Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup mandelate racemase

     ⌊ Family mandelate racemase

  ⌊ FunctionalDomain uncharacterized mandelate racemase subgroup sequence (ID 1558438)

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
Pseudomonas putida Taxon ID: 303 518268536 WP_019438744.1 (RefSeq) URP
Pseudomonas putida S12 Taxon ID: 1215087 734576867 AJA14081.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a A0A0A7PVN6 A0A0A7PVN6_PSEPU (TrEMBL)

Sequence

Length of Enzyme (full-length): 359 | Length of Functional Domain: 359

1       10        20        30        40        50        60

MSEVLITGLRTRAVNVPLAYPVHTAVGTVGTAPLVLIDLATSAGVVGHSYLFAYTPVALK
SLKQLLDDMAALIVNELLAPVSLEAMLAKRFCLAGYTGLIRMAAAGIDMAAWDALGKVHE
TPLVKLLGANARPVQTYDSHSLDGVKLATERAVTAAELGFRAVKTKIGYPTLDQDLAVVR
SIRQAVGDDFGIMVDYNQSLDVPAAIKRSQALQQEGVTWIEEPTLQHDYEGHQRIQSKLD
VPVQMGENWLGPEEMFKALSVGACRLAMPDAMKIGGVTGWIRASALAQQFGIPMSSHLFQ
EISAHLLAATPTAHWLERLDLAGSVIEPTLTFEGGNAVIPDLPGVGIIWREKEIEKYLV
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
195 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
221 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
247 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
195 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
221 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
247 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
270 Asp (D) side chain controls pKa of catalytic His perturbates pKa -- spectator IDA
297 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
166 Lys (K) side chain abstracts alpha proton from s-mandelate (base) proton relay -- reactant IDA PubMed:7893690
195 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:8292591
221 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:8292591
247 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:8292591
270 Asp (D) side chain controls pKa of H297 perturbates pKa -- spectator IDA PubMed:8639525
297 His (H) side chain abstracts alpha proton from r-mandelate (base) proton relay -- reactant IDA PubMed:1909893
317 Glu (E) side chain general acid catalyst, stabilizes transition state electrostatic stabiliser -- spectator,
proton relay -- reactant 		IDA PubMed:7893689

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1MDR The Role Of Lysine 166 In The Mechanism Of Mandelate Racemase From Pseudomonas Putida: Mechanistic And Crystallographic Evidence For Stereospecific Alkylation By (R)-Alpha-Phenylglycidate Mandelate Racemase 9 2.1 Magnesium Ion • Atrolactic Acid (2-Phenyl-Lactic Acid) CSA • PDB • PDBSum
4FP1 P. Putida Mandelate Racemase Co-Crystallized With 3,3,3-Trifluoro-2-Hydroxy-2-(Trifluoromethyl) Propionic Acid Mandelate Racemase 9 1.68 Magnesium Ion • 3,3,3-Trifluoro-2-Hydroxy-2-(Trifluoromethyl)Propanoic Acid CSA • PDB • PDBSum
3UXL P. Putida Mandelate Racemase Co-Crystallized With The Intermediate Analogue Cupferron Mandelate Racemase 9 2.2 Magnesium Ion • 1-Hydroxy-2-Oxo-1-Phenylhydrazine CSA • PDB • PDBSum
3UXK P. Putida Mandelate Racemase Co-Crystallized With The Intermediate Analogue Benzohydroxamate Mandelate Racemase 9 2.2 Magnesium Ion • Benzhydroxamic Acid CSA • PDB • PDBSum
4M6U P. Putida Mandelate Racemase Co-Crystallized With Tartronic Acid Mandelate Racemase 9 1.8 Magnesium Ion • Tartronate CSA • PDB • PDBSum
2MNR Mechanism Of The Reaction Catalyzed By Mandelate Racemase. 2. Crystal Structure Of Mandelate Racemase At 2.5 Angstroms Resolution: Identification Of The Active Site And Possible Catalytic Residues Mandelate Racemase 9 1.9 Manganese (Ii) Ion • Sulfate Ion CSA • PDB • PDBSum
1MNS On The Role Of Lysine 166 In The Mechanism Of Mandelate Racemase From Pseudomonas Putida: Mechanistic And Crystallographic Evidence For Stereospecific Alkylation By (R)-Alpha-Phenylglycidate Mandelate Racemase 9 2.0 Magnesium Ion • Atrolactic Acid (2-Phenyl-Lactic Acid) CSA • PDB • PDBSum
1MRA Mandelate Racemase Mutant D270N Co-Crystallized With (S)-Atrolactate Mandelate Racemase 9 2.1 Yes Magnesium Ion • Atrolactic Acid (2-Phenyl-Lactic Acid) CSA • PDB • PDBSum
1MDL Mandelate Racemase Mutant K166R Co-Crystallized With (R)-Mandelate Mandelate Racemase 9 1.85 Yes Magnesium Ion
(2 more ⇓) 		CSA • PDB • PDBSum
1DTN Mandelate Racemase Mutant D270N Co-Crystallized With (S)-Atrolactate Mandelate Racemase 9 2.1 Yes Magnesium Ion • Atrolactic Acid (2-Phenyl-Lactic Acid) CSA • PDB • PDBSum
4HNC P. Putida C92S/K166C/C264S Mandelate Racemase Co-Crystallized With Benzilic Acid Mandelate Racemase 9 1.89 Yes Magnesium Ion • Hydroxy(Diphenyl)Acetic 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, 3:31 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
April 7, 2015, 6:56 a.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.