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CATH Superfamily 3.30.9.10

D-Amino Acid Oxidase, subunit A, 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:

"
D-Amino Acid Oxidase, subunit A, 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 17720: Aerobic glycerol-3-phosphate dehydrogenase

There are 4 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-3-phosphate oxidase. [EC: 1.1.3.21]
sn-glycerol 3-phosphate + O(2) = glycerone phosphate + H(2)O(2).
    		 264 A0A059MXG5 A0A081PMX8 A0A081PP71 A0A081PS15 A0A081PZ59 A0A081Q8I5 A0A081QEZ0 A0A081QLC7 A0A081QLL1 A0A081SA00
    (254 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.
    		 35 A0A095Z9X1 A0A0B0I9V7 A0A0H3C1M0 A0A0L7Y3R6 A0A0M1X765 A0A0M1ZZL8 A0A0M2A6I8 A0A0R1G2Y2 A0A0V8ELX1 A0A0X3RK10
    (25 more...)
    D-alanine--poly(phosphoribitol) ligase. [EC: 6.1.1.13]
    ATP + D-alanine + poly(ribitol phosphate) = AMP + diphosphate + O-D- alanyl-poly(ribitol phosphate).
    • A thioester bond is formed transiently between D-alanine and the sulfhydryl group of the 4'-phosphopantetheine prosthetic group of D-alanyl carrier protein during the activation of the alanine.
    • Involved in the synthesis of teichoic acids.
    		 2 A5LLP4 A5M8Q3
    Exopolyphosphatase. [EC: 3.6.1.11]
    (Polyphosphate)(n) + H(2)O = (polyphosphate)(n-1) + phosphate.
      		 1 E6LDC8
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