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P11444 (MANR_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mandelate racemase

Short name=MR
EC=5.1.2.2
Gene names
Name:mdlA
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

(S)-mandelate = (R)-mandelate.

Cofactor

Divalent metal ions. Magnesium seems to be the preferred ion.

Pathway

Aromatic compound metabolism; (R)-mandelate degradation; benzoate from (R)-mandelate: step 1/4.

Subunit structure

Homooctamer.

Sequence similarities

Belongs to the mandelate racemase/muconate lactonizing enzyme family.

Ontologies

Keywords
   Biological processMandelate pathway
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcellular amino acid catabolic process

Inferred from electronic annotation. Source: InterPro

mandelate catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionmandelate racemase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Mandelate racemase
PRO_0000171247

Sites

Active site1661Proton acceptor; specific for S-mandelate
Active site2971Proton acceptor; specific for R-mandelate
Metal binding1951Magnesium
Metal binding2211Magnesium
Metal binding2471Magnesium
Binding site3171Substrate

Experimental info

Mutagenesis1661K → A, M or Q: Loss of activity. Ref.7
Mutagenesis2971H → N: Loss of activity. Ref.4
Mutagenesis3171E → Q: Reduces activity 10000-fold.

Secondary structure

.............................................................. 359
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11444 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 1C105BCA021F4028

FASTA35938,565
        10         20         30         40         50         60 
MSEVLITGLR TRAVNVPLAY PVHTAVGTVG TAPLVLIDLA TSAGVVGHSY LFAYTPVALK 

        70         80         90        100        110        120 
SLKQLLDDMA AMIVNEPLAP VSLEAMLAKR FCLAGYTGLI RMAAAGIDMA AWDALGKVHE 

       130        140        150        160        170        180 
TPLVKLLGAN ARPVQAYDSH SLDGVKLATE RAVTAAELGF RAVKTKIGYP ALDQDLAVVR 

       190        200        210        220        230        240 
SIRQAVGDDF GIMVDYNQSL DVPAAIKRSQ ALQQEGVTWI EEPTLQHDYE GHQRIQSKLN 

       250        260        270        280        290        300 
VPVQMGENWL GPEEMFKALS IGACRLAMPD AMKIGGVTGW IRASALAQQF GIPMSSHLFQ 

       310        320        330        340        350 
EISAHLLAAT PTAHWLERLD LAGSVIEPTL TFEGGNAVIP DLPGVGIIWR EKEIGKYLV 

« Hide

References

[1]"Cloning, DNA sequence analysis, and expression in Escherichia coli of the gene for mandelate racemase from Pseudomonas putida."
Ransom S.C., Gerlt J.A., Powers V.M., Kenyon G.L.
Biochemistry 27:540-545(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 12633 / DSM 291 / JCM 13063 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90.
[2]"Mandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli."
Tsou A.Y., Ransom S.C., Gerlt J.A., Buechter D.D., Babbitt P.C., Kenyon G.L.
Biochemistry 29:9856-9862(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 12633 / DSM 291 / JCM 13063 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90.
[3]"Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous."
Neidhart D.J., Kenyon G.L., Gerlt J.A., Petsko G.A.
Nature 347:692-694(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: SIMILARITY TO MLE.
[4]"Mechanism of the reaction catalyzed by mandelate racemase. 3. Asymmetry in reactions catalyzed by the H297N mutant."
Landro J.A., Kallarakal A.T., Ransom S.C., Gerlt J.A., Kozarich J.W., Neidhart D.J., Kenyon G.L.
Biochemistry 30:9274-9281(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-297.
[5]"Mechanism of the reaction catalyzed by mandelate racemase. 2. Crystal structure of mandelate racemase at 2.5-A resolution: identification of the active site and possible catalytic residues."
Neidhart D.J., Howell P.L., Petsko G.A., Powers V.M., Li R.S., Kenyon G.L., Gerlt J.A.
Biochemistry 30:9264-9273(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[6]"Mechanism of the reaction catalyzed by mandelate racemase: importance of electrophilic catalysis by glutamic acid 317."
Mitra B., Kallarakal A.T., Kozarich J.W., Gerlt J.A., Clifton J.G., Petsko G.A., Kenyon G.L.
Biochemistry 34:2777-2787(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT GLN-317.
[7]"Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the K166R mutant."
Kallarakal A.T., Mitra B., Kozarich J.W., Gerlt J.A., Clifton J.G., Petsko G.A., Kenyon G.L.
Biochemistry 34:2788-2797(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT ARG-166 IN COMPLEX WITH SUBSTRATE, MUTAGENESIS OF LYS-166.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M19043 Genomic DNA. Translation: AAA25887.1.
AY143338 Genomic DNA. Translation: AAC15504.1.
PIRA28700.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DTNX-ray2.10A1-359[»]
1MDLX-ray1.85A1-359[»]
1MDRX-ray2.10A1-359[»]
1MNSX-ray2.00A3-359[»]
1MRAX-ray2.10A1-359[»]
2MNRX-ray1.90A3-359[»]
3UXKX-ray2.20A/B/C/D1-359[»]
3UXLX-ray2.20A/B/C/D1-359[»]
4FP1X-ray1.68A/B1-359[»]
4HNCX-ray1.89A/B1-359[»]
4M6UX-ray1.80A/B1-359[»]
ProteinModelPortalP11444.
SMRP11444. Positions 3-359.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP11444.
ChEMBLCHEMBL4739.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-2421.
UniPathwayUPA00873; UER00852.

Family and domain databases

InterProIPR018110. Mandel_Rmase/mucon_lact_enz_CS.
IPR013342. Mandelate_racemase_C.
IPR013341. Mandelate_racemase_N.
IPR001354. MR_MLE.
[Graphical view]
PANTHERPTHR13794. PTHR13794. 1 hit.
PfamPF01188. MR_MLE. 1 hit.
PF02746. MR_MLE_N. 1 hit.
[Graphical view]
SMARTSM00922. MR_MLE. 1 hit.
[Graphical view]
PROSITEPS00908. MR_MLE_1. 1 hit.
PS00909. MR_MLE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP11444.

Entry information

Entry nameMANR_PSEPU
AccessionPrimary (citable) accession number: P11444
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: April 16, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways