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Protein

Mandelate racemase

Gene

mdlA

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

Functioni

Catalytic activityi

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

Cofactori

Mg2+3 PublicationsNote: Divalent metal ions. Magnesium seems to be the preferred ion.3 Publications

Pathwayi: (R)-mandelate degradation

This protein is involved in step 1 of the subpathway that synthesizes benzoate from (R)-mandelate.Curated
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Mandelate racemase (mdlA)
  2. (S)-mandelate dehydrogenase (mdlB)
  3. Benzoylformate decarboxylase (mdlC)
  4. NAD(P)-dependent benzaldehyde dehydrogenase (mdlD)
This subpathway is part of the pathway (R)-mandelate degradation, which is itself part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes benzoate from (R)-mandelate, the pathway (R)-mandelate degradation and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei166Proton acceptor; specific for S-mandelate1
Metal bindingi195Magnesium1 Publication2 Publications1
Metal bindingi221Magnesium1 Publication2 Publications1
Metal bindingi247Magnesium1 Publication2 Publications1
Active sitei297Proton acceptor; specific for R-mandelate1
Binding sitei317Substrate1 Publication2 Publications1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Mandelate pathway

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-2421.
BRENDAi5.1.2.2. 5092.
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)DescriptionActionsGraphical viewLength
Mutagenesisi166K → A, M or Q: Loss of activity. 1 Publication1
Mutagenesisi297H → N: Loss of activity. 1 Publication1
Mutagenesisi317E → Q: Reduces activity 10000-fold. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL4739.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001712471 – 359Mandelate racemaseAdd BLAST359

Interactioni

Subunit structurei

Homooctamer.1 Publication

Chemistry databases

BindingDBiP11444.

Structurei

Secondary structure

1359
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 23Combined sources19
Beta strandi28 – 41Combined sources14
Beta strandi46 – 52Combined sources7
Helixi56 – 58Combined sources3
Helixi59 – 73Combined sources15
Beta strandi76 – 78Combined sources3
Helixi80 – 90Combined sources11
Turni91 – 94Combined sources4
Helixi98 – 118Combined sources21
Helixi123 – 126Combined sources4
Beta strandi134 – 139Combined sources6
Helixi144 – 157Combined sources14
Beta strandi161 – 166Combined sources6
Helixi172 – 186Combined sources15
Beta strandi188 – 195Combined sources8
Helixi202 – 215Combined sources14
Beta strandi218 – 221Combined sources4
Helixi229 – 237Combined sources9
Beta strandi243 – 245Combined sources3
Helixi252 – 260Combined sources9
Beta strandi265 – 267Combined sources3
Turni271 – 275Combined sources5
Helixi276 – 290Combined sources15
Helixi300 – 308Combined sources9
Beta strandi316 – 318Combined sources3
Turni321 – 325Combined sources5
Beta strandi330 – 333Combined sources4
Beta strandi336 – 338Combined sources3
Beta strandi341 – 344Combined sources4
Helixi351 – 357Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4X2PX-ray1.65A1-359[»]
ProteinModelPortaliP11444.
SMRiP11444.
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.
IPR015654. Mandelate_racemase.
IPR013342. Mandelate_racemase_C.
IPR013341. Mandelate_racemase_N_dom.
IPR001354. MR/MLE/MAL.
[Graphical view]
PANTHERiPTHR13794. PTHR13794. 1 hit.
PfamiPF13378. MR_MLE_C. 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:
EMBLi
GenBanki
DDBJi
Links Updated
M19043 Genomic DNA. Translation: AAA25887.1.
AY143338 Genomic DNA. Translation: AAC15504.1.
PIRiA28700.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19043 Genomic DNA. Translation: AAA25887.1.
AY143338 Genomic DNA. Translation: AAC15504.1.
PIRiA28700.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4X2PX-ray1.65A1-359[»]
ProteinModelPortaliP11444.
SMRiP11444.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP11444.
ChEMBLiCHEMBL4739.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00873; UER00852.
BioCyciMetaCyc:MONOMER-2421.
BRENDAi5.1.2.2. 5092.

Miscellaneous databases

EvolutionaryTraceiP11444.

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.
IPR015654. Mandelate_racemase.
IPR013342. Mandelate_racemase_C.
IPR013341. Mandelate_racemase_N_dom.
IPR001354. MR/MLE/MAL.
[Graphical view]
PANTHERiPTHR13794. PTHR13794. 1 hit.
PfamiPF13378. MR_MLE_C. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 106 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.