Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup muconate cycloisomerase

     ⌊ Family dipeptide epimerase

  ⌊ FunctionalDomain dipeptide epimerase (ID 2239649)

Superfamily Assignment Evidence Code(s) IEA
Family Assignment Evidence Code IEA
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank: obsolete GI = 658532811

Sequence

Length of Enzyme (full-length): 366 | Length of Functional Domain: 360

1       10        20        30        40        50        60

MKIIRIETSRIAVPLTKPFKTALRTVYTAESVIVRITYDSGAVGWGEAPPTLVITGDSMD
SIESAIHHVLKPALLGKSLAGYEAILHDIQHLLTGNMSAKAAVEMALYDGWAQMCGLPLY
QMLGGYRDTLETDYTVSVNSPEEMAADAENYLKQGFQTLKIKVGKDDIATDIARIQEIRK
RVGSAVKLRLDANQGWRPKEAVTAIRKMEDAGLGIELVEQPVHKDDLAGLKKVTDATDTP
IMADESVFTPRQAFEVLQTRSADLINIKLMKAGGISGAEKINAMAEACGVECMVGSMIET
KLGITAAAHFAASKRNITRFDFDAPLMLKTDVFKGGITYSGSTVSMPGKPGLGITGTALL
KGEKEQ
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
191 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
219 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
244 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
162 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant ICS PubMed:11747448
191 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
219 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
244 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
Family CAR This EFD conserves 5/5 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
162 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant ICS PubMed:11747448
191 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
219 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
244 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
268 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant ICS PubMed:11747448

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1TKK The Structure Of A Substrate-Liganded Complex Of The L-Ala-D/L-Glu Epimerase From Bacillus Subtilis Similar To Chloromuconate Cycloisomerase 24 2.1 Magnesium Ion
(2 more ⇓) 		CSA • PDB • PDBSum
1JPM L-Ala-D/L-Glu Epimerase L-Ala-D/L-Glu Epimerase 24 2.25 Magnesium Ion • Glycerol 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
Aug. 1, 2014, 2:39 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
Sept. 14, 2015, 3:13 a.m. update domain end position 356 360
update domain start position 11 1
EC number assigned by UniProtKB accession ID.