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: waiting to be named.

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 17801: Heavy metal translocating P-type ATPase

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
Mercury(II) reductase. [EC: 1.16.1.1]
Hg + NADP(+) + H(+) = Hg(2+) + NADPH.
    382 A0A069DMD6 A0A069DMD6 A0A081QD45 A0A081QD45 A0A094JSI3 A0A094JSI3 A0A094WPK5 A0A094WPK5 A0A099DCL7 A0A099DCL7
    (372 more...)
    Cu(2+)-exporting ATPase. [EC: 3.6.3.4]
    ATP + H(2)O + Cu(2+)(Side 1) = ADP + phosphate + Cu(2+)(Side 2).
    • A P-type ATPase that undergoes covalent phosphorylation during the transport cycle.
    • The enzyme from the termophilic bacterium Archaeoglobus fulgidus is involved in copper extrusion from the cell.
    178 A0A068YSG0 A0A068YSG0 A0A075WDQ8 A0A075WDQ8 A0A088X865 A0A088X865 A0A088X865 A0A088X865 A0A095FAW7 A0A095FAW7
    (168 more...)
    Dihydrolipoyl dehydrogenase. [EC: 1.8.1.4]
    Protein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH.
    • A component of the multienzyme 2-oxo-acid dehydrogenase complexes.
    • In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12 and catalyzes oxidation of its dihydrolipoyl groups.
    • It plays a similar role in the oxoglutarate and 3-methyl-2- oxobutanoate dehydrogenase complexes.
    • Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system, in which it acts, together with EC 1.4.4.2 and EC 2.1.2.10 to break down glycine.
    • It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate.
    • Was first shown to catalyze the oxidation of NADH by methylene blue; this activity was called diaphorase.
    • The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein.
    • Formerly EC 1.6.4.3.
    32 A0A023DJI8 A0A023DJI8 A0A0A2SM61 A0A0A2SM61 A0A0A2SWI0 A0A0A2SWI0 A0A0D0Q5C5 A0A0D0Q5C5 A0A0G3Y3J2 A0A0G3Y3J2
    (22 more...)
    Cu(+) exporting ATPase. [EC: 3.6.3.54]
    ATP + H(2)O + Cu(+)(Side 1) = ADP + phosphate + Cu(+)(Side 2).
    • A P-type ATPase that undergoes covalent phosphorylation during the transport cycle.
    • This enzyme transports Cu(+) or Ag(+), and cannot transport the divalent ions, contrary to EC 3.6.3.4, which mainly transports the divalent copper ion.
    • Formerly EC 3.6.3.n1.
    24 A0A075WDQ8 A0A075WDQ8 A0A0M1VDQ5 A0A0M1VDQ5 A0A0M9AEE9 A0A0M9AEE9 A0A0P0RHD7 A0A0P0RHD7 A0A110AV68 A0A110AV68
    (14 more...)
    Cadmium-exporting ATPase. [EC: 3.6.3.3]
    ATP + H(2)O + Cd(2+)(In) = ADP + phosphate + Cd(2+)(Out).
    • P-type ATPase that undergoes covalent phosphorylation during the transport cycle.
    10 A0A068YSG0 A0A068YSG0 A0A0P4V2I5 A0A0P4V2I5 A0ZAE8 A0ZAE8 G2FBX0 G2FBX0 X5JZ76 X5JZ76
    Zinc-exporting ATPase. [EC: 3.6.3.5]
    ATP + H(2)O + Zn(2+)(In) = ADP + phosphate + Zn(2+)(Out).
    • P-type ATPase that undergoes covalent phosphorylation during the transport cycle.
    • This enzyme also exports Cd(2+) and Co(2+).
    2 G2FBX0 G2FBX0
    Molybdenum cofactor guanylyltransferase. [EC: 2.7.7.77]
    GTP + molybdenum cofactor = diphosphate + guanylyl molybdenum cofactor.
    • Catalyzes the guanylation of the molybdenum cofactor.
    • This modification occurs only in prokaryotes.
    2 D3DIX9 D3DIX9
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