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CATH Superfamily 3.40.50.720

NAD(P)-binding Rossmann-like Domain

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:

"
NAD(P)-binding Rossmann-like Domain
".

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 291944: Methionine adenosyltransferase 2 subunit beta

There are 3 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
DTDP-4-dehydrorhamnose reductase. [EC: 1.1.1.133]
dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + NADPH.
  • In the reverse direction, reduction on the 4-position of the hexose moiety takes place only while the substrate is bound to another enzyme that catalyzes epimerization at C-3 and C-5; the complex has been referred to as dTDP-L-rhamnose synthase.
 14 A0A073KXA5 A0A073KXA5 A0A0P9FZI9 A0A0P9FZI9 A3QIB2 A3QIB2 B0TS50 B0TS50 E3TF31 E3TF31
(4 more...)
Methionine adenosyltransferase. [EC: 2.5.1.6]
ATP + L-methionine + H(2)O = phosphate + diphosphate + S-adenosyl-L- methionine.
  • Formerly EC 2.4.2.13.
 2 A0A061I2T0 A0A061I2T0
Elongation factor 4. [EC: 3.6.5.n1]
GTP + H(2)O = GDP + phosphate.
  • The enzyme is required for accurate and efficient protein synthesis under certain stress conditions.
  • May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes.
  • Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly.
  • Binds to ribosomes in a GTP-dependent manner.
 2 T1JJJ9 T1JJJ9