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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei26 – 261SubstratePROSITE-ProRule annotation
Binding sitei108 – 1081FMNPROSITE-ProRule annotation2 Publications
Binding sitei129 – 1291FMNPROSITE-ProRule annotation2 Publications
Binding sitei131 – 1311SubstratePROSITE-ProRule annotation
Binding sitei156 – 1561FMNPROSITE-ProRule annotation2 Publications
Binding sitei165 – 1651SubstratePROSITE-ProRule annotation
Binding sitei250 – 2501FMNPROSITE-ProRule annotation2 Publications
Active sitei274 – 2741Proton acceptorPROSITE-ProRule annotation
Binding sitei277 – 2771SubstratePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi303 – 32725FMNPROSITE-ProRule annotation2 PublicationsAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 393393(S)-mandelate dehydrogenasePRO_0000206327Add
BLAST

Interactioni

Subunit structurei

Homotetramer.2 Publications

Structurei

Secondary structure

1
393
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 1811Combined sources
Helixi21 – 288Combined sources
Helixi35 – 428Combined sources
Helixi43 – 464Combined sources
Beta strandi47 – 493Combined sources
Beta strandi64 – 663Combined sources
Beta strandi69 – 779Combined sources
Helixi83 – 853Combined sources
Helixi90 – 10112Combined sources
Beta strandi105 – 1073Combined sources
Helixi115 – 1217Combined sources
Beta strandi126 – 1305Combined sources
Helixi135 – 14713Combined sources
Beta strandi152 – 1565Combined sources
Helixi166 – 1716Combined sources
Turni216 – 2183Combined sources
Helixi219 – 2224Combined sources
Helixi233 – 24210Combined sources
Beta strandi245 – 2528Combined sources
Helixi255 – 2639Combined sources
Beta strandi267 – 2715Combined sources
Helixi274 – 2763Combined sources
Helixi285 – 2873Combined sources
Helixi289 – 2968Combined sources
Beta strandi300 – 3023Combined sources
Helixi309 – 3179Combined sources
Beta strandi323 – 3264Combined sources
Helixi327 – 35933Combined sources
Helixi364 – 3663Combined sources
Helixi369 – 3713Combined sources
Beta strandi372 – 3743Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 4-375.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20932.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 377377FMN hydroxy acid dehydrogenasePROSITE-ProRule annotationAdd
BLAST

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
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. Positions 4-375.
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: October 14, 2015
This is version 99 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.