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CATH Superfamily 3.40.640.10

Type I PLP-dependent aspartate aminotransferase-like (Major 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:

"
Type I PLP-dependent aspartate aminotransferase-like (Major 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 63148: Aminotransferase class-III family protein

There are 12 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
Adenosylmethionine--8-amino-7-oxononanoate transaminase. [EC: 2.6.1.62]
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4- methylthio-2-oxobutanoate + 7,8-diaminononanoate.
  • S-adenosylhomocysteine can also act as donor.
 278 A0A023DIZ0 A0A023DIZ0 A0A063B7B1 A0A063B7B1 A0A063B9F3 A0A063B9F3 A0A068N5U0 A0A068N5U0 A0A068YJ80 A0A068YJ80
(268 more...)
Beta-alanine--pyruvate transaminase. [EC: 2.6.1.18]
L-alanine + 3-oxopropanoate = pyruvate + beta-alanine.
    		 252 A0A066TNV1 A0A066TNV1 A0A069PHP6 A0A069PHP6 A0A069Q9J3 A0A069Q9J3 A0A081FXA8 A0A081FXA8 A0A081YDY8 A0A081YDY8
    (242 more...)
    Taurine--pyruvate aminotransferase. [EC: 2.6.1.77]
    Taurine + pyruvate = L-alanine + 2-sulfoacetaldehyde.
    • The enzyme from Bilophila wadsworthia catalyzes a reversible reaction that starts an anaerobic taurine degradation pathway.
    • beta-alanine is also a significant amino group donor.
    • The enzyme from the bacterium Pseudomonas denitrificans PD1222 can also use hypotaurine, producing 2-sulfinoacetaldehyde, which spontaneously hydrolyzes to sulfite and acetaldehyde.
    • Unlike EC 2.6.1.55, 2-oxoglutarate cannot serve as an acceptor for the amino group.
    		 238 A0A063UBX9 A0A063UBX9 A0A0A0XMZ7 A0A0A0XMZ7 A0A0C6F0T9 A0A0C6F0T9 A0A0C6P1G4 A0A0C6P1G4 A0A0E1LMM6 A0A0E1LMM6
    (228 more...)
    4-aminobutyrate--pyruvate transaminase. [EC: 2.6.1.96]
    (1) 4-aminobutanoate + pyruvate = succinate semialdehyde + L-alanine. (2) 4-aminobutanoate + glyoxylate = succinate semialdehyde + glycine.
    • The enzyme is found in plants that do not have the 2-oxoglutarate dependent enzyme (cf. EC 2.6.1.19).
    • The reaction with pyruvate is reversible while the reaction with glyoxylate only takes place in the forward direction.
    		 94 A0A078BDN8 A0A078BDN8 A0A088NRI1 A0A088NRI1 A0A089NLP4 A0A089NLP4 A0A090DCD7 A0A090DCD7 A0A090DIF3 A0A090DIF3
    (84 more...)
    4-aminobutyrate--2-oxoglutarate transaminase. [EC: 2.6.1.19]
    4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
    • Some preparations also act on beta-alanine, 5-aminopentanoate and (R,S)-3-amino-2-methylpropanoate.
    		 56 A0A069PS56 A0A069PS56 A0A078FCE5 A0A078FCE5 A0A078HJ76 A0A078HJ76 A0A078HPK5 A0A078HPK5 A0A081FYD8 A0A081FYD8
    (46 more...)
    Acetylornithine transaminase. [EC: 2.6.1.11]
    N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate.
    • Also acts on L-ornithine and N(2)-succinyl-L-ornithine.
    		 46 A0A0C1YL15 A0A0C1YL15 A0A0D5M0H8 A0A0D5M0H8 A0A0D5M788 A0A0D5M788 A0A0K6LZF9 A0A0K6LZF9 A0A0T8L0C4 A0A0T8L0C4
    (36 more...)
    Lysine--8-amino-7-oxononanoate transaminase. [EC: 2.6.1.105]
    L-lysine + 8-amino-7-oxononanoate = (S)-2-amino-6-oxohexanoate + 7,8- diaminononanoate.
    • Participates in the pathway for biotin biosynthesis.
    • The enzyme from the bacterium Bacillus subtilis cannot use S-adenosyl-L-methionine as amino donor and catalyzes an alternative reaction for the conversion of 8-amino-7-oxononanoate to 7,8- diaminononanoate (cf. EC 2.6.1.62).
    • Formerly EC 2.6.1.n2.
    		 6 A0A132BX51 A0A132BX51 A0A132C0R8 A0A132C0R8 A0A1L9NUT2 A0A1L9NUT2
    Acetoacetyl-CoA reductase. [EC: 1.1.1.36]
    (R)-3-hydroxyacyl-CoA + NADP(+) = 3-oxoacyl-CoA + NADPH.
      		 4 A0A1C9VL45 A0A1C9VL45 A0A1L1PTX5 A0A1L1PTX5
      Taurine--2-oxoglutarate transaminase. [EC: 2.6.1.55]
      Taurine + 2-oxoglutarate = sulfoacetaldehyde + L-glutamate.
      • Also acts on D,L-3-amino-isobutanoate, beta-alanine and 3-aminopropanesulfonate.
      • Involved in the microbial utilization of beta-alanine.
      		 4 A0A1A0CLE5 A0A1A0CLE5 A0A1A5VL25 A0A1A5VL25
      Diaminobutyrate--2-oxoglutarate transaminase. [EC: 2.6.1.76]
      L-2,4-diaminobutanoate + 2-oxoglutarate = L-aspartate 4-semialdehyde + L-glutamate.
      • Differs from EC 2.6.1.46, which has pyruvate as the amino-group acceptor.
      • This is the first enzyme in the ectoine biosynthesis pathway, the other enzymes involved being EC 2.3.1.178 and EC 4.2.1.108.
      		 4 A0A1B8NWM3 A0A1B8NWM3 E1V7V7 E1V7V7
      Glutamate-1-semialdehyde 2,1-aminomutase. [EC: 5.4.3.8]
      (S)-4-amino-5-oxopentanoate = 5-aminolevulinate.
        		 4 A0A083ZQS8 A0A083ZQS8 G8PMG4 G8PMG4
        Glutamine synthetase. [EC: 6.3.1.2]
        ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine.
        • Glutamine synthetase, which catalyzes the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life.
        • Several types have been described, differing in their oligomeric structures and cofactor requirements.
        		 2 G8Q4R3 G8Q4R3
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