Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family L-talarate/galactarate dehydratase

  ⌊ FunctionalDomain L-talarate/galactarate dehydratase (ID 18835)

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
Polaromonas sp. JS666 Taxon ID: 296591 169404767 URP
Polaromonas sp. JS666 Taxon ID: 296591 169404766 URP
Polaromonas sp. JS666 Taxon ID: 296591 169404765 URP
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Sequence

Length of Enzyme (full-length): 393 | Length of Functional Domain: 377

1       10        20        30        40        50        60

MSLKTTTSSTPSDRITWVRISSCYLPLATPISDAKVLTGRQKPMTEIAILFAEIETAGGH
QGLGFSYSKRAGGPGQFAHAREIAPALIGEDPSDIAKLWDKLCWAGASAGRSGLSTQAIG
AFDVALWDLKAKRAGLSLAKLLGSYRDSVRCYNTSGGFLHTPIDQLMVNASASIERGIGG
IKLKVGQPDGALDIARVTAVRKHLGDAVPLMVDANQQWDRPTAQRMCRIFEPFNLVWIEE
PLDAYDHEGHAALALQFDTPIATGEMLTSAAEHGDLIRHRAADYLMPDAPRVGGITPFLK
IASLAEHAGLMLAPHFAMELHVHLAAAYPREPWVEHFEWLEPLFNERIEIRDGRMLVPTR
PGLGLTLSGQVKAWTREEAQVGTRPEGHHHHHH
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
213 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
239 Glu (E) 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
Subgroup CAR This EFD conserves 5/5 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
213 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
239 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
265 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
288 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
315 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
69 Lys (K) side chain assists catalytic His activation -- spectator ICS PubMed:17649980
184 Lys (K) side chain abstracts proton from C2 of galactarate proton relay -- reactant ICS PubMed:17649980
213 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:17649980
239 Glu (E) 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
288 Asp (D) side chain Controls pKa of catalytic His activation -- spectator ICS PubMed:17649980
315 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
3CB3 Crystal Structure Of L-Talarate Dehydratase From Polaromonas Sp. Js666 Complexed With Mg And L-Glucarate Mandelate Racemase/Muconate Lactonizing Enzyme 3 2.0 Magnesium Ion • L-Glucaric Acid CSA • PDB • PDBSum
2OG9 Crystal Structure Of Mandelate Racemase/Muconate Lactonizing Enzyme From Polaromonas Sp. Js666 Mandelate Racemase/Muconate Lactonizing Enzyme 3 1.9 Selenomethionine • Calcium Ion 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 updateSFLD2.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.