Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P51016 (HOA_PSEUF) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 onPlasmid pVI150
OrganismPseudomonas sp. (strain CF600)
Taxonomic identifier79676 [NCBI]
Taxonomic lineageBacteriaProteobacteria

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

(S)-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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 3453444-hydroxy-2-oxovalerate aldolase HAMAP-Rule MF_01656
PRO_0000079938

Regions

Region17 – 182Substrate binding HAMAP-Rule MF_01656

Sites

Active site211Proton acceptor Potential
Metal binding181Manganese
Metal binding2001Manganese; via tele nitrogen
Metal binding2021Manganese; via tele nitrogen
Binding site1711Substrate
Binding site2001Substrate
Binding site2911Substrate
Site171Transition state stabilizer By similarity

Secondary structure

..................................................... 345
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P51016 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 8B38B37A8A0EFEE0

FASTA34537,471
        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 

« Hide

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1NVMX-ray1.70A/C/E/G1-345[»]
ProteinModelPortalP51016.
SMRP51016. Positions 2-341.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP51016. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12778.
UniPathwayUPA00156.
UPA00728.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01656. HOA.
InterProIPR017629. 4OH_2_O-val_aldolase.
IPR013785. Aldolase_TIM.
IPR012425. DmpG_comm.
IPR000891. PYR_CT.
[Graphical view]
PANTHERPTHR10277:SF3. PTHR10277:SF3. 1 hit.
PfamPF07836. DmpG_comm. 1 hit.
PF00682. HMGL-like. 1 hit.
[Graphical view]
ProDomPD005364. DmpG_comm. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR03217. 4OH_2_O_val_ald. 1 hit.
PROSITEPS50991. PYR_CT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP51016.

Entry information

Entry nameHOA_PSEUF
AccessionPrimary (citable) accession number: P51016
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways