type="protein sequence ID" value="AAD02175.1"/>
    <property type="molecule type" value="mRNA"/>
  </dbReference>
  <dbReference type="HSSP" id="P00221" key="8">
    <property type="pdb accession" value="1A70"/>
  </dbReference>
  <dbReference type="SMR" id="Q9ZTS2" key="9">
    <property type="residue range" value="48-144"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006057" key="10">
    <property type="entry name" value="2Fe2S"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006058" key="11">
    <property type="entry name" value="2Fe2S_fd_BS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR010241" key="12">
    <property type="entry name" value="Fdx_plant"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001041" key="13">
    <property type="entry name" value="Ferredoxin"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00111" key="14">
    <property type="entry name" value="Fer2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00159" key="15">
    <property type="entry name" value="2FE2SFRDOXIN"/>
  </dbReference>
  <dbReference type="TIGRFAMs" id="TIGR02008" key="16">
    <property type="entry name" value="fdx_plant"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00197" key="17">
    <property type="entry name" value="2FE2S_FER_1"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS51085" key="18">
    <property type="entry name" value="2FE2S_FER_2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <keyword id="KW-0001">2Fe-2S</keyword>
  <keyword id="KW-0150">Chloroplast</keyword>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0597">Phosphorylation</keyword>
  <keyword id="KW-0809">Transit peptide</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="transit peptide" description="Chloroplast" status="by similarity">
    <location>
      <begin position="1"/>
      <end position="47"/>
    </location>
  </feature>
  <feature type="chain" description="Ferredoxin">
    <location>
      <begin position="48"/>
      <end position="144"/>
    </location>
  </feature>
  <feature type="domain" description="2Fe-2S ferredoxin-type">
    <location>
      <begin position="50"/>
      <end position="140"/>
    </location>
  </feature>
  <feature type="metal ion-binding site" description="Iron-sulfur (2Fe-2S)" status="by similarity">
    <location>
      <position position="86"/>
    </location>
  </feature>
  <feature type="metal ion-binding site" description="Iron-sulfur (2Fe-2S)" status="by similarity">
    <location>
      <position position="91"/>
    </location>
  </feature>
  <feature type="metal ion-binding site" description="Iron-sulfur (2Fe-2S)" status="by similarity">
    <location>
      <position position="94"/>
    </location>
  </feature>
  <feature type="metal ion-binding site" description="Iron-sulfur (2Fe-2S)" status="by similarity">
    <location>
      <position position="124"/>
    </location>
  </feature>
  <feature type="modified residue" description="Phosphothreonine">
    <location>
      <position position="136"/>
    </location>
  </feature>
  <sequence length="144" mass="15178" checksum="E9763663281D58EB" modified="2003-10-10">
MASVSATMISTSFMPRKPAVTSLKPIPNVGEALFGLKSANGGKVTCMASY
KVKLITPDGPIEFDCPDNVYILDQAEEAGHDLPYSCRAGSCSSCAGKIAG
GAVDQTDGNFLDDDQLEEGWVLTCVAYPQSDVTIETHKEAELVG
</sequence>
</entry>
<copyright>
This Swiss-Prot entry is copyright. It is produced through a collaboration
between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
the European Bioinformatics Institute.  There are no  restrictions on  its
use as long as its content is in no way modified and this statement is not
removed.</copyright>
</uniprot>

