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CATH Superfamily 3.40.50.300

P-loop containing nucleotide triphosphate hydrolases

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 628459: Translation elongation factor Tu

There are 8 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.
 307 A0A010PQ17 A0A017H253 A0A017H2I8 A0A026S0C2 A0A027T5K2 A0A027YVS5 A0A059IAY6 A0A061I8C8 A0A063KDQ8 A0A064AB51
(297 more...)
Adenylyl-sulfate kinase. [EC: 2.7.1.25]
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl 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.
 28 A0A060QD53 A0A067Z354 A0A087PMR3 A0A0C9LKJ9 A0A0D6MUQ3 A0A0D6N6R0 A0A0D6NDZ6 A0A0D6NMR6 A0A0D6NS02 A0A0D6P0U9
(18 more...)
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.
 20 A0A086J5U5 A0A086J5X3 A0A086KZI0 A0A086PFM9 A0A0B2PC11 A0A0L8AHS9 A0A139XHY8 A0A150Y2L8 A0A151G9Q4 B7P0L0
(10 more...)
Heterotrimeric G-protein GTPase. [EC: 3.6.5.1]
GTP + H(2)O = GDP + phosphate.
  • This group comprises GTP-hydrolyzing systems, where GTP and GDP alternate in binding.
  • This group includes stimulatory and inhibitory G-proteins such as G(s), G(i), G(o) and G(olf), targeting adenylate cyclase and/or K(+) and Ca(2+) channels; G(q) stimulating phospholipase C; transducin activating cGMP phosphodiesterase; gustducin activating cAMP phosphodiesterase.
  • G(olf) is instrumental in odor perception, transducin in vision and gustducin in taste recognition.
  • At least 16 different alpha subunits (39-52 kDa), 5 beta subunits (36 kDa) and 12 gamma subunits (6-9 kDa) are known.
  • Formerly EC 3.6.1.46.
 4 A0A0A7EAQ1 A0A0A7EB34 A0A0A7EC82 A0A0A7ECE1
[Formate-C-acetyltransferase]-activating enzyme. [EC: 1.97.1.4]
S-adenosyl-L-methionine + dihydroflavodoxin + [formate C-acetyltransferase]-glycine = 5'-deoxyadenosine + L-methionine + flavodoxin semiquinone + [formate C-acetyltransferase]-glycin-2-yl radical.
  • A single glycine residue in EC 2.3.1.54 is oxidized to the corresponding radical by transfer of H from its CH(2) to AdoMet with concomitant cleavage of the latter.
  • The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5'-yl radical, which then abstracts a hydrogen radical from the glycine residue.
 3 C8N6E8 C8N6G0 F9EZB9
DNA topoisomerase (ATP-hydrolyzing). [EC: 5.99.1.3]
ATP-dependent breakage, passage and rejoining of double-stranded DNA.
  • Can introduce negative superhelical turns into double-stranded circular DNA.
  • One unit has nicking-closing activity, and another catalyzes super- twisting and hydrolysis of ATP (cf. EC 5.99.1.2).
 1 B1V852
Adenylosuccinate synthase. [EC: 6.3.4.4]
GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)- AMP.
    		 1 A0A0J9W6L4
    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.
    		 1 A0A171AB77
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