Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family L-talarate/galactarate dehydratase

  ⌊ FunctionalDomain L-talarate/galactarate dehydratase (ID 92424)

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 Typhimurium str. USDA-ARS-USMARC-1909 Taxon ID: 1454642 808190833 AKD10376.1 (Genbank) URP
Salmonella enterica subsp. enterica serovar Typhimurium str. USDA-ARS-USMARC-1899 Taxon ID: 1454639 764062065 AJQ80836.1 (Genbank) URP
Salmonella enterica subsp. enterica serovar Newport str. USDA-ARS-USMARC-1927 Taxon ID: 1454620 764052960 AJQ71733.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a E8XG12 E8XG12_SALT4 (TrEMBL)
n/a V7ITY2 V7ITY2_SALET (TrEMBL)
n/a M7RKQ2 M7RKQ2_SALDU (TrEMBL)

Sequence

Length of Enzyme (full-length): 405 | Length of Functional Domain: 377

1       10        20        30        40        50        60

MIIRRKKMALSANSDAVTYAKAANTRTAAETGDRIEWVKLSLAFLPLATPVSDAKVLTGR
QKPLTEVAIIIAEIRSRDGFEGVGFSYSKRAGGQGIYAHAKEIADNLLGEDPNDIDKIYT
KLLWAGASVGRSGMAVQAISPIDIALWDMKAKRAGLPLAKLLGAHRDSVQCYNTSGGFLH
TPLDQVLKNVVISRENGIGGIKLKVGQPNCAEDIRRLTAVREALGDEFPLMVDANQQWDR
ETAIRMGRKMEQFNLIWIEEPLDAYDIEGHAQLAAALDTPIATGEMLTSFREHEQLILGN
ASDFVQPDAPRVGGISPFLKIMDLAAKHGRKLAPHFAMEVHLHLSAAYPLEPWLEHFEWL
NPLFNEQLELRDGRMWISDRHGLGFTLSEQARRWTQLTCEFGKRP
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
233 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
259 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
285 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
233 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
259 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
285 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
308 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
335 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
89 Lys (K) side chain assists catalytic His activation -- spectator ICS PubMed:17649980
204 Lys (K) side chain abstracts proton from C2 of galactarate proton relay -- reactant ICS PubMed:17649980
233 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:17649980
259 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:17649980
285 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:17649980
308 Asp (D) side chain Controls pKa of catalytic His activation -- spectator ICS PubMed:17649980
335 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, 3:17 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.