P51016 (HOA_PSEUF) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
4-hydroxy-2-oxovalerate aldolase
Short name=HOA
EC=4.1.3.39

Alternative name(s):
4-hydroxy-2-keto-pentanoic acid aldolase
4-hydroxy-2-oxopentanoate aldolase

Gene names

Name:

dmpG

Encoded on

Plasmid pVI150

Organism

Pseudomonas sp. (strain CF600)

Taxonomic identifier

79676 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › unclassified Proteobacteria › unclassified pseudomonads

Protein attributes

Sequence length	345 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of aromatic compounds such as phenols, cresols and catechols. Ref.1
Catalytic activity	4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate. Ref.2
Enzyme regulation	Six- to eight-fold activated by Mn2+. Retains residual activity after EDTA treatment in vitro. Also activated by NADH and, to a lesser extent, by NAD+. Strongly inhibited by Zn2+. Mg2+ and Ca2+ have no effect on enzymatic activity. Ref.2
Pathway	Aromatic compound metabolism; benzoate degradation via hydroxylation. HAMAP-Rule MF_01656 Aromatic compound metabolism; phenol degradation. HAMAP-Rule MF_01656
Subunit structure	Heterotetramer composed of two DmpG (aldolase) and two DmpF (dehydrogenase) subunits, which allows a direct channeling of acetaldehyde between the two active sites. Ref.2 Ref.3
Sequence similarities	Belongs to the 4-hydroxy-2-oxovalerate aldolase family.
Biophysicochemical properties	pH dependence: Optimum pH is 8.5-9.0. HAMAP-Rule MF_01656

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	Manganese Metal-binding
Molecular function	Lyase
Technical term	3D-structure Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological_process	aromatic compound catabolic process Inferred from direct assay Ref.2. Source: UniProtKB benzoate catabolic process via hydroxylation Inferred from electronic annotation. Source: UniProtKB-UniPathway phenol-containing compound catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	4-hydroxy-2-oxovalerate aldolase activity Inferred from direct assay Ref.2. Source: UniProtKB manganese ion binding Inferred from direct assay Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 345

344

4-hydroxy-2-oxovalerate aldolase HAMAP-Rule MF_01656

PRO_0000079938

Regions

Region

17 – 18

2

Substrate binding HAMAP-Rule MF_01656

Sites

Active site

21

1

Proton acceptor Potential

Metal binding

18

1

Manganese

Metal binding

200

1

Manganese; via tele nitrogen

Metal binding

202

1

Manganese; via tele nitrogen

Binding site

171

1

Substrate

Binding site

200

1

Substrate

Binding site

291

1

Substrate

Site

17

1

Transition state stabilizer By similarity

Secondary structure

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345

Helix Strand Turn

Details...

Beta strand

10 – 13

4

Turn

15 – 17

3

Helix

18 – 22

5

Turn

23 – 25

3

Helix

29 – 42

14

Beta strand

45 – 48

4

Turn

60 – 62

3

Helix

69 – 77

9

Beta strand

81 – 89

9

Helix

96 – 105

10

Beta strand

109 – 115

7

Helix

119 – 122

4

Helix

123 – 132

10

Beta strand

135 – 142

8

Helix

148 – 161

14

Beta strand

164 – 169

6

Helix

177 – 190

14

Beta strand

195 – 200

6

Helix

208 – 217

10

Beta strand

222 – 226

5

Helix

227 – 229

3

Helix

239 – 249

11

Helix

257 – 266

10

Helix

269 – 271

3

Helix

280 – 288

9

Helix

294 – 305

12

Helix

309 – 319

11

Helix

327 – 340

14

Sequences

	Sequence		Length	Mass (Da)
	P51016 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 8B38B37A8A0EFEE0	FASTA	345	37,471
	10 20 30 40 50 60 MTFNPSKKLY ISDVTLRDGS HAIRHQYTLD DVRAIARALD KAKVDSIEVA HGDGLQGSSF 70 80 90 100 110 120 NYGFGRHTDL EYIEAVAGEI SHAQIATLLL PGIGSVHDLK NAYQAGARVV RVATHCTEAD 130 140 150 160 170 180 VSKQHIEYAR NLGMDTVGFL MMSHMIPAEK LAEQGKLMES YGATCIYMAD SGGAMSMNDI 190 200 210 220 230 240 RDRMRAFKAV LKPETQVGMH AHHNLSLGVA NSIVAVEEGC DRVDASLAGM GAGAGNAPLE 250 260 270 280 290 300 VFIAVAERLG WNHGTDLYTL MDAADDIVRP LQDRPVRVDR ETLGLGYAGV YSSFLRHAEI 310 320 330 340 AAAKYNLKTL DILVELGHRR MVGGQEDMIV DVALDLLAAH KENRA

References

[1]	"Nucleotide sequence and functional analysis of the complete phenol/3,4-dimethylphenol catabolic pathway of Pseudomonas sp. strain CF600." Shingler V., Marklund U., Powlowski J. J. Bacteriol. 174:711-724(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: CF600.
[2]	"Purification and properties of the physically associated meta-cleavage pathway enzymes 4-hydroxy-2-ketovalerate aldolase and aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain CF600." Powlowski J., Sahlman L., Shingler V. J. Bacteriol. 175:377-385(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-7, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, SUBUNIT, INTERACTION WITH DMPF, PH DEPENDENCE. Strain: CF600.
[3]	"Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate." Manjasetty B.A., Powlowski J., Vrielink A. Proc. Natl. Acad. Sci. U.S.A. 100:6992-6997(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH DMPF; NAD; MANGANESE AND OXALATE, SUBUNIT, REACTION MECHANISM. Strain: CF600.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X60835 Genomic DNA. Translation: CAA43227.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NVM	X-ray	1.70	A/C/E/G	1-345	[»]

ProteinModelPortal

P51016.

SMR

P51016. Positions 2-341.

ModBase

Search...

Protein-protein interaction databases

IntAct

P51016. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-12778.

UniPathway

UPA00156.
UPA00728.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

HAMAP

MF_01656. HOA.

InterPro

IPR017629. 4OH_2_O-val_aldolase.
IPR013785. Aldolase_TIM.
IPR012425. DmpG_comm.
IPR000891. PYR_CT.
[Graphical view]

PANTHER

PTHR10277:SF3. PTHR10277:SF3. 1 hit.

Pfam

PF07836. DmpG_comm. 1 hit.
PF00682. HMGL-like. 1 hit.
[Graphical view]

ProDom

PD005364. DmpG_comm. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR03217. 4OH_2_O_val_ald. 1 hit.

PROSITE

PS50991. PYR_CT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P51016.

Entry information

Entry name

HOA_PSEUF

Accession

Primary (citable) accession number: P51016

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program