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<entry dataset="Swiss-Prot" created="2001-11-16" modified="2026-09-02" version="139" xmlns="http://uniprot.org/uniprot">
  <accession>Q9R6T9</accession>
  <accession>A5GIQ3</accession>
  <name>PSAB_SYNPW</name>
  <protein>
    <recommendedName>
      <fullName evidence="1">Photosystem I P700 chlorophyll a apoprotein A2</fullName>
      <ecNumber evidence="1">1.97.1.12</ecNumber>
    </recommendedName>
    <alternativeName>
      <fullName evidence="1">PsaB</fullName>
    </alternativeName>
  </protein>
  <gene>
    <name evidence="1" type="primary">psaB</name>
    <name type="ordered locus">SynWH7803_0392</name>
  </gene>
  <organism>
    <name type="scientific">Synechococcus sp. (strain WH7803)</name>
    <dbReference type="NCBI Taxonomy" id="32051"/>
    <lineage>
      <taxon>Bacteria</taxon>
      <taxon>Bacillati</taxon>
      <taxon>Cyanobacteriota</taxon>
      <taxon>Cyanophyceae</taxon>
      <taxon>Synechococcales</taxon>
      <taxon>Synechococcaceae</taxon>
      <taxon>Synechococcus</taxon>
    </lineage>
  </organism>
  <reference key="1">
    <citation type="journal article" date="2000" name="Photosyn. Res." volume="65" first="131" last="139">
      <title>Rapid evolutionary divergence of photosystem I core subunits PsaA and PsaB in the marine prokaryote Prochlorococcus.</title>
      <authorList>
        <person name="van der Staay G.W.M."/>
        <person name="Moon-van der Staay S.Y."/>
        <person name="Garczarek L."/>
        <person name="Partensky F."/>
      </authorList>
      <dbReference type="PubMed" id="16228480"/>
      <dbReference type="DOI" id="10.1023/a:1006445810996"/>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
  </reference>
  <reference key="2">
    <citation type="submission" date="2006-05" db="EMBL/GenBank/DDBJ databases">
      <authorList>
        <consortium name="Genoscope"/>
      </authorList>
    </citation>
    <scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
    <source>
      <strain>WH7803</strain>
    </source>
  </reference>
  <comment type="function">
    <text evidence="1">PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6.</text>
  </comment>
  <comment type="catalytic activity">
    <reaction evidence="1">
      <text>reduced [plastocyanin] + hnu + oxidized [2Fe-2S]-[ferredoxin] = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin]</text>
      <dbReference type="Rhea" id="RHEA:30407"/>
      <dbReference type="Rhea" id="RHEA-COMP:10000"/>
      <dbReference type="Rhea" id="RHEA-COMP:10001"/>
      <dbReference type="Rhea" id="RHEA-COMP:10039"/>
      <dbReference type="Rhea" id="RHEA-COMP:10040"/>
      <dbReference type="ChEBI" id="CHEBI:29036"/>
      <dbReference type="ChEBI" id="CHEBI:30212"/>
      <dbReference type="ChEBI" id="CHEBI:33737"/>
      <dbReference type="ChEBI" id="CHEBI:33738"/>
      <dbReference type="ChEBI" id="CHEBI:49552"/>
      <dbReference type="EC" id="1.97.1.12"/>
    </reaction>
  </comment>
  <comment type="cofactor">
    <text evidence="1">PSI electron transfer chain: 5 chlorophyll a, 1 chlorophyll a', 2 phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 chlorophyll a, 22 carotenoids, 3 phospholipids and 1 galactolipid. P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.</text>
  </comment>
  <comment type="subunit">
    <text evidence="1">The PsaA/B heterodimer binds the P700 chlorophyll special pair and subsequent electron acceptors. PSI consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The cyanobacterial PSI reaction center is composed of one copy each of PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric complexes.</text>
  </comment>
  <comment type="subcellular location">
    <subcellularLocation>
      <location evidence="1">Cellular thylakoid membrane</location>
      <topology evidence="1">Multi-pass membrane protein</topology>
    </subcellularLocation>
  </comment>
  <comment type="similarity">
    <text evidence="1">Belongs to the PsaA/PsaB family.</text>
  </comment>
  <dbReference type="EC" id="1.97.1.12" evidence="1"/>
  <dbReference type="EMBL" id="AJ133190">
    <property type="protein sequence ID" value="CAB64209.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="EMBL" id="CT971583">
    <property type="protein sequence ID" value="CAK22818.1"/>
    <property type="molecule type" value="Genomic_DNA"/>
  </dbReference>
  <dbReference type="AlphaFoldDB" id="Q9R6T9"/>
  <dbReference type="SMR" id="Q9R6T9"/>
  <dbReference type="STRING" id="32051.SynWH7803_0392"/>
  <dbReference type="KEGG" id="syx:SynWH7803_0392"/>
  <dbReference type="eggNOG" id="COG2885">
    <property type="taxonomic scope" value="Bacteria"/>
  </dbReference>
  <dbReference type="HOGENOM" id="CLU_016126_1_0_3"/>
  <dbReference type="OrthoDB" id="499313at2"/>
  <dbReference type="Proteomes" id="UP000001566">
    <property type="component" value="Chromosome"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009522">
    <property type="term" value="C:photosystem I"/>
    <property type="evidence" value="ECO:0000501"/>
    <property type="project" value="InterPro"/>
  </dbReference>
  <dbReference type="GO" id="GO:0031676">
    <property type="term" value="C:plasma membrane-derived thylakoid membrane"/>
    <property type="evidence" value="ECO:0000501"/>
    <property type="project" value="UniProtKB-SubCell"/>
  </dbReference>
  <dbReference type="GO" id="GO:0009055">
    <property type="term" value="F:electron transfer activity"/>
    <property type="evidence" value="ECO:0000501"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0000287">
    <property type="term" value="F:magnesium ion binding"/>
    <property type="evidence" value="ECO:0000501"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="GO" id="GO:0015979">
    <property type="term" value="P:photosynthesis"/>
    <property type="evidence" value="ECO:0000501"/>
    <property type="project" value="UniProtKB-UniRule"/>
  </dbReference>
  <dbReference type="FunFam" id="1.20.1130.10:FF:000001">
    <property type="entry name" value="Photosystem I P700 chlorophyll a apoprotein A2"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Gene3D" id="1.20.1130.10">
    <property type="entry name" value="Photosystem I PsaA/PsaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="HAMAP" id="MF_00482">
    <property type="entry name" value="PSI_PsaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR001280">
    <property type="entry name" value="PSI_PsaA/B"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR020586">
    <property type="entry name" value="PSI_PsaA/B_CS"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR036408">
    <property type="entry name" value="PSI_PsaA/B_sf"/>
  </dbReference>
  <dbReference type="InterPro" id="IPR006244">
    <property type="entry name" value="PSI_PsaB"/>
  </dbReference>
  <dbReference type="NCBIfam" id="TIGR01336">
    <property type="entry name" value="psaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30128">
    <property type="entry name" value="OUTER MEMBRANE PROTEIN, OMPA-RELATED"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PANTHER" id="PTHR30128:SF19">
    <property type="entry name" value="PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A1-RELATED"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="Pfam" id="PF00223">
    <property type="entry name" value="PsaA_PsaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PIRSF" id="PIRSF002905">
    <property type="entry name" value="PSI_A"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PRINTS" id="PR00257">
    <property type="entry name" value="PHOTSYSPSAAB"/>
  </dbReference>
  <dbReference type="SUPFAM" id="SSF81558">
    <property type="entry name" value="Photosystem I subunits PsaA/PsaB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <dbReference type="PROSITE" id="PS00419">
    <property type="entry name" value="PHOTOSYSTEM_I_PSAAB"/>
    <property type="match status" value="1"/>
  </dbReference>
  <proteinExistence type="inferred from homology"/>
  <keyword id="KW-0004">4Fe-4S</keyword>
  <keyword id="KW-0148">Chlorophyll</keyword>
  <keyword id="KW-0157">Chromophore</keyword>
  <keyword id="KW-0249">Electron transport</keyword>
  <keyword id="KW-0408">Iron</keyword>
  <keyword id="KW-0411">Iron-sulfur</keyword>
  <keyword id="KW-0460">Magnesium</keyword>
  <keyword id="KW-0472">Membrane</keyword>
  <keyword id="KW-0479">Metal-binding</keyword>
  <keyword id="KW-0560">Oxidoreductase</keyword>
  <keyword id="KW-0602">Photosynthesis</keyword>
  <keyword id="KW-0603">Photosystem I</keyword>
  <keyword id="KW-1185">Reference proteome</keyword>
  <keyword id="KW-0793">Thylakoid</keyword>
  <keyword id="KW-0812">Transmembrane</keyword>
  <keyword id="KW-1133">Transmembrane helix</keyword>
  <keyword id="KW-0813">Transport</keyword>
  <feature type="chain" id="PRO_0000088656" description="Photosystem I P700 chlorophyll a apoprotein A2">
    <location>
      <begin position="1"/>
      <end position="738"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=I" evidence="1">
    <location>
      <begin position="46"/>
      <end position="69"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=II" evidence="1">
    <location>
      <begin position="135"/>
      <end position="158"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=III" evidence="1">
    <location>
      <begin position="175"/>
      <end position="199"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=IV" evidence="1">
    <location>
      <begin position="273"/>
      <end position="291"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=V" evidence="1">
    <location>
      <begin position="333"/>
      <end position="356"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=VI" evidence="1">
    <location>
      <begin position="372"/>
      <end position="398"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=VII" evidence="1">
    <location>
      <begin position="420"/>
      <end position="442"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=VIII" evidence="1">
    <location>
      <begin position="521"/>
      <end position="539"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=IX" evidence="1">
    <location>
      <begin position="579"/>
      <end position="600"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=X" evidence="1">
    <location>
      <begin position="647"/>
      <end position="669"/>
    </location>
  </feature>
  <feature type="transmembrane region" description="Helical; Name=XI" evidence="1">
    <location>
      <begin position="711"/>
      <end position="731"/>
    </location>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="563"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="572"/>
    </location>
    <ligand>
      <name>[4Fe-4S] cluster</name>
      <dbReference type="ChEBI" id="CHEBI:49883"/>
      <note>ligand shared between dimeric partners</note>
    </ligand>
  </feature>
  <feature type="binding site" description="axial binding residue" evidence="1">
    <location>
      <position position="658"/>
    </location>
    <ligand>
      <name>chlorophyll a</name>
      <dbReference type="ChEBI" id="CHEBI:58416"/>
      <label>B1</label>
    </ligand>
    <ligandPart>
      <name>Mg</name>
      <dbReference type="ChEBI" id="CHEBI:25107"/>
    </ligandPart>
  </feature>
  <feature type="binding site" description="axial binding residue" evidence="1">
    <location>
      <position position="666"/>
    </location>
    <ligand>
      <name>chlorophyll a</name>
      <dbReference type="ChEBI" id="CHEBI:58416"/>
      <label>B3</label>
    </ligand>
    <ligandPart>
      <name>Mg</name>
      <dbReference type="ChEBI" id="CHEBI:25107"/>
    </ligandPart>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="674"/>
    </location>
    <ligand>
      <name>chlorophyll a</name>
      <dbReference type="ChEBI" id="CHEBI:58416"/>
      <label>B3</label>
    </ligand>
  </feature>
  <feature type="binding site" evidence="1">
    <location>
      <position position="675"/>
    </location>
    <ligand>
      <name>phylloquinone</name>
      <dbReference type="ChEBI" id="CHEBI:18067"/>
      <label>B</label>
    </ligand>
  </feature>
  <evidence type="ECO:0000255" key="1">
    <source>
      <dbReference type="HAMAP-Rule" id="MF_00482"/>
    </source>
  </evidence>
  <sequence length="738" mass="81818" checksum="B47FEE66CE669ACF" modified="2000-05-01" version="1">MATKFPSFSQGLAQDPTTRRIWYGIATAHDFESHDGMTEEKLYQKLFSTHFGHLAIIGLWVSGNLFHIAWQGNFEQWVADPLHVRPIAHAIWDPHFGQGAIDAFTQAGASSPVNIAYSGLYHWFYTIGMTTNAELYQGSIFMMILSAWALFAGWLHLQPKFRPSLAWFKNAESRLNHHLAVLFGFSSIAWTGHLVHVAIPESRGQHVGWDNFLNVMPHPAGLGPFFTGNWGVYAQNPDTMGQVFGSAEGSGTAILTFLGGFHPQTEALWLTDIAHHHLAIGVIFVIAGHMYRTNFGIGHSIREILEAHNPPQGTPGDLGAGHKGLYDTINNSLHFQLGLALASLGVVTSLVAQHMYAMPSYAFIAKDYTTQAALYTHHQYIAIFLMCGAFAHGAIFFIRDYDPEANKDNVLARMLEHKEAIISHLSWVSLFLGFHTLGLYVHNDVVVAFGTPEKQILVEPVFAQFVQAASGKAIYGFDVLLANTGGVAANANAAYMGGWMDAINGVRGSNDLFLPIGPGDFLVHHAIALGLHTTTLILVKGALDARGSKLMPDKKDFGYSFPCDGPGRGGTCDISAWDAFYLAVFWALNTVGWVTFYWHWKHLAIWQGNVAQFNESSTYLMGWFRDYLWLNSSQLINGYNPFGSNNLAVWAWMFLFGHLVWATGFMFLISWRGYWQELIETIVWAHQRTPLANLVGWRDKPVALSIVQARVVGLAHFTIGYILTYAAFLIASTSGKFG</sequence>
</entry>
<copyright>
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms Distributed under the Creative Commons Attribution (CC BY 4.0) License
</copyright>
</uniprot>