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CATH Superfamily 3.30.230.10

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 28512: Translation elongation factor 2

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
Protein-synthesizing GTPase. [EC: 3.6.5.3]
GTP + H(2)O = GDP + phosphate.
  • This enzyme comprises a family of proteins involved in prokaryotic as well as eukaryotic protein synthesis.
  • In the initiation factor complex, it is IF-2b (98 kDa) that binds GTP and subsequently hydrolyzes it in prokaryotes.
  • In eukaryotes, it is eIF-2 (150 kDa) that binds GTP.
  • In the elongation phase, the GTP-hydrolyzing proteins are the EF-Tu polypeptide of the prokaryotic transfer factor (43 kDa), the eukaryotic elongation factor EF-1-alpha (53 kDa), the prokaryotic EF-G (77 kDa), the eukaryotic EF-2 (70-110 kDa) and the signal recognition particle that play a role in endoplasmic reticulum protein synthesis (325 kDa).
  • EF-Tu and EF-1-alpha catalyze binding of aminoacyl-tRNA to the ribosomal A-site, while EF-G and EF-2 catalyze the translocation of peptidyl-tRNA from the A-site to the P-site.
  • GTPase activity is also involved in polypeptide release from the ribosome with the aid of the pRFs and eRFs.
  • Formerly EC 3.6.1.48.
 24 A0A0B2R191 A0A0B2R191 A0A0B2R210 A0A0B2R210 A0A0B2R4R9 A0A0B2R4R9 A0A0D2MMI2 A0A0D2MMI2 A0A151SRJ2 A0A151SRJ2
(14 more...)
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.
 4 A0A161MA03 A0A161MA03 A0A170Y4A6 A0A170Y4A6
Transferred entry: 1.5.1.38, 1.5.1.39 and 1.5.1.41. [EC: 1.5.1.29]
    		2 B0EI57 B0EI57
    Sphingomyelin phosphodiesterase. [EC: 3.1.4.12]
    Sphingomyelin + H(2)O = N-acylsphingosine + phosphocholine.
    • Has very little activity on phosphatidylcholine.
    		 2 B0E9Y1 B0E9Y1
    Sulfate adenylyltransferase. [EC: 2.7.7.4]
    ATP + sulfate = diphosphate + adenylyl sulfate.
    • The human phosphoadenosine-phosphosulfate synthase (PAPS) system is a bifunctional enzyme: ATP sulfurylase, which catalyzes the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate and the second step is catalyzed by the APS kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme bound APS and ATP.
    • This is in contrast to what is found in bacteria, yeasts, fungi and plants, where the formation of PAPS is carried out by two individual polypeptides, EC 2.7.7.4 and EC 2.7.1.25.
    		 2 B0EQ47 B0EQ47
    Phosphatidylinositol-3,4-bisphosphate 4-phosphatase. [EC: 3.1.3.66]
    1-phosphatidyl-myo-inositol 3,4-bisphosphate + H(2)O = 1-phosphatidyl- 1D-myo-inositol 3-phosphate + phosphate.
    • Magnesium-independent.
    • This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyzes Ins(1,3,4)P(3) to Ins(1,3)P(2).
    • It also converts Ins(3,4)P(2) into Ins-3-P.
    		 2 B0EQ47 B0EQ47
    Pyruvate kinase. [EC: 2.7.1.40]
    ATP + pyruvate = ADP + phosphoenolpyruvate.
    • UTP, GTP, CTP, ITP and dATP can also act as donors.
    • Also phosphorylates hydroxylamine and fluoride in the presence of CO(2).
    		 2 H3FAW0 H3FAW0