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Protein

(S)-mandelate dehydrogenase

Gene

mdlB

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

Functioni

Reduction of (S)-mandelate to benzoylformate.

Catalytic activityi

(S)-2-hydroxy-2-phenylacetate + acceptor = 2-oxo-2-phenylacetate + reduced acceptor.

Cofactori

Pathwayi: (R)-mandelate degradation

This protein is involved in step 2 of the subpathway that synthesizes benzoate from (R)-mandelate.
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
Binding sitei26SubstratePROSITE-ProRule annotation1
Binding sitei108FMNPROSITE-ProRule annotation2 Publications1
Binding sitei129FMNPROSITE-ProRule annotation2 Publications1
Binding sitei131SubstratePROSITE-ProRule annotation1
Binding sitei156FMNPROSITE-ProRule annotation2 Publications1
Binding sitei165SubstratePROSITE-ProRule annotation1
Binding sitei250FMNPROSITE-ProRule annotation2 Publications1
Active sitei274Proton acceptorPROSITE-ProRule annotation1
Binding sitei277SubstratePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi303 – 327FMNPROSITE-ProRule annotation2 PublicationsAdd BLAST25

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism, Mandelate pathway

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-2422.
BRENDAi1.1.99.31. 5092.
SABIO-RKP20932.
UniPathwayiUPA00873; UER00853.

Names & Taxonomyi

Protein namesi
Recommended name:
(S)-mandelate dehydrogenase (EC:1.1.99.31)
Alternative name(s):
L(+)-mandelate dehydrogenase
Short name:
MDH
Gene namesi
Name:mdlB
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002063271 – 393(S)-mandelate dehydrogenaseAdd BLAST393

Interactioni

Subunit structurei

Homotetramer.2 Publications

Structurei

Secondary structure

1393
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 18Combined sources11
Helixi21 – 28Combined sources8
Helixi35 – 42Combined sources8
Helixi43 – 46Combined sources4
Beta strandi47 – 49Combined sources3
Beta strandi64 – 66Combined sources3
Beta strandi69 – 77Combined sources9
Helixi83 – 85Combined sources3
Helixi90 – 101Combined sources12
Beta strandi105 – 107Combined sources3
Helixi115 – 121Combined sources7
Beta strandi126 – 130Combined sources5
Helixi135 – 147Combined sources13
Beta strandi152 – 156Combined sources5
Helixi166 – 171Combined sources6
Turni216 – 218Combined sources3
Helixi219 – 222Combined sources4
Helixi233 – 242Combined sources10
Beta strandi245 – 252Combined sources8
Helixi255 – 263Combined sources9
Beta strandi267 – 271Combined sources5
Helixi274 – 276Combined sources3
Helixi285 – 287Combined sources3
Helixi289 – 296Combined sources8
Beta strandi300 – 302Combined sources3
Helixi309 – 317Combined sources9
Beta strandi323 – 326Combined sources4
Helixi327 – 359Combined sources33
Helixi364 – 366Combined sources3
Helixi369 – 371Combined sources3
Beta strandi372 – 374Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HUVX-ray2.15A1-176[»]
A216-393[»]
1P4CX-ray1.35A1-176[»]
A216-393[»]
1P5BX-ray1.35A1-176[»]
A216-393[»]
2A7NX-ray1.80A1-176[»]
A216-393[»]
2A7PX-ray2.20A1-176[»]
A216-393[»]
2A85X-ray2.50A1-176[»]
A216-393[»]
3GIYX-ray1.60A1-176[»]
A216-393[»]
ProteinModelPortaliP20932.
SMRiP20932.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20932.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 377FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd BLAST377

Sequence similaritiesi

Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.PROSITE-ProRule annotation
Contains 1 FMN hydroxy acid dehydrogenase domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
PfamiPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20932-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQNLFNVED YRKLRQKRLP KMVYDYLEGG AEDEYGVKHN RDVFQQWRFK
60 70 80 90 100
PKRLVDVSRR SLQAEVLGKR QSMPLLIGPT GLNGALWPKG DLALARAATK
110 120 130 140 150
AGIPFVLSTA SNMSIEDLAR QCDGDLWFQL YVIHREIAQG MVLKALHTGY
160 170 180 190 200
TTLVLTTDVA VNGYRERDLH NRFKIPMSYS AKVVLDGCLH PRWSLDFVRH
210 220 230 240 250
GMPQLANFVS SQTSSLEMQA ALMSRQMDAS FNWEALRWLR DLWPHKLLVK
260 270 280 290 300
GLLSAEDADR CIAEGADGVI LSNHGGRQLD CAISPMEVLA QSVAKTGKPV
310 320 330 340 350
LIDSGFRRGS DIVKALALGA EAVLLGRATL YGLAARGETG VDEVLTLLKA
360 370 380 390
DIDRTLAQIG CPDITSLSPD YLQNEGVTNT APVDHLIGKG THA
Length:393
Mass (Da):43,437
Last modified:February 1, 1991 - v1
Checksum:i18BE23E459BB3987
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY143338 Genomic DNA. Translation: AAC15503.1.
PIRiB44767.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY143338 Genomic DNA. Translation: AAC15503.1.
PIRiB44767.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HUVX-ray2.15A1-176[»]
A216-393[»]
1P4CX-ray1.35A1-176[»]
A216-393[»]
1P5BX-ray1.35A1-176[»]
A216-393[»]
2A7NX-ray1.80A1-176[»]
A216-393[»]
2A7PX-ray2.20A1-176[»]
A216-393[»]
2A85X-ray2.50A1-176[»]
A216-393[»]
3GIYX-ray1.60A1-176[»]
A216-393[»]
ProteinModelPortaliP20932.
SMRiP20932.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00873; UER00853.
BioCyciMetaCyc:MONOMER-2422.
BRENDAi1.1.99.31. 5092.
SABIO-RKP20932.

Miscellaneous databases

EvolutionaryTraceiP20932.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
PfamiPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMDLB_PSEPU
AccessioniPrimary (citable) accession number: P20932
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 2, 2016
This is version 101 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, Direct protein sequencing

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.