Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup methylaspartate ammonia-lyase

     ⌊ Family methylaspartate ammonia-lyase


1KKR (methylaspartate ammonia-lyase)
Total 100% <100%
Functional domains 154 0 154
UniProtKB 764 0 764
GI 1527 0 1527
Structures 6
Reactions 1
Functional domains of this family were last updated on Nov. 22, 2017
New functional domains were last added to this family on May 7, 2015

Enzymes in the beta-methylaspartate ammonia-lyase (MAL) family catalyze the reversible anti elimination of ammonia from L-threo-(2S,3S)-3-methylaspartic acid to form mesaconic acid, in the catabolic pathway for glutamate. Enzymes in the MAL family require an additional monovalent metal ion, beyond the one divalent metal required across all enzymes in the enolase superfamily, for optimal activity.

No References.

No notes.

Static File Downloads

File Name Description Parameters Stats
network.fam7.bs60.mek250K.xgmml One node per sequence network min bit score = 60
max edge count = 250K		 size = 4.1M
num_edges = 11781
num_nodes = 154
sfld_alignment_fam7.msa Annotated Sequence Alignment, Stockholm format 7 sequences
size: 4.4K

Total number of functional domains in this group.
Number of Functional Domains that have been manually or automatically been assigned to a family.
Number of Functional Domains that have not been assigned to a family.
Number of structures available from the PDB for members of this group.
Number of Functional Domains with 100% of Conserved Residues
Number of Functional Domains with less than 100% Conserved Residues

Active Site

Catalyzed Reaction(s)

methylaspartate ammonia-lyase

+
threo-3-methyl-L-aspartate(1-)
58724		 mesaconate(2-)
36986		 ammonium
28938

EC: 4.3.1.2 | IntEnz: 4.3.1.2 | Kegg: 4.3.1.2 | BioCyc: 4.3.1.2 | BRENDA: 4.3.1.2