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 633103: Chromosome partition protein Smc

There are 5 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
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).
3 B0EUG2 B7Q750 L0B318
Heme-transporting ATPase. [EC: 3.6.3.41]
ATP + H(2)O + heme(In) = ADP + phosphate + heme(Out).
  • An enzyme found in Gram-negative bacteria that exports heme.
1 B0EUG2
Acylphosphatase. [EC: 3.6.1.7]
An acylphosphate + H(2)O = a carboxylate + phosphate.
    1 R4MBV8
    H(+)-transporting two-sector ATPase. [EC: 3.6.3.14]
    ATP + H(2)O + H(+)(In) = ADP + phosphate + H(+)(Out).
    • A multisubunit non-phosphorylated ATPase that is involved in the transport of ions.
    • Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)).
    • The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases.
    • All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits.
    • Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis.
    • This movement is driven by the H(+) electrochemical potential gradient.
    • The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP.
    • Formerly EC 3.6.1.34.
    1 G0R5C3
    Endopeptidase La. [EC: 3.4.21.53]
    Hydrolysis of proteins in presence of ATP.
    • ATP hydrolysis is linked with peptide bond hydrolysis.
    • Vanadate inhibits both reactions.
    • A similar enzyme occurs in animal mitochondria.
    • Belongs to peptidase family S16.
    1 B0EUG2
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