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CATH Superfamily 1.20.1090.10

Dehydroquinate synthase-like - alpha domain

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:

"
Dehydroquinate synthase-like - alpha domain
".

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 7046: Putative glycerol-1-phosphate dehydrogenase (NAD(P...

There are 6 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
Glycerol dehydrogenase. [EC: 1.1.1.6]
Glycerol + NAD(+) = glycerone + NADH.
  • Also acts on 1,2-propanediol.
 1713 A0A010ZB78 A0A010ZL11 A0A017I5N8 A0A022PKY0 A0A023T622 A0A023V589 A0A023V7R1 A0A023YU11 A0A023Z5P2 A0A024KLW3
(1703 more...)
Sn-glycerol-1-phosphate dehydrogenase. [EC: 1.1.1.261]
sn-glycerol 1-phosphate + NAD(P)(+) = glycerone phosphate + NAD(P)H.
  • Responsible for the formation of archaea-specific sn-glycerol-1- phosphate, the first step in the biosynthesis of polar lipids in archaea.
  • It is the enantiomer of sn-glycerol 3-phosphate, the form of glycerophosphate found in bacteria and eukaryotes.
  • The other enzymes involved in the biosynthesis of polar lipids in archaea are EC 2.5.1.41 and EC 2.5.1.42, which together alkylate the hydroxy groups of glycerol 1-phosphate to give unsaturated archaetidic acid, which is acted upon by EC 2.7.7.67 to form CDP- unsaturated archaeol.
  • The final step in the pathway involves the addition of L-serine, with concomitant removal of CMP, leading to the production of unsaturated archaetidylserine.
  • Activity of the enzyme is stimulated by K(+).
 622 A0A031LPP6 A0A060HFS1 A0A062VEI4 A0A063YV11 A0A063ZIU1 A0A075FX80 A0A075G9R9 A0A075GDJ4 A0A075GKZ4 A0A075GNJ0
(612 more...)
Alcohol dehydrogenase. [EC: 1.1.1.1]
(1) An alcohol + NAD(+) = an aldehyde or ketone + NADH. (2) A secondary alcohol + NAD(+) = a ketone + NADH.
  • Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol.
  • The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
 277 A0A027TFH8 A0A028A2S4 A0A028DM53 A0A029L0Q4 A0A059N146 A0A069XH47 A0A070FFU1 A0A070SSL4 A0A070V2W9 A0A074IJZ6
(267 more...)
(R)-aminopropanol dehydrogenase. [EC: 1.1.1.75]
(R)-1-aminopropan-2-ol + NAD(+) = aminoacetone + NADH.
    		 87 A0A059N146 A0A066T641 A0A086IKK8 A0A090NKU9 A0A090NY30 A0A0A6ZNL4 A0A0A7A0W6 A0A0E1CCU4 A0A0E1CHI4 A0A0E1CRL5
    (77 more...)
    Glycerol-3-phosphate dehydrogenase. [EC: 1.1.5.3]
    sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol.
    • An essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis.
    • In bacteria, the enzyme is localized to the cytoplasmic membrane, while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane.
    • In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8 forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD(+) by the mitochondrial electron-transport chain.
    • This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix.
    • Insect flight muscle uses only CoQ(10) as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ(9).
    • The enzyme is activated by calcium.
    • Formerly EC 1.1.2.1 and EC 1.1.99.5.
    		 9 A0A0D6I6E7 A0A0F6B7Z1 A0A0F7JAT2 A0A0H3NH12 A0A0L5UW51 A0A0M0PPS8 A0A0U1FDG8 E8XEN2 Q8ZLH1
    3-dehydroquinate synthase. [EC: 4.2.3.4]
    3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate.
    • The hydrogen atoms on C-7 of the substrate are retained on C-2 of the products.
    • Formerly EC 4.6.1.3.
    		 2 T1ALG8 T1C4P8
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