Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family L-talarate/galactarate dehydratase

  ⌊ FunctionalDomain L-talarate/galactarate dehydratase (ID 279623)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Salmonella enterica subsp. enterica serovar Enteritidis str. 2010K-0286 Taxon ID: 1192593 514650303 EPJ08305.1 (Genbank) URP
Salmonella enterica subsp. enterica serovar Enteritidis str. 2010K-0284 Taxon ID: 1192592 514646373 EPJ04693.1 (Genbank) URP
Salmonella enterica subsp. enterica serovar Enteritidis str. 2010K-0271 Taxon ID: 1192591 514633216 EPI92286.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a G5R788 G5R788_SALSE (TrEMBL)
n/a S4HWU7 S4HWU7_SALEN (TrEMBL)

Sequence

Length of Enzyme (full-length): 411 | Length of Functional Domain: 377

1       10        20        30        40        50        60

MLAQSFCDYQEKKMALSANSDAVTYAKAANTRTAAETGDRIEWVKLSLAFLPLATPVSDA
KVLTGRQKPLTEVAIIIAEIRSRDGFEGVGFSYSKRAGGQGIYAHAKEIADNLLGEDPND
IDKIYTKLLWAGASVGRSGMAVQAISPIDIALWDMKAKRAGLPLAKLLGAHRDSVQCYNT
SGGFLHTPLDQVLKNVVISRENGIGGIKLKVGQPNCAEDIRRLTAVREALGDEFPLMVDA
NQQWDRETAIRMGRKMEQFNLIWIEEPLDAYDIEGHAQLAAALDTPIATGEMLTSFREHE
QLILGNASDFVQPDAPRVGGISPFLKIMDLAAKHGRKLAPHFAMEVHLHLSAAYPLEPWL
EHFEWLNPLFNEQLELRDGRMWISDRHGLGFTLSEQARRWTQLTCEFGKRP
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
239 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
265 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
291 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
239 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
265 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
291 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
314 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
341 His (H) side chain proton abstraction (general base) proton relay -- reactant IDA
Family CAR This EFD conserves 7/7 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
95 Lys (K) side chain assists catalytic His activation -- spectator ICS PubMed:17649980
210 Lys (K) side chain abstracts proton from C2 of galactarate proton relay -- reactant ICS PubMed:17649980
239 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:17649980
265 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:17649980
291 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:17649980
314 Asp (D) side chain Controls pKa of catalytic His activation -- spectator ICS PubMed:17649980
341 His (H) side chain abstracts proton from C2 of L-talarate; donates proton to enolate anion intermediate, facilitating departure of 3-OH leaving group; donates proton to C3 to form product proton relay -- reactant ICS PubMed:17649980

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
Aug. 1, 2014, 2:39 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.