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CATH Superfamily 1.10.150.20

5' to 3' exonuclease, C-terminal subdomain

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:

"
5' to 3' exonuclease, C-terminal subdomain
".

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 27404: NADH-quinone oxidoreductase, E subunit

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
NADH:ubiquinone reductase (H(+)-translocating). [EC: 1.6.5.3]
NADH + ubiquinone + 5 H(+)(In) = NAD(+) + ubiquinol + 4 H(+)(Out).
  • The complex is present in mitochondria and aerobic bacteria.
  • Breakdown of the complex can release EC 1.6.99.3.
  • In photosynthetic bacteria, reversed electron transport through this enzyme can reduce NAD(+) to NADH.
 110 A0A017H9U8 A0A017HTG9 A0A024INB4 A0A024KJH9 A0A058ZPM2 A0A058ZQR5 A0A059F8R8 A0A069E1J6 A0A073IIM1 A0A083ZRI1
(100 more...)
Transferred entry: 1.6.5.11. [EC: 1.6.99.5]
    		41 A0A021X655 A0A060HZ75 A0A090E8U1 A0A090EUS1 A0A090F0M6 A0A090GF11 A0A090GLI3 A0A090GV94 A0A0A8GAK9 A0A0B4X266
    (31 more...)
    NADH dehydrogenase (quinone). [EC: 1.6.5.11]
    NADH + a quinone = NAD(+) + a quinol.
    • Menaquinone or other quinones can act as acceptor.
    • Inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives.
    • Formerly EC 1.6.99.5.
    		 41 A0A072C4S0 A0A0H5D3C7 A0A0L6CRH4 A0A0M6XTL1 A0A0M6XYY2 A0A0M6YH02 A0A0M6YWU0 A0A0M7A3H4 A0A0M7AF85 A0A0M7B7B4
    (31 more...)
    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.
    		 5 A3SWX1 A3SWX2 A3U1M2 A3UCV4 A3X7S3
    [Myosin light-chain] kinase. [EC: 2.7.11.18]
    ATP + [myosin light-chain] = ADP + [myosin light-chain] phosphate.
    • Requires calmodulin for activity.
    • The 20 kDa light chain from smooth muscle myosin is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors, more slowly.
    • Formerly EC 2.7.1.117.
    		 1 G8SLI5
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