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Protein

Aklavinone 12-hydroxylase DnrF

Gene

dnrF

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

Functioni

Involved in the biosynthesis of the anthracyclines carminomycin, rhodomycin and daunorubicin (daunomycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the incorporation of a hydroxyl group at position C-11 of aklavinone, resulting in epsilon-rhodomycinone. It cannot accept substrates glycosylated at position C-7. It can also hydroxylate 11-deoxycarminomycinone and can use both NAD or NADP.1 Publication

Catalytic activityi

Aklavinone + NADPH + O2 = epsilon-rhodomycinone + NADP+ + H2O.1 Publication

Cofactori

FADBy similarity

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei37FADBy similarity1
Binding sitei121FADBy similarity1
Binding sitei145FAD; via amide nitrogenBy similarity1
Active sitei224Proton acceptorBy similarity1
Binding sitei308FADBy similarity1
Binding sitei317Aklavinone; via amide nitrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi17 – 18FADBy similarity2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

FAD, Flavoprotein, NAD, NADP, Nucleotide-binding

Enzyme and pathway databases

BRENDAi1.14.13.180. 6073.
UniPathwayiUPA00054.
UPA01040.
UPA01042.

Names & Taxonomyi

Protein namesi
Recommended name:
Aklavinone 12-hydroxylase DnrF (EC:1.14.13.180)
Alternative name(s):
Aklavinone 11-hydroxylase
Gene namesi
Name:dnrF
OrganismiStreptomyces peucetius
Taxonomic identifieri1950 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004256761 – 489Aklavinone 12-hydroxylase DnrFAdd BLAST489

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP32009.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PheA/TfdB FAD monooxygenase family.Curated

Phylogenomic databases

KOiK15950.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR002938. FAD-bd.
IPR023753. FAD/NAD-binding_dom.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

P32009-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALTKPDVDV LVVGGGLGGL STALFLARRG ARVLLVERHA STSVLPKAAG
60 70 80 90 100
QNPRTMELFR FGGVADEILA TDDIRGAQGD FTIKVVERVG GRVLHSFAES
110 120 130 140 150
FEELVGATEQ CTPMPWALAP QDRVEPVLVA HAAKHGAEIR FATELTSFQA
160 170 180 190 200
GDDGVTARLR DLGTGAESTV SARYLVAADG PRSAIRESLG ITRHGHGTLA
210 220 230 240 250
HFMGVIFEAD LTAVVPPGST GWYYLQHPDF TGTFGPTDRP NRHTFYVATT
260 270 280 290 300
PERGERPEDY TPQRCTELIR LAVDAPGLVP DILDIQAWDM AAYIADRWRE
310 320 330 340 350
GPVLLVGDAA KVTPPTGGMG GNTAIGDGFD VAWKLAAVLR GEAGERLLDS
360 370 380 390 400
YGAERSLVSR LVVDESLAIY AQRMAPHLLG SVPEERGTAQ VVLGFRYRST
410 420 430 440 450
AVAAEDDDPE PTEDPRRPSG RPGFRAPHVW IEQDGTRRST VELFGDCWVL
460 470 480
LAAPEGGAWP GRPPAPPRIW ASASTSISSA AMSPPPPAN
Length:489
Mass (Da):52,317
Last modified:March 19, 2014 - v2
Checksum:i5BBE25F0974B34EE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18082 Genomic DNA. Translation: AAC43342.1.
M73758 Genomic DNA. Translation: AAA74716.1.
PIRiS27706.

Genome annotation databases

KEGGiag:AAC43342.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18082 Genomic DNA. Translation: AAC43342.1.
M73758 Genomic DNA. Translation: AAA74716.1.
PIRiS27706.

3D structure databases

ProteinModelPortaliP32009.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAC43342.

Phylogenomic databases

KOiK15950.

Enzyme and pathway databases

UniPathwayiUPA00054.
UPA01040.
UPA01042.
BRENDAi1.14.13.180. 6073.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR002938. FAD-bd.
IPR023753. FAD/NAD-binding_dom.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiDNRF_STRPE
AccessioniPrimary (citable) accession number: P32009
Secondary accession number(s): P72497
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: March 19, 2014
Last modified: September 7, 2016
This is version 52 of the entry and version 2 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.