Reviewed, UniProtKB/Swiss-Prot P20932 (MDLB_PSEPU)

Names and origin

Protein names

Recommended name:
    (S)-mandelate dehydrogenase
    EC=1.1.99.31
Alternative name(s):
    L(+)-mandelate dehydrogenase
      Short name=MDH

Gene names

Name:

mdlB

Organism

Pseudomonas putida

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Reduction of (S)-mandelate to benzoylformate.
Catalytic activity	(S)-2-hydroxy-2-phenylacetate + acceptor = 2-oxo-2-phenylacetate + reduced acceptor.
Cofactor	FMN.
Pathway	Aromatic compound metabolism; mandelic acid degradation; benzoic acid from (R)-mandelic acid: step 2/4.
Subunit structure	Homotetramer. Ref.2 Ref.3
Subcellular location	Membrane.
Sequence similarities	Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family. Contains 1 FMN hydroxy acid dehydrogenase domain.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism Mandelate pathway
Cellular component	Membrane
Ligand	FMN Flavoprotein
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW mandelate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	(S)-mandelate dehydrogenase activity Inferred from electronic annotation. Source: EC FMN binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 393

393

(S)-mandelate dehydrogenase

PRO_0000206327

Regions

Domain

1 – 377

377

FMN hydroxy acid dehydrogenase

Nucleotide binding

303 – 327

25

FMN

Sites

Active site

274

1

Proton acceptor By similarity

Binding site

26

1

Substrate Potential

Binding site

108

1

FMN

Binding site

129

1

FMN

Binding site

131

1

Substrate By similarity

Binding site

156

1

FMN

Binding site

165

1

Substrate By similarity

Binding site

250

1

FMN

Binding site

277

1

Substrate Potential

Secondary structure

1

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393

Helix Strand Turn

Details...

Helix

8 – 18

11

Helix

21 – 28

8

Helix

35 – 42

8

Helix

43 – 46

4

Beta strand

47 – 49

3

Beta strand

64 – 66

3

Beta strand

69 – 77

9

Helix

83 – 85

3

Helix

90 – 101

12

Beta strand

105 – 107

3

Helix

115 – 121

7

Beta strand

126 – 130

5

Helix

135 – 147

13

Beta strand

152 – 156

5

Helix

166 – 171

6

Helix

182 – 195

14

Turn

206 – 218

13

Helix

219 – 222

4

Helix

233 – 242

10

Beta strand

245 – 252

8

Helix

255 – 263

9

Beta strand

267 – 271

5

Helix

274 – 276

3

Helix

285 – 287

3

Helix

289 – 296

8

Beta strand

300 – 302

3

Helix

309 – 317

9

Beta strand

323 – 326

4

Helix

327 – 359

33

Helix

364 – 366

3

Helix

369 – 371

3

Beta strand

372 – 374

3

Sequences

	Sequence		Length	Mass (Da)
	P20932-1 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 18BE23E459BB3987	FASTA	393	43,437
	10 20 30 40 50 60 MSQNLFNVED YRKLRQKRLP KMVYDYLEGG AEDEYGVKHN RDVFQQWRFK PKRLVDVSRR 70 80 90 100 110 120 SLQAEVLGKR QSMPLLIGPT GLNGALWPKG DLALARAATK AGIPFVLSTA SNMSIEDLAR 130 140 150 160 170 180 QCDGDLWFQL YVIHREIAQG MVLKALHTGY TTLVLTTDVA VNGYRERDLH NRFKIPMSYS 190 200 210 220 230 240 AKVVLDGCLH PRWSLDFVRH GMPQLANFVS SQTSSLEMQA ALMSRQMDAS FNWEALRWLR 250 260 270 280 290 300 DLWPHKLLVK GLLSAEDADR CIAEGADGVI LSNHGGRQLD CAISPMEVLA QSVAKTGKPV 310 320 330 340 350 360 LIDSGFRRGS DIVKALALGA EAVLLGRATL YGLAARGETG VDEVLTLLKA DIDRTLAQIG 370 380 390 CPDITSLSPD YLQNEGVTNT APVDHLIGKG THA

References

[1]	"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: 2271624] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-30. Strain: ATCC 12633 / DSM 291 / NCIB 9494 / NCTC 10936 / Stanier 90.
[2]	"Structure of an active soluble mutant of the membrane-associated (S)-mandelate dehydrogenase." Sukumar N., Xu Y., Gatti D.L., Mitra B., Mathews F.S. Biochemistry 40:9870-9878(2001) [PubMed: 11502180] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH FMN, SUBUNIT.
[3]	"High resolution structures of an oxidized and reduced flavoprotein. The water switch in a soluble form of (S)-mandelate dehydrogenase." Sukumar N., Dewanti A.R., Mitra B., Mathews F.S. J. Biol. Chem. 279:3749-3757(2004) [PubMed: 14604988] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH FMN, SUBUNIT.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AY143338 Genomic DNA. Translation: AAC15503.1.

PIR

B44767.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HUV	X-ray	2.15	A	1-393	[»]
1P4C	X-ray	1.35	A	1-393	[»]
1P5B	X-ray	1.35	A	1-393	[»]
2A7N	X-ray	1.80	A	1-393	[»]
2A7P	X-ray	2.20	A	1-393	[»]
2A85	X-ray	2.50	A	1-393	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MON-2422.

BRENDA

1.1.99.31. 403.

Family and domain databases

InterPro

IPR012133. a-Hydoxy_acid_DH_FMN.
IPR013785. Aldolase_TIM.
IPR000262. FMN-dep_DH.
IPR017934. FMN-dep_OHA_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

Pfam

PF01070. FMN_dh. 1 hit.
[Graphical view]

PIRSF

PIRSF000138. Al-hdrx_acd_dh. 1 hit.

PROSITE

PS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MDLB_PSEPU

Accession

Primary (citable) accession number: P20932

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)