Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

  ⌊ FunctionalDomain Uncharacterized Mandelate racemase subgroup sequence (ID 21204)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Salmonella enterica Taxon ID: 28901 446285292 WP_000363147.1 (RefSeq) URP

Sequence

Length of Enzyme (full-length): 211 | Length of Functional Domain: 211

1       10        20        30        40        50        60

ENGIGGIKLKVGQPNCAEDIRRLTAVREALGDEFPLMVDANQQWDRETAIRMGRKMEQFN
LIWIEEPLDAYDIEGHAQLAAALDTPIATGEMLTSFREHEQLILGNASDFVQPDAPRVGG
ISPFLKIMDLAAKHGRKLAPHFAMEVHLHLSAAYPLEPWLEHFEWLNPLFNEQLELRDGR
MWISDRHGLGFTLSEQARRWTQLTCEFGKRP
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
39 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
65 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
91 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
39 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
65 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
91 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
114 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
141 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
2PP0 Crystal Structure Of L-Talarate/Galactarate Dehydratase From Salmonella Typhimurium Lt2 L-Talarate/Galactarate Dehydratase 128 2.2 Glycerol CSA • PDB • PDBSum
2PP1 Crystal Structure Of L-Talarate/Galactarate Dehydratase From Salmonella Typhimurium Lt2 Liganded With Mg And L-Lyxarohydroxamate L-Talarate/Galactarate Dehydratase 128 2.2 Magnesium Ion • (2R,3S,4R)-2,3,4-Trihydroxy-5-(Hydroxyamino)-5-Oxopentanoic Acid CSA • PDB • PDBSum
2PP3 Crystal Structure Of L-Talarate/Galactarate Dehydratase Mutant K197A Liganded With Mg And L-Glucarate L-Talarate/Galactarate Dehydratase 126 2.2 Yes Magnesium Ion • L-Glucaric Acid 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, 2:39 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.