Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family L-talarate/galactarate dehydratase

  ⌊ FunctionalDomain L-talarate/galactarate dehydratase (ID 5914)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code IES PubMed:17649980
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Polaromonas sp. JS666 Taxon ID: 296591 499800672 WP_011481406.1 (RefSeq) URP
Polaromonas sp. JS666 Taxon ID: 296591 91695570 ABE42399.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a Q12GE3 Q12GE3_POLSJ (TrEMBL)

Sequence

Length of Enzyme (full-length): 383 | Length of Functional Domain: 377

1       10        20        30        40        50        60

MKTTTSSTPSDRITWVRISSCYLPLATPISDAKVLTGRQKPMTEIAILFAEIETAGGHQG
LGFSYSKRAGGPGQFAHAREIAPALIGEDPSDIAKLWDKLCWAGASAGRSGLSTQAIGAF
DVALWDLKAKRAGLSLAKLLGSYRDSVRCYNTSGGFLHTPIDQLMVNASASIERGIGGIK
LKVGQPDGALDIARVTAVRKHLGDAVPLMVDANQQWDRPTAQRMCRIFEPFNLVWIEEPL
DAYDHEGHAALALQFDTPIATGEMLTSAAEHGDLIRHRAADYLMPDAPRVGGITPFLKIA
SLAEHAGLMLAPHFAMELHVHLAAAYPREPWVEHFEWLEPLFNERIEIRDGRMLVPTRPG
LGLTLSGQVKAWTREEAQVGTRP
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
211 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
237 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
263 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
211 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
237 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
263 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
286 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
313 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
67 Lys (K) side chain assists catalytic His activation -- spectator ICS PubMed:17649980
182 Lys (K) side chain abstracts proton from C2 of galactarate proton relay -- reactant ICS PubMed:17649980
211 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:17649980
237 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:17649980
263 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:17649980
286 Asp (D) side chain Controls pKa of catalytic His activation -- spectator ICS PubMed:17649980
313 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

Catalyzed Reactions

galactarate dehydratase

+
galactarate(2-)
16537		 5-dehydro-4-deoxy-D-glucarate(2-)
42819		 water
15377

EC: 4.2.1.42 | IntEnz: 4.2.1.42 | Kegg: 4.2.1.42 | BioCyc: 4.2.1.42 | BRENDA: 4.2.1.42

L-talarate dehydratase

+
L-altrarate(2-)
37547		 5-dehydro-4-deoxy-D-glucarate(2-)
42819		 water
15377

EC: 4.2.1.156 | IntEnz: 4.2.1.156 | Kegg: 4.2.1.156 | BioCyc: 4.2.1.156 | BRENDA: 4.2.1.156

L-talarate epimerase

L-altrarate(2-)
37547		 galactarate(2-)
16537

EC: 5.1.-.- | IntEnz: 5.1.-.- | Kegg: 5.1.-.- | BioCyc: 5.1.-.- | BRENDA: 5.1.-.- |

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, 2:34 a.m. update curation agent updateSFLDGIs.py setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.