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Protein

Aklaviketone reductase DauE

Gene

dauE

Organism
Streptomyces sp. (strain C5)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of aklavinone which is an important precursor common to the formation of the clinically significant anthracyclines such as carminomycin, daunorubicin (daunomycin), rhodomycin, aclacinomycin T (aklavin) and aclacinomycin A (aclarubicin). These compounds are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the NADPH-specific conversion of aklaviketone to yield aklavinone. It can also convert maggiemycin and 7-oxodaunomycinone to epsilon-rhodomycinone and daunomycinone, respectively.4 Publications

Catalytic activityi

Aklavinone + NADP+ = aklaviketone + NADPH.1 Publication

Pathwayi: daunorubicin biosynthesis

This protein is involved in the pathway daunorubicin biosynthesis, which is part of Antibiotic biosynthesis.
View all proteins of this organism that are known to be involved in the pathway daunorubicin biosynthesis and in Antibiotic biosynthesis.

Pathwayi: carminomycin biosynthesis

This protein is involved in the pathway carminomycin biosynthesis, which is part of Antibiotic biosynthesis.
View all proteins of this organism that are known to be involved in the pathway carminomycin biosynthesis and in Antibiotic biosynthesis.

Pathwayi: rhodomycin biosynthesis

This protein is involved in the pathway rhodomycin biosynthesis, which is part of Antibiotic biosynthesis.
View all proteins of this organism that are known to be involved in the pathway rhodomycin biosynthesis and in Antibiotic biosynthesis.

Pathwayi: aclacinomycin biosynthesis

This protein is involved in the pathway aclacinomycin biosynthesis, which is part of Antibiotic biosynthesis.
View all proteins of this organism that are known to be involved in the pathway aclacinomycin biosynthesis and in Antibiotic biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei86 – 861NADP; via carbonyl oxygenBy similarity
Active sitei152 – 1521Proton acceptorBy similarity
Binding sitei185 – 1851NADP; via amide nitrogen and carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi58 – 592NADPBy similarity
Nucleotide bindingi152 – 1565NADPBy similarity

GO - Molecular functioni

GO - Biological processi

  • antibiotic biosynthetic process Source: UniProtKB
  • daunorubicin biosynthetic process Source: UniProtKB
  • doxorubicin metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18180.
BRENDAi1.1.1.362. 1284.
UniPathwayiUPA00054.
UPA01040.
UPA01042.
UPA01043.

Names & Taxonomyi

Protein namesi
Recommended name:
Aklaviketone reductase DauE (EC:1.1.1.362)
Gene namesi
Name:dauE
OrganismiStreptomyces sp. (strain C5)
Taxonomic identifieri45212 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene accumulate maggiemycin. In the absence of the aklavinone intermediate, aklaviketone is apparently hydroxylated at C-11 to form maggiemycin.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 251251Aklaviketone reductase DauEPRO_0000425674Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ53882.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK15944.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Q53882-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENTQRSVIV TGGGSGIGRA VARAFAARGD RVLVVGRTAG PLAETVDGHK
60 70 80 90 100
EAHTLAVDIT DPAAPQAVVR EVRERLGGVV DVLVNNAATA VFGHLGELDR
110 120 130 140 150
TAVEAQVATN LVAPVLLTQA LLDPLETASG LVVNIGSAGA LGRRAWPGNA
160 170 180 190 200
VYGAAKAGLD LLTRSWAVEL GPRGIRVIGV APGVIETGAG VRAGMSQEAY
210 220 230 240 250
DGFLEAMGQR VPLGRVGRPE DVAWWVVRLA DPEAAYASGA VLAVDGGLSV

T
Length:251
Mass (Da):25,632
Last modified:November 1, 1996 - v1
Checksum:i64E53501FECC2847
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43704 Genomic DNA. Translation: AAB08021.1.

Genome annotation databases

KEGGiag:AAB08021.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43704 Genomic DNA. Translation: AAB08021.1.

3D structure databases

ProteinModelPortaliQ53882.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAB08021.

Phylogenomic databases

KOiK15944.

Enzyme and pathway databases

UniPathwayiUPA00054.
UPA01040.
UPA01042.
UPA01043.
BioCyciMetaCyc:MONOMER-18180.
BRENDAi1.1.1.362. 1284.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDNRE_STRS5
AccessioniPrimary (citable) accession number: Q53882
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 19, 2014
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.