Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family L-talarate/galactarate dehydratase

  ⌊ FunctionalDomain L-talarate/galactarate dehydratase (ID 425272)

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
Enterobacter radicincitans Taxon ID: 283686 494616881 WP_007375123.1 (RefSeq)
Kosakonia radicincitans UMEnt01/12 Taxon ID: 1455607 635194300 KDE38129.1 (Genbank) URP
Enterobacter radicincitans DSM 16656 Taxon ID: 1177180 396090316 EJI87888.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a A0A1V0LDW7 A0A1V0LDW7_9ENTR (TrEMBL)
n/a A0A1K1WAB8 A0A1K1WAB8_9ENTR (TrEMBL)
n/a A0A1T5HMK3 A0A1T5HMK3_9ENTR (TrEMBL)

Sequence

Length of Enzyme (full-length): 398 | Length of Functional Domain: 377

1       10        20        30        40        50        60

MTVSANSDAVTYAKAAGAKTAAETGDRIAWVKLSLAFLPLATPVSDAKVLTGRQKPLTEV
AIIIAEIRSRDGFEGVGFSYSKRAGGQGIYAHAKEIADNLLGEDPNDIDKIYTKLLWAGA
SVGRSGMAVQAISPIDIALWDMKAKRAGLPLAKLLGAHRDSVQCYNTSGGFLHTPLDQVL
KNVIISRENGIGGIKIKVGQPDTKEDIRRLTAVREALGDDFPLMVDANQQWDRETAIRMG
RQMEKFNLIWIEEPLDAYDVEGHAQLAAALDTPIATGEMLTSFREHEQLILGNASDFVQP
DAPRVGGISPFLKIMDLAAKHGRKLAPHFAMEVHLHLSAAYPLEPWLEHFEWLNPLFNEQ
LELRDGRMYVSDRHGLGFSISEQARAWTQTSCEFGKRP
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
226 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
252 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
278 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
226 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
252 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
278 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
301 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
328 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
82 Lys (K) side chain assists catalytic His activation -- spectator ICS PubMed:17649980
197 Lys (K) side chain abstracts proton from C2 of galactarate proton relay -- reactant ICS PubMed:17649980
226 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:17649980
252 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:17649980
278 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:17649980
301 Asp (D) side chain Controls pKa of catalytic His activation -- spectator ICS PubMed:17649980
328 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, 2:45 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.