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P11444

- MANR_PSEPU

UniProt

P11444 - MANR_PSEPU

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Protein

Mandelate racemase

Gene

mdlA

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-mandelate = (R)-mandelate.3 Publications

Cofactori

Divalent metal ions. Magnesium seems to be the preferred ion.3 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei166 – 1661Proton acceptor; specific for S-mandelate
Metal bindingi195 – 1951Magnesium2 Publications1 Publication
Metal bindingi221 – 2211Magnesium2 Publications1 Publication
Metal bindingi247 – 2471Magnesium2 Publications1 Publication
Active sitei297 – 2971Proton acceptor; specific for R-mandelate
Binding sitei317 – 3171Substrate2 Publications1 Publication

GO - Molecular functioni

  1. mandelate racemase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cellular amino acid catabolic process Source: InterPro
  2. mandelate catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Mandelate pathway

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-2421.
UniPathwayiUPA00873; UER00852.

Names & Taxonomyi

Protein namesi
Recommended name:
Mandelate racemase (EC:5.1.2.23 Publications)
Short name:
MR
Gene namesi
Name:mdlA
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi166 – 1661K → A, M or Q: Loss of activity. 1 Publication
Mutagenesisi297 – 2971H → N: Loss of activity. 1 Publication
Mutagenesisi317 – 3171E → Q: Reduces activity 10000-fold. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Mandelate racemasePRO_0000171247Add
BLAST

Interactioni

Subunit structurei

Homooctamer.1 Publication

Structurei

Secondary structure

1
359
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 1612
Beta strandi22 – 243
Beta strandi27 – 293
Beta strandi31 – 4111
Beta strandi46 – 527
Helixi56 – 583
Helixi59 – 7315
Beta strandi76 – 783
Helixi80 – 9011
Turni91 – 944
Helixi98 – 11821
Helixi123 – 1264
Beta strandi134 – 1396
Helixi144 – 15714
Beta strandi161 – 1666
Helixi172 – 18615
Beta strandi188 – 1958
Helixi202 – 21413
Beta strandi218 – 2214
Helixi229 – 2368
Beta strandi243 – 2453
Helixi252 – 2609
Beta strandi265 – 2673
Turni271 – 2755
Helixi276 – 29015
Helixi300 – 3089
Beta strandi316 – 3183
Turni321 – 3255
Beta strandi330 – 3334
Beta strandi336 – 3383
Beta strandi341 – 3444
Helixi351 – 3577

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP11444.
SMRiP11444. Positions 3-359.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11444.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
InterProiIPR029065. Enolase_C-like.
IPR029017. Enolase_N_like.
IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
IPR013342. Mandelate_racemase_C.
IPR013341. Mandelate_racemase_N_dom.
IPR001354. MR/MLE/MAL.
[Graphical view]
PANTHERiPTHR13794. PTHR13794. 1 hit.
PfamiPF01188. MR_MLE. 1 hit.
PF02746. MR_MLE_N. 1 hit.
[Graphical view]
SMARTiSM00922. MR_MLE. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
PROSITEiPS00908. MR_MLE_1. 1 hit.
PS00909. MR_MLE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11444-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEVLITGLR TRAVNVPLAY PVHTAVGTVG TAPLVLIDLA TSAGVVGHSY
60 70 80 90 100
LFAYTPVALK SLKQLLDDMA AMIVNEPLAP VSLEAMLAKR FCLAGYTGLI
110 120 130 140 150
RMAAAGIDMA AWDALGKVHE TPLVKLLGAN ARPVQAYDSH SLDGVKLATE
160 170 180 190 200
RAVTAAELGF RAVKTKIGYP ALDQDLAVVR SIRQAVGDDF GIMVDYNQSL
210 220 230 240 250
DVPAAIKRSQ ALQQEGVTWI EEPTLQHDYE GHQRIQSKLN VPVQMGENWL
260 270 280 290 300
GPEEMFKALS IGACRLAMPD AMKIGGVTGW IRASALAQQF GIPMSSHLFQ
310 320 330 340 350
EISAHLLAAT PTAHWLERLD LAGSVIEPTL TFEGGNAVIP DLPGVGIIWR

EKEIGKYLV
Length:359
Mass (Da):38,565
Last modified:October 1, 1989 - v1
Checksum:i1C105BCA021F4028
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19043 Genomic DNA. Translation: AAA25887.1.
AY143338 Genomic DNA. Translation: AAC15504.1.
PIRiA28700.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19043 Genomic DNA. Translation: AAA25887.1 .
AY143338 Genomic DNA. Translation: AAC15504.1 .
PIRi A28700.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DTN X-ray 2.10 A 1-359 [» ]
1MDL X-ray 1.85 A 1-359 [» ]
1MDR X-ray 2.10 A 1-359 [» ]
1MNS X-ray 2.00 A 3-359 [» ]
1MRA X-ray 2.10 A 1-359 [» ]
2MNR X-ray 1.90 A 3-359 [» ]
3UXK X-ray 2.20 A/B/C/D 1-359 [» ]
3UXL X-ray 2.20 A/B/C/D 1-359 [» ]
4FP1 X-ray 1.68 A/B 1-359 [» ]
4HNC X-ray 1.89 A/B 1-359 [» ]
4M6U X-ray 1.80 A/B 1-359 [» ]
ProteinModelPortali P11444.
SMRi P11444. Positions 3-359.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P11444.
ChEMBLi CHEMBL4739.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00873 ; UER00852 .
BioCyci MetaCyc:MONOMER-2421.

Miscellaneous databases

EvolutionaryTracei P11444.

Family and domain databases

Gene3Di 3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
InterProi IPR029065. Enolase_C-like.
IPR029017. Enolase_N_like.
IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
IPR013342. Mandelate_racemase_C.
IPR013341. Mandelate_racemase_N_dom.
IPR001354. MR/MLE/MAL.
[Graphical view ]
PANTHERi PTHR13794. PTHR13794. 1 hit.
Pfami PF01188. MR_MLE. 1 hit.
PF02746. MR_MLE_N. 1 hit.
[Graphical view ]
SMARTi SM00922. MR_MLE. 1 hit.
[Graphical view ]
SUPFAMi SSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
PROSITEi PS00908. MR_MLE_1. 1 hit.
PS00909. MR_MLE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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, CATALYTIC ACTIVITY.
  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 (1.90 ANGSTROMS) OF 3-359 IN COMPLEX WITH MANGANESE, COFACTOR.
  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 IN COMPLEX WITH MAGNESIUM, COFACTOR, MUTAGENESIS OF GLU-317, CATALYTIC ACTIVITY.
  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 AND MAGNESIUM, COFACTOR, MUTAGENESIS OF LYS-166, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiMANR_PSEPU
AccessioniPrimary (citable) accession number: P11444
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: October 29, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3