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Protein

4-hydroxy-2-oxovalerate aldolase

Gene

dmpG

Organism
Pseudomonas sp. (strain CF600)
Status
Reviewed-Annotation score: 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.UniRule annotation1 Publication

Catalytic activityi

(S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate.UniRule annotation1 Publication

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: benzoate degradation via hydroxylation

This protein is involved in the pathway benzoate degradation via hydroxylation, which is part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the pathway benzoate degradation via hydroxylation and in Aromatic compound metabolism.

Pathwayi: phenol degradation

This protein is involved in the pathway phenol degradation, which is part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the pathway phenol degradation and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei17Transition state stabilizerUniRule annotation1
Metal bindingi18ManganeseUniRule annotation1 Publication1
Active sitei21Proton acceptorUniRule annotation1
Binding sitei171Substrate1
Metal bindingi200Manganese; via tele nitrogenUniRule annotation1 Publication1
Binding sitei200Substrate1
Metal bindingi202Manganese; via tele nitrogenUniRule annotation1 Publication1
Binding sitei291Substrate1

GO - Molecular functioni

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

GO - Biological processi

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.
BRENDAi4.1.3.39. 5085.
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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000799382 – 3454-hydroxy-2-oxovalerate aldolaseAdd BLAST344

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 interactor.

Structurei

Secondary structure

1345
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 13Combined sources4
Turni15 – 17Combined sources3
Helixi18 – 22Combined sources5
Turni23 – 25Combined sources3
Helixi29 – 42Combined sources14
Beta strandi45 – 48Combined sources4
Turni60 – 62Combined sources3
Helixi69 – 77Combined sources9
Beta strandi81 – 89Combined sources9
Helixi96 – 105Combined sources10
Beta strandi109 – 115Combined sources7
Helixi119 – 122Combined sources4
Helixi123 – 132Combined sources10
Beta strandi135 – 142Combined sources8
Helixi148 – 161Combined sources14
Beta strandi164 – 169Combined sources6
Helixi177 – 190Combined sources14
Beta strandi195 – 200Combined sources6
Helixi208 – 217Combined sources10
Beta strandi222 – 226Combined sources5
Helixi227 – 229Combined sources3
Helixi239 – 249Combined sources11
Helixi257 – 266Combined sources10
Helixi269 – 271Combined sources3
Helixi280 – 288Combined sources9
Helixi294 – 305Combined sources12
Helixi309 – 319Combined sources11
Helixi327 – 340Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NVMX-ray1.70A/C/E/G1-345[»]
ProteinModelPortaliP51016.
SMRiP51016.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51016.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 261Pyruvate carboxyltransferasePROSITE-ProRule annotationAdd BLAST253

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni17 – 18Substrate binding2

Sequence similaritiesi

Belongs to the 4-hydroxy-2-oxovalerate aldolase family.UniRule annotation
Contains 1 pyruvate carboxyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

KOiK01666.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01656. HOA. 1 hit.
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.

P51016-1 [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:
EMBLi
GenBanki
DDBJi
Links Updated
X60835 Genomic DNA. Translation: CAA43227.1.

Genome annotation databases

KEGGiag:CAA43227.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60835 Genomic DNA. Translation: CAA43227.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NVMX-ray1.70A/C/E/G1-345[»]
ProteinModelPortaliP51016.
SMRiP51016.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP51016. 1 interactor.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA43227.

Phylogenomic databases

KOiK01666.

Enzyme and pathway databases

UniPathwayiUPA00156.
UPA00728.
BioCyciMetaCyc:MONOMER-12778.
BRENDAi4.1.3.39. 5085.

Miscellaneous databases

EvolutionaryTraceiP51016.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01656. HOA. 1 hit.
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]
ProtoNetiSearch...

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: November 2, 2016
This is version 77 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

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.