Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

  ⌊ FunctionalDomain Uncharacterized Mandelate racemase subgroup sequence (ID 54244)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Klebsiella pneumoniae subsp. rhinoscleromatis ATCC 13884 Taxon ID: 667127 259039322 EEW40464.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a C8T753 C8T753_KLEPR (TrEMBL)

Sequence

Length of Enzyme (full-length): 182 | Length of Functional Domain: 182

1       10        20        30        40        50        60

MLDCWMSQDVNYATKLAHACAPYNLKWIEECLPPQQYEGYRELKRQAPAGMMVTSGEHHG
TLQSFRTLSETGIDIMQPDVGWCGGLTTLVEIAAIAKARGQLVVPHGSSVYSHHAVITFT
NTPFSEFLMTSPDCATLRPQFDPILLGEPVPESGRIHKSVLDKPGFGVELNRDCNLKRPY
QH
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
3 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
29 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
57 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
Subgroup CAR This EFD conserves 5/5 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
3 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
29 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
57 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
79 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
106 His (H) side chain proton abstraction (general base) proton relay -- reactant IDA

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2I5Q Crystal Structure Of Apo L-Rhamnonate Dehydratase From Escherichia Coli L-Rhamnonate Dehydratase 319 2.1 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, 2:48 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.