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CATH Superfamily 3.30.360.10

Dihydrodipicolinate Reductase; domain 2

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Dihydrodipicolinate Reductase; domain 2
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 24332: Alpha-aminoadipic semialdehyde synthase, mitochond...

There are 7 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Saccharopine dehydrogenase (NADP(+), L-glutamate-forming). [EC: 1.5.1.10]
N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NADP(+) + H(2)O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH.
    		 68 A0A060TBC7 A0A060TBC7 A0A084GH64 A0A084GH64 A0A0F4YTX1 A0A0F4YTX1 A0A0F8DHK5 A0A0F8DHK5 A0A0G2RK33 A0A0G2RK33
    (58 more...)
    Saccharopine dehydrogenase (NADP(+), L-lysine-forming). [EC: 1.5.1.8]
    N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NADP(+) + H(2)O = L-lysine + 2-oxoglutarate + NADPH.
      		 22 A0A084GH64 A0A084GH64 A2QB21 A2QB21 A2VCW9 A2VCW9 A4D0W4 A4D0W4 A8E657 A8E657
      (12 more...)
      Saccharopine dehydrogenase (NAD(+), L-glutamate-forming). [EC: 1.5.1.9]
      N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NAD(+) + H(2)O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADH.
        		 14 A0A084GH64 A0A084GH64 A2VCW9 A2VCW9 A4D0W4 A4D0W4 A8E657 A8E657 Q3UEQ9 Q3UEQ9
        (4 more...)
        Saccharopine dehydrogenase (NAD(+), L-lysine-forming). [EC: 1.5.1.7]
        N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NAD(+) + H(2)O = L-lysine + 2-oxoglutarate + NADH.
          		 8 A0A0J5PEL4 A0A0J5PEL4 B0Y6W5 B0Y6W5 Q4WQ27 Q4WQ27 Q9VLX0 Q9VLX0
          Spermidine synthase. [EC: 2.5.1.16]
          S-adenosyl 3-(methylthio)propylamine + putrescine = 5'-S-methyl- 5'-thioadenosine + spermidine.
          • The enzymes from the plant Glycine max and from mammalia are highly specific for putrescine as the amine acceptor.
          • The enzymes from the bacteria Escherichia coli and Thermotoga maritima prefer putrescine but are more tolerant toward other amine acceptors, such as spermidine and cadaverine.
          • Cf. EC 2.5.1.22 and EC 2.5.1.23.
          		 6 A0A0B7FLP5 A0A0B7FLP5 A0A0L6VJ40 A0A0L6VJ40 B0CXB5 B0CXB5
          Endo-1,4-beta-xylanase. [EC: 3.2.1.8]
          Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
            		 2 A0A166QX06 A0A166QX06
            Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific). [EC: 2.5.1.87]
            (2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = n diphosphate + ditrans,polycis-polyprenyl diphosphate (n = 10-55).
            • The enzyme is involved in biosynthesis of dolichol (a long-chain polyprenol) with a saturated alpha-isoprene unit, which serves as a glycosyl carrier in protein glycosylation.
            • The yeast Saccharomyces cerevisiae has two different enzymes that catalyze this reaction.
            • Rer2p synthesizes a well-defined family of polyprenols of 13-18 isoprene residues with dominating C(80) (16 isoprene residues) extending to C(120), while Srt1p synthesizes mainly polyprenol with 22 isoprene subunits.
            • Largest Srt1p products reach C(290).
            • The enzyme from Arabidopsis thaliana catalyzes the formation of polyprenyl diphosphates with predominant carbon number C(120).
            		 2 A0A0F8WYN3 A0A0F8WYN3
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