Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup methylaspartate ammonia-lyase

  ⌊ FunctionalDomain uncharacterized methylaspartate ammonia-lyase subgroup sequence, enolase superfamily (ID 3791868)

Superfamily Assignment Evidence Code(s) IEA
This entry was last updated onNov. 21, 2017

References to Other Databases

Uniprot

Protein NameAccessionEC Number Identifier
n/a W1FRI7 W1FRI7_ECOLX (TrEMBL)

Sequence

Length of Enzyme (full-length): 348 | Length of Functional Domain: 348

1       10        20        30        40        50        60

MGDCAAVQYSGAGGRDPLFLAENFIPFLNDHIKPLLEGRDVDSFLTNARFFDELRIDGHL
LHTAVRYGLSQALLDAAALATGRLKAEVVCDEWQLPCVPEAIPLFGQSGDDRYIAVDKMI
LKGVDVLPHALINNVEEKLGFKGEKLREYVRWLSNRILSLRTNESYHPTLHIDVYGTIGL
IFDMDPVRCAEYIASLEAEAQGLPLYIEGPVDAGNKPDQIRMLTEITQELTRLGSGVKIV
ADEWCNTYQDIVDFTDAGSCHMVQIKTPDLGGIHNIVDAVLYCNKHGMEAYQGGTCNETE
ISARTCVHVALAARPMRMLIKPGMGFDEGLNIVFNEMNRTIALLQTKD
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
173 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
208 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
242 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
173 Asp (D) side chain metal ligand metal ligand -- binding ICS PubMed:11748244
208 Glu (E) side chain metal ligand metal ligand -- binding ICS PubMed:11748244
242 Asp (D) side chain metal ligand metal ligand -- binding ICS PubMed:11748244
266 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant ICS PubMed:11748244

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1KKR Crystal Structure Of Citrobacter Amalonaticus Methylaspartate Ammonia Lyase Containing (2S,3S)-3-Methylaspartic Acid 3-Methylaspartate Ammonia-Lyase 25 2.1 Selenomethionine
(2 more ⇓) 		CSA • PDB • PDBSum
1KKO Crystal Structure Of Citrobacter Amalonaticus Methylaspartate Ammonia Lyase 3-Methylaspartate Ammonia-Lyase 25 1.33 Selenomethionine • Sulfate Ion 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
June 8, 2015, 3:47 a.m. update name uncharacterized Enolase superfamily sequence uncharacterized methylaspartate ammonia-lyase subgroup sequence, enolase superfamily
Aug. 10, 2015, 3:36 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.