Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup methylaspartate ammonia-lyase

     ⌊ Family methylaspartate ammonia-lyase

  ⌊ FunctionalDomain methylaspartate ammonia-lyase (ID 38608)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Taxon ID: 544 496059648 WP_008784155.1 (RefSeq)
Citrobacter sp. BIDMC108 Taxon ID: 1686385 838606086 KLV90355.1 (Genbank) URP
Citrobacter sp. MGH105 Taxon ID: 1686380 838587268 KLV71676.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a A0A1C0PEX7 A0A1C0PEX7_CITFR (TrEMBL)
n/a A0A0J1NLH3 A0A0J1NLH3_9ENTR (TrEMBL)

Sequence

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

1       10        20        30        40        50        60

MKIKQALFTAGYSSFYFDDQQAIKNGAGHDGFIYTGDPVTPGFTSVRQAGECVSVQLILE
NGAVAVGDCAAVQYSGAGGRDPLFLAENFIPFLNDHIKPLLEGRDVDSFLTNARFFDELR
IDGHLLHTAVRYGLSQALLDAAALATGRLKAEVVCDEWQLPCVPEAIPLFGQSGDDRYIA
VDKMILKGVDVLPHALINNVEEKLGFKGEKLREYVRWLSNRILSLRTNESYHPTLHIDVY
GTIGLIFDMDPVRCAEYIASLEAEAQGLPLYIEGPVDAGNKPDQIRMLTEITQELTRLGS
GVKIVADEWCNTYQDIVDFTDAGSCHMVQIKTPDLGGIHNIVDAVLYCNKHGMEAYQGGT
CNETEISARTCVHVALAARPMRMLIKPGMGFDEGLNIVFNEMNRTIALLQTKD
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

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
Nov. 3, 2014, 2:42 a.m. update curation agent updateSFLDGIs.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.