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:

"
P-loop containing nucleotide triphosphate hydrolases
".

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 633777: Vacuolar dynamin GTPase VpsA

There are 9 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
Dynamin GTPase. [EC: 3.6.5.5]
GTP + H(2)O = GDP + phosphate.
  • An enzyme with a molecular mass of about 100 kDa that is involved in endocytosis and is instrumental in pinching off membrane vesicles.
  • Formerly EC 3.6.1.50.
165 A0A024V718 A0A024VQS7 A0A024VYA4 A0A024WIF7 A0A024WR14 A0A024X6T3 A0A060RVG0 A0A060RZ73 A0A061I1Z7 A0A061I6R1
(155 more...)
Phosphogluconate dehydratase. [EC: 4.2.1.12]
6-phospho-D-gluconate = 2-dehydro-3-deoxy-6-phospho-D-gluconate + H(2)O.
    1 B0E6L6
    Branched-chain-amino-acid transaminase. [EC: 2.6.1.42]
    (1) L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate. (2) L-isoleucine + 2-oxoglutarate = (S)-3-methyl-2-oxopentanoate + L-glutamate. (3) L-valine + 2-oxoglutarate = 3-methyl-2-oxobutanoate + L-glutamate.
    • Also acts on L-isoleucine and L-valine.
    • Different from EC 2.6.1.66.
    1 A8I5K1
    Phenylalanine dehydrogenase. [EC: 1.4.1.20]
    L-phenylalanine + H(2)O + NAD(+) = phenylpyruvate + NH(3) + NADH.
    • The enzymes from Bacillus badius and Sporosarcina ureae are highly specific for L-phenylalanine; that from Bacillus sphaericus also acts on L-tyrosine.
    1 B0E6L6
    2-alkenal reductase (NAD(P)(+)). [EC: 1.3.1.74]
    A n-alkanal + NAD(P)(+) = an alk-2-enal + NAD(P)H.
    • Highly specific for 4-hydroxynon-2-enal and non-2-enal.
    • Alk-2-enals of shorter chain have lower affinities.
    • Exhibits high activities also for alk-2-enones such as but-3-en-2-one and pent-3-en-2-one.
    • Inactive with cyclohex-2-en-1-one and 12-oxophytodienoic acid.
    • Involved in the detoxification of alpha,beta-unsaturated aldehydes and ketones (cf. EC 1.3.1.102).
    1 A0A0B2R543
    Nucleoside-triphosphate phosphatase. [EC: 3.6.1.15]
    NTP + H(2)O = NDP + phosphate.
    • The enzyme is found in eukaryotes and thermophilic bacteria, but appears to be absent from mesophilic bacteria.
    • Also hydrolyzes nucleoside diphosphates, thiamine diphosphate and FAD.
    • The enzyme from the plant Pisum sativum (garden pea) is regulated by calmodulin.
    1 A0A171AEB9
    UMP/CMP kinase. [EC: 2.7.4.14]
    (1) ATP + (d)CMP = ADP + (d)CDP. (2) ATP + UMP = ADP + UDP.
    • This eukaryotic enzyme is a bifunctional enzyme that catalyzes the phosphorylation of both CMP and UMP with similar efficiency.
    • dCMP can also act as acceptor.
    • Different from the monofunctional prokaryotic enzymes EC 2.7.4.25, CMP kinase and EC 2.7.4.22, UMP kinase.
    • This eukaryotic enzyme is a bifunctional enzyme that catalyzes the phosphorylation of both CMP and UMP with similar efficiency.
    • dCMP can also act as acceptor.
    • Different from the monofunctional prokaryotic enzymes EC 2.7.4.25 and EC 2.7.4.22.
    • Formerly EC 2.7.4.5.
    1 A0A178VKQ6
    Alpha-galactosidase. [EC: 3.2.1.22]
    Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha- D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.
    • Also hydrolyzes alpha-D-fucosides.
    1 A0A0W0GD54
    Protein-serine/threonine phosphatase. [EC: 3.1.3.16]
    [a protein]-serine/threonine phosphate + H(2)O = [a protein]- serine/threonine + phosphate.
    • A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48).
    • The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1).
    1 A0A1B0CY18
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