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    <ns1:pria214s6i xml:lang="en">Glutathione S-transferase F9</ns1:pria214s6i>
    <ns1:pria214u1i xml:lang="en">GSTF7</ns1:pria214u1i>
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    <ns1:pria214u2i xml:lang="en">F7F1.7</ns1:pria214u2i>
    <rdfs:label xml:lang="en">GSTF9_ARATH</rdfs:label>
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    <ns1:pria214u3i xml:lang="en">At2g30860</ns1:pria214u3i>
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    <ns1:pria214s2i xml:lang="en">GSTF9</ns1:pria214s2i>
    <ns1:pria214s8i xml:lang="en">MVLKVYGPHFASPKRALVTLIEKGVAFETIPVDLMKGEHKQPAYLALQPFGTVPAVVDGDYKIFESRAVMRYVAEKYRSQGPDLLGKTVEDRGQVEQWLDVEATTYHPPLLNLTLHIMFASVMGFPSDEKLIKESEEKLAGVLDVYEAHLSKSKYLAGDFVSLADLAHLPFTDYLVGPIGKAYMIKDRKHVSAWWDDISSRPAWKETVAKYSFPA</ns1:pria214s8i>
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    <ns1:pria214u1i xml:lang="en">GLUTTR</ns1:pria214u1i>
    <ns1:pria214s3i xml:lang="en">In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC), and glutathione peroxidase activity toward cumene hydroperoxide and linoleic acid-13-hydroperoxide. May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.</ns1:pria214s3i>
    <ns1:pria214s9i xml:lang="en">AtGSTF7</ns1:pria214s9i>
    <ns1:pria214s4i>215</ns1:pria214s4i>
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    <ns1:pria214s9i xml:lang="en">GST class-phi member 9</ns1:pria214s9i>
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