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Protein

Acetylacetone-cleaving enzyme

Gene

dke1

Organism
Acinetobacter johnsonii
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves acetylacetone to equimolar amounts of methylglyoxal and acetate, consuming one equivalent of molecular oxygen.1 Publication

Catalytic activityi

Pentane-2,4-dione + O2 = acetate + 2-oxopropanal.1 Publication

Cofactori

Fe cation1 PublicationNote: Binds 1 Fe cation per subunit.1 Publication

Pathwayi: acetylacetone degradation

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

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16107.
BRENDAi1.13.11.50. 103.
UniPathwayiUPA00734.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylacetone-cleaving enzyme (EC:1.13.11.501 Publication)
Alternative name(s):
Acetylacetone dioxygenase
Diketone cleaving dioxygenase
Diketone cleaving enzyme
Gene namesi
Name:dke1
OrganismiAcinetobacter johnsonii
Taxonomic identifieri40214 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000799251 – 153Acetylacetone-cleaving enzymeAdd BLAST153

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1153
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 15Combined sources4
Helixi18 – 20Combined sources3
Helixi26 – 28Combined sources3
Beta strandi29 – 31Combined sources3
Beta strandi34 – 41Combined sources8
Turni42 – 45Combined sources4
Beta strandi46 – 53Combined sources8
Beta strandi57 – 59Combined sources3
Beta strandi62 – 66Combined sources5
Beta strandi68 – 79Combined sources12
Helixi83 – 85Combined sources3
Beta strandi87 – 98Combined sources12
Beta strandi103 – 105Combined sources3
Beta strandi108 – 111Combined sources4
Beta strandi113 – 121Combined sources9
Beta strandi123 – 126Combined sources4
Beta strandi132 – 136Combined sources5
Helixi138 – 148Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BALX-ray1.95A/B/C/D1-153[»]
ProteinModelPortaliQ8GNT2.
SMRiQ8GNT2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8GNT2.

Family & Domainsi

Phylogenomic databases

KOiK20148.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8GNT2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDYCNKKHTA EEYVKISDNN YVPFPEAFSD GGITWQLLHS SPETSSWTAI
60 70 80 90 100
FNCPAGSSFA SHIHAGPGEY FLTKGKMEVR GGEQEGGSTA YAPSYGFESS
110 120 130 140 150
GALHGKTFFP VESQFYMTFL GPLNFIDDNG KVIASIGWAE AQGAWLATKN

EAA
Length:153
Mass (Da):16,607
Last modified:March 1, 2003 - v1
Checksum:iF3FBCB762E8F250F
GO

Mass spectrometryi

Molecular mass is 16607 Da from positions 1 - 153. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF489107 Genomic DNA. Translation: AAN45859.1.

Genome annotation databases

KEGGiag:AAN45859.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF489107 Genomic DNA. Translation: AAN45859.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BALX-ray1.95A/B/C/D1-153[»]
ProteinModelPortaliQ8GNT2.
SMRiQ8GNT2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAN45859.

Phylogenomic databases

KOiK20148.

Enzyme and pathway databases

UniPathwayiUPA00734.
BioCyciMetaCyc:MONOMER-16107.
BRENDAi1.13.11.50. 103.

Miscellaneous databases

EvolutionaryTraceiQ8GNT2.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDKE1_ACIJO
AccessioniPrimary (citable) accession number: Q8GNT2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: March 1, 2003
Last modified: November 2, 2016
This is version 55 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.