Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup methylaspartate ammonia-lyase

     ⌊ Family methylaspartate ammonia-lyase

  ⌊ FunctionalDomain methylaspartate ammonia-lyase (ID 41)

Superfamily Assignment Evidence Code(s) FSM PubMed:8987982
Family Assignment Evidence Code IES PubMed:1420191
This entry was last updated onNov. 21, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Clostridium tetanomorphum Taxon ID: 1553 737160861 WP_035147529.1 (RefSeq)
Clostridium tetanomorphum DSM 665 Taxon ID: 1230342 618853050 KAJ52266.1 (Genbank) URP
Clostridium tetanomorphum Taxon ID: 1553 259429 AAB24070.1 (Genbank)
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Uniprot

Protein NameAccessionEC Number Identifier
Methylaspartate ammonia-lyase Q05514 4.3.1.2 MAAL_CLOTT (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 413 | Length of Functional Domain: 413

1       10        20        30        40        50        60

MKIVDVLCTPGLTGFYFDDQRAIKKGAGHDGFTYTGSTVTEGFTQVRQKGESISVLLVLE
DGQVAHGDCAAVQYSGAGGRDPLFLAKDFIPVIEKEIAPKLIGREITNFKPMAEEFDKMT
VNGNRLHTAIRYGITQAILDAVAKTRKVTMAEVIRDEYNPGAEINAVPVFAQSGDDRYDN
VDKMIIKEADVLPHALINNVEEKLGLKGEKLLEYVKWLRDRIIKLRVREDYAPIFHIDVY
GTIGAAFDVDIKAMADYIQTLAEAAKPFHLRIEGPMDVEDRQKQMEAMRDLRAELDGRGV
DAELVADEWCNTVEDVKFFTDNKAGHMVQIKTPDLGGVNNIADAIMYCKANGMGAYCGGT
CNETNRSAEVTTNIGMACGARQVLAKPGMGVDEGMMIVKNEMNRVLALVGRRK
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues
Superfamily CAR This EFD conserves 3/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
238 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
273 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
307 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
Subgroup CAR This EFD conserves 4/4 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
238 Asp (D) side chain metal ligand metal ligand -- binding ICS PubMed:11748244
273 Glu (E) side chain metal ligand metal ligand -- binding ICS PubMed:11748244
307 Asp (D) side chain metal ligand metal ligand -- binding ICS PubMed:11748244
331 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant ICS PubMed:11748244
Family CAR This EFD conserves 5/5 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
194 His (H) side chain stabilizes transition state electrostatic stabiliser -- spectator ICS PubMed:11748244
238 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:11748244
273 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:11748244
307 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:11748244
331 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant ICS PubMed:11748244

Catalyzed Reaction

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

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1KCZ Crystal Structure Of Beta-Methylaspartase From Clostridium Tetanomorphum. Mg-Complex. Beta-Methylaspartase 3 1.9 Cysteinesulfonic Acid
(2 more ⇓) 		CSA • PDB • PDBSum
1KD0 Crystal Structure Of Beta-Methylaspartase From Clostridium Tetanomorphum. Apo-Structure. Beta-Methylaspartase 3 1.9 Selenomethionine • 1,2-Ethanediol CSA • PDB • PDBSum
3ZVI Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant L384A Methylaspartate Ammonia-Lyase 3 1.9 Yes Propionamide
(3 more ⇓) 		CSA • PDB • PDBSum
3ZVH Methylaspartate Ammonia Lyase From Clostridium Tetanomorphum Mutant Q73A Methylaspartate Ammonia-Lyase • Methylaspartate Ammonia-Lyase 3 1.99 Yes S-Hydroxycysteine
(4 more ⇓) 		CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History
Time Change Annotation Old Value New Value
Nov. 3, 2014, 2:33 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.