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Protein
Submitted name:

Diketoreductase

Gene

dkr

Organism
Acinetobacter baylyi
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei34 – 341NADCombined sources
Binding sitei100 – 1001NADCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 154NADCombined sources
Nucleotide bindingi94 – 952NADCombined sources
Nucleotide bindingi120 – 1223NADCombined sources

GO - Molecular functioni

  1. 3-hydroxyacyl-CoA dehydrogenase activity Source: InterPro
  2. NAD+ binding Source: InterPro

GO - Biological processi

  1. fatty acid metabolic process Source: InterPro
Complete GO annotation...

Keywords - Ligandi

NADCombined sources, Nucleotide-bindingCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
DiketoreductaseImported
Gene namesi
Name:dkrImported
OrganismiAcinetobacter baylyiImported
Taxonomic identifieri202950 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DYDX-ray1.95A1-283[»]
4E12X-ray1.93A1-283[»]
4E13X-ray2.08A1-283[»]
ProteinModelPortaliB1P3E1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR022694. 3-OHacyl-CoA_DH.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. DH_multihelical.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000105. HCDH. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.

Sequencei

Sequence statusi: Complete.

B1P3E1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTGITNVTVL GTGVLGSQIA FQTAFHGFAV TAYDINTDAL DAAKKRFEGL
60 70 80 90 100
AAVYEKEVAG AADGAAQKAL GGIRYSDDLA QAVKDADLVI EAVPESLDLK
110 120 130 140 150
RDIYTKLGEL APAKTIFATN SSTLLPSDLV GYTGRGDKFL ALHFANHVWV
160 170 180 190 200
NNTAEVMGTT KTDPEVYQQV VEFASAIGMV PIELKKEKAG YVLNSLLVPL
210 220 230 240 250
LDAAAELLVD GIADPETIDK TWRIGTGAPK GPFEIFDIVG LTTAYNISSV
260 270 280
SGPKQREFAA YLKENYIDKG KLGLATGEGF YRY
Length:283
Mass (Da):30,237
Last modified:April 29, 2008 - v1
Checksum:i275E6E9E18FDD09A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU273886 Genomic DNA. Translation: ABY48099.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU273886 Genomic DNA. Translation: ABY48099.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DYDX-ray1.95A1-283[»]
4E12X-ray1.93A1-283[»]
4E13X-ray2.08A1-283[»]
ProteinModelPortaliB1P3E1.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR022694. 3-OHacyl-CoA_DH.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. DH_multihelical.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 1 hit.
PF02737. 3HCDH_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000105. HCDH. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning, expression, and characterization of a novel diketoreductase from Acinetobacter baylyi."
    Wu X., Liu N., He Y., Chen Y.
    Acta Biochim. Biophys. Sin. 41:163-170(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC 33305Imported.
  2. "Dual catalysis mode for the dicarbonyl reduction catalyzed by diketoreductase."
    Lu M., Huang Y., White M.A., Wu X., Liu N., Cheng X., Chen Y.
    Chem. Commun. (Camb.) 48:11352-11354(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH NAD.

Entry informationi

Entry nameiB1P3E1_ACIBI
AccessioniPrimary (citable) accession number: B1P3E1
Entry historyi
Integrated into UniProtKB/TrEMBL: April 29, 2008
Last sequence update: April 29, 2008
Last modified: January 7, 2015
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.