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 63248: Cysteine sulfinic acid decarboxylase

There are 10 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
Diaminobutyrate decarboxylase. [EC: 4.1.1.86]
L-2,4-diaminobutanoate = propane-1,3-diamine + CO(2).
  • N(4)-acetyl-L-2,4-diaminobutanoate, 2,3-diaminopropanoate, ornithine and lysine are not substrates.
  • In Acinetobacter baumannii it is cotranscribed with the neighboring dat gene that encodes EC 2.6.1.76, which can supply the substrate for the decarboxylase.
710 A0A009FSC0 A0A009FSC0 A0A009G6T9 A0A009G6T9 A0A009H2T3 A0A009H2T3 A0A009HHM1 A0A009HHM1 A0A009IRE1 A0A009IRE1
(700 more...)
Aromatic-L-amino-acid decarboxylase. [EC: 4.1.1.28]
(1) L-dopa = dopamine + CO(2). (2) 5-hydroxy-L-tryptophan = 5-hydroxytryptamine + CO(2).
  • Also acts on other aromatic L-amino acids, including L-tryptophan.
  • Formerly EC 4.1.1.26 and EC 4.1.1.27.
268 A0A024K6S8 A0A024K6S8 A0A061ILT2 A0A061ILT2 A0A068QPH6 A0A068QPH6 A0A084G1F7 A0A084G1F7 A0A085U7L2 A0A085U7L2
(258 more...)
Glutamate decarboxylase. [EC: 4.1.1.15]
L-glutamate = 4-aminobutanoate + CO(2).
  • The brain enzyme also acts on L-cysteate, 3-sulfino-L-alanine and L-aspartate.
102 A0A0G3VGT7 A0A0G3VGT7 A0A0G3VI11 A0A0G3VI11 A0A0J9UE83 A0A0J9UE83 A0A0M1QLV9 A0A0M1QLV9 A0A0S2Z3V5 A0A0S2Z3V5
(92 more...)
Tyrosine decarboxylase. [EC: 4.1.1.25]
L-tyrosine = tyramine + CO(2).
  • The bacterial enzyme also acts on 3-hydroxytyrosine and, more slowly, on 3-hydroxyphenylalanine.
86 A0A076K1U2 A0A076K1U2 A0A088RWY6 A0A088RWY6 A0A0B2PP13 A0A0B2PP13 A0A0B2Q3G6 A0A0B2Q3G6 A0A0B2QNE1 A0A0B2QNE1
(76 more...)
Transferred entry: 4.1.1.28. [EC: 4.1.1.26]
    74 O01950 O01950 O01951 O01951 O01952 O01952 O02010 O02010 O02011 O02011
    (64 more...)
    Sulfinoalanine decarboxylase. [EC: 4.1.1.29]
    3-sulfino-L-alanine = hypotaurine + CO(2).
    • Also acts on L-cysteate.
    38 A0A024RAX7 A0A024RAX7 A0A0N9E6M5 A0A0N9E6M5 A0A0N9E6Z6 A0A0N9E6Z6 A0A140C532 A0A140C532 A0A140C533 A0A140C533
    (28 more...)
    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.
    32 A0A090IMW2 A0A090IMW2 A0A090P4F9 A0A090P4F9 A0A090R3G5 A0A090R3G5 A0A090S3R2 A0A090S3R2 A0A090T3R2 A0A090T3R2
    (22 more...)
    Histidine decarboxylase. [EC: 4.1.1.22]
    L-histidine = histamine + CO(2).
      20 A0A0B4KEQ1 A0A0B4KEQ1 A0A0G3VI98 A0A0G3VI98 I0B8M2 I0B8M2 P16453 P16453 P19113 P19113
      (10 more...)
      Aspartate 1-decarboxylase. [EC: 4.1.1.11]
      L-aspartate = beta-alanine + CO(2).
        20 A0A0C5QEV9 A0A0C5QEV9 A6QM00 A6QM00 A7U8C7 A7U8C7 A9YVA8 A9YVA8 H9JRC8 H9JRC8
        (10 more...)
        DNA-formamidopyrimidine glycosylase. [EC: 3.2.2.23]
        Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
        • May play a significant role in processes leading to recovery from mutagenesis and/or cell death by alkylating agents.
        • Also involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA.
        2 A0A0H3PEX0 A0A0H3PEX0
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