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 2070: Syntaxin 4A (Placental), isoform CRA_a

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
Aspartate transaminase. [EC: 2.6.1.1]
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate.
  • Also acts on L-tyrosine, L-phenylalanine and L-tryptophan.
  • This activity can be formed from EC 2.6.1.57 by controlled proteolysis.
2 A0A146HFR4 A0A146HFR4
Nicotinate-nucleotide diphosphorylase (carboxylating). [EC: 2.4.2.19]
Beta-nicotinate D-ribonucleotide + diphosphate + CO(2) = pyridine-2,3- dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate.
  • The reaction is catalyzed in the opposite direction.
  • Since quinolinate is synthesized from L-tryptophan in eukaryotes, but from L-aspartate in some prokaryotes, this is the first NAD(+) biosynthesis enzyme shared by both eukaryotes and prokaryotes.
2 A0A0L1HLQ3 A0A0L1HLQ3
Nicotinate phosphoribosyltransferase. [EC: 6.3.4.21]
Nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H(2)O = beta- nicotinate D-ribonucleotide + diphosphate + ADP + phosphate.
  • The enzyme, which is involved in pyridine nucleotide recycling, can form beta-nicotinate D-ribonucleotide and diphosphate from nicotinate and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) in the absence of ATP.
  • However, when ATP is available the enzyme is phosphorylated resulting in a much lower K(m) for nicotinate.
  • The phospho-enzyme is hydrolyzed during the transferase reaction, regenerating the low affinity form.
  • The presence of ATP shifts the products/substrates equilibrium from 0.67 to 1100.
  • Formerly EC 2.4.2.11.
2 A0A0L1HLQ3 A0A0L1HLQ3