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  <ns1:cria214s11i rdf:about="http://metadb.riken.jp/db/SciNetS_ria214i/cria214s11ria214u2550002050i">
    <ns1:pria214s2i xml:lang="en">PFE1050w</ns1:pria214s2i>
    <ns5:attributionURL rdf:resource="http://www.uniprot.org/uniprot/P50250"/>
    <ns1:pria214s7i rdf:resource="http://metadb.riken.jp/db/SciNetS_ria214i/cria214s11ria214u2682230161i"/>
    <ns8:pria349s10i rdf:resource="http://metadb.riken.jp/db/SciNetS_rib166i/crib166u30rib166u36329i"/>
    <ns1:pria214s9i xml:lang="en">PfSAHH</ns1:pria214s9i>
    <ns1:pria214s4i>479</ns1:pria214s4i>
    <ns1:pria214s9i xml:lang="en">S-adenosyl-L-homocysteine hydrolase</ns1:pria214s9i>
    <ns1:pria214s7i rdf:resource="http://metadb.riken.jp/db/SciNetS_ria214i/cria214s11ria214u2672006106i"/>
    <ns1:pria214s3i xml:lang="en">Adenosylhomocysteine is a competitive inhibitor of S- adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.</ns1:pria214s3i>
    <ns1:pria214s8i xml:lang="en">MVENKSKVKDISLAPFGKMQMEISENEMPGLMRIREEYGKDQPLKNAKITGCLHMTVECALLIETLQKLGAQIRWCSCNIYSTADYAAAAVSTLENVTVFAWKNETLEEYWWCVESALTWGDGDDNGPDMIVDDGGDATLLVHKGVEYEKLYEEKNILPDPEKAKNEEERCFLTLLKNSILKNPKKWTNIAKKIIGVSEETTTGVLRLKKMDKQNELLFTAINVNDAVTKQKYDNVYGCRHSLPDGLMRATDFLISGKIVVICGYGDVGKGCASSMKGLGARVYITEIDPICAIQAVMEGFNVVTLDEIVDKGDFFITCTGNVDVIKLEHLLKMKNNAVVGNIGHFDDEIQVNELFNYKGIHIENVKPQVDRITLPNGNKIIVLARGRLLNLGCATGHPAFVMSFSFCNQTFAQLDLWQNKDTNKYENKVYLLPKHLDEKVALYHLKKLNASLTELDDNQCQFLGVNKSGPFKSNEYRY</ns1:pria214s8i>
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    <rdfs:label xml:lang="en">SAHH_PLAF7</rdfs:label>
    <rdfs:seeAlso rdf:resource="http://database.riken.jp/sw/item/cria214s11ria214u2550002050i"/>
    <ns1:pria214u2i xml:lang="en">PFE1050w</ns1:pria214u2i>
    <ns1:pria214s6i xml:lang="en">Adenosylhomocysteinase</ns1:pria214s6i>
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