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P51016

- HOA_PSEUF

UniProt

P51016 - HOA_PSEUF

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Protein

4-hydroxy-2-oxovalerate aldolase

Gene

dmpG

Organism
Pseudomonas sp. (strain CF600)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 PublicationUniRule annotation

Catalytic activityi

(S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate.1 PublicationUniRule annotation

Enzyme regulationi

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.1 Publication

pH dependencei

Optimum pH is 8.5-9.0.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei17 – 171Transition state stabilizerUniRule annotation
Metal bindingi18 – 181Manganese1 PublicationUniRule annotation
Active sitei21 – 211Proton acceptorUniRule annotation
Binding sitei171 – 1711Substrate
Metal bindingi200 – 2001Manganese; via tele nitrogen1 PublicationUniRule annotation
Binding sitei200 – 2001Substrate
Metal bindingi202 – 2021Manganese; via tele nitrogen1 PublicationUniRule annotation
Binding sitei291 – 2911Substrate

GO - Molecular functioni

  1. 4-hydroxy-2-oxovalerate aldolase activity Source: UniProtKB
  2. manganese ion binding Source: UniProtKB

GO - Biological processi

  1. aromatic compound catabolic process Source: UniProtKB
  2. benzoate catabolic process via hydroxylation Source: UniProtKB-UniPathway
  3. phenol-containing compound catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12778.
UniPathwayiUPA00156.
UPA00728.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxy-2-oxovalerate aldolaseUniRule annotation (EC:4.1.3.39UniRule annotation)
Short name:
HOAUniRule annotation
Alternative name(s):
4-hydroxy-2-keto-pentanoic acid aldolaseUniRule annotation
4-hydroxy-2-oxopentanoate aldolaseUniRule annotation
Gene namesi
Name:dmpG
Encoded oniPlasmid pVI1500 Publication
OrganismiPseudomonas sp. (strain CF600)
Taxonomic identifieri79676 [NCBI]
Taxonomic lineageiBacteriaProteobacteria

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 3453444-hydroxy-2-oxovalerate aldolasePRO_0000079938Add
BLAST

Interactioni

Subunit structurei

Heterotetramer composed of two DmpG (aldolase) and two DmpF (dehydrogenase) subunits, which allows a direct channeling of acetaldehyde between the two active sites.2 Publications

Protein-protein interaction databases

IntActiP51016. 1 interaction.

Structurei

Secondary structure

1
345
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 134Combined sources
Turni15 – 173Combined sources
Helixi18 – 225Combined sources
Turni23 – 253Combined sources
Helixi29 – 4214Combined sources
Beta strandi45 – 484Combined sources
Turni60 – 623Combined sources
Helixi69 – 779Combined sources
Beta strandi81 – 899Combined sources
Helixi96 – 10510Combined sources
Beta strandi109 – 1157Combined sources
Helixi119 – 1224Combined sources
Helixi123 – 13210Combined sources
Beta strandi135 – 1428Combined sources
Helixi148 – 16114Combined sources
Beta strandi164 – 1696Combined sources
Helixi177 – 19014Combined sources
Beta strandi195 – 2006Combined sources
Helixi208 – 21710Combined sources
Beta strandi222 – 2265Combined sources
Helixi227 – 2293Combined sources
Helixi239 – 24911Combined sources
Helixi257 – 26610Combined sources
Helixi269 – 2713Combined sources
Helixi280 – 2889Combined sources
Helixi294 – 30512Combined sources
Helixi309 – 31911Combined sources
Helixi327 – 34014Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NVMX-ray1.70A/C/E/G1-345[»]
ProteinModelPortaliP51016.
SMRiP51016. Positions 2-341.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51016.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni17 – 182Substrate binding

Sequence similaritiesi

Belongs to the 4-hydroxy-2-oxovalerate aldolase family.UniRule annotation

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01656. HOA.
InterProiIPR017629. 4OH_2_O-val_aldolase.
IPR013785. Aldolase_TIM.
IPR012425. DmpG_comm.
IPR000891. PYR_CT.
[Graphical view]
PANTHERiPTHR10277:SF3. PTHR10277:SF3. 1 hit.
PfamiPF07836. DmpG_comm. 1 hit.
PF00682. HMGL-like. 1 hit.
[Graphical view]
ProDomiPD005364. DmpG_comm. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsiTIGR03217. 4OH_2_O_val_ald. 1 hit.
PROSITEiPS50991. PYR_CT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P51016 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTFNPSKKLY ISDVTLRDGS HAIRHQYTLD DVRAIARALD KAKVDSIEVA
60 70 80 90 100
HGDGLQGSSF NYGFGRHTDL EYIEAVAGEI SHAQIATLLL PGIGSVHDLK
110 120 130 140 150
NAYQAGARVV RVATHCTEAD VSKQHIEYAR NLGMDTVGFL MMSHMIPAEK
160 170 180 190 200
LAEQGKLMES YGATCIYMAD SGGAMSMNDI RDRMRAFKAV LKPETQVGMH
210 220 230 240 250
AHHNLSLGVA NSIVAVEEGC DRVDASLAGM GAGAGNAPLE VFIAVAERLG
260 270 280 290 300
WNHGTDLYTL MDAADDIVRP LQDRPVRVDR ETLGLGYAGV YSSFLRHAEI
310 320 330 340
AAAKYNLKTL DILVELGHRR MVGGQEDMIV DVALDLLAAH KENRA
Length:345
Mass (Da):37,471
Last modified:October 1, 1996 - v1
Checksum:i8B38B37A8A0EFEE0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X60835 Genomic DNA. Translation: CAA43227.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X60835 Genomic DNA. Translation: CAA43227.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NVM X-ray 1.70 A/C/E/G 1-345 [» ]
ProteinModelPortali P51016.
SMRi P51016. Positions 2-341.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P51016. 1 interaction.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00156 .
UPA00728 .
BioCyci MetaCyc:MONOMER-12778.

Miscellaneous databases

EvolutionaryTracei P51016.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01656. HOA.
InterProi IPR017629. 4OH_2_O-val_aldolase.
IPR013785. Aldolase_TIM.
IPR012425. DmpG_comm.
IPR000891. PYR_CT.
[Graphical view ]
PANTHERi PTHR10277:SF3. PTHR10277:SF3. 1 hit.
Pfami PF07836. DmpG_comm. 1 hit.
PF00682. HMGL-like. 1 hit.
[Graphical view ]
ProDomi PD005364. DmpG_comm. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
TIGRFAMsi TIGR03217. 4OH_2_O_val_ald. 1 hit.
PROSITEi PS50991. PYR_CT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiHOA_PSEUF
AccessioniPrimary (citable) accession number: P51016
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 66 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, Plasmid

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

External Data

Dasty 3