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Protein

Carminomycin 4-O-methyltransferase DnrK

Gene

dnrK

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

Functioni

Involved in the biosynthesis of the anthracyclines carminomycin and daunorubicin (daunomycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. In vivo, catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to the 4-O-position of carminomycin to form daunorubicin. In vitro, it also methylates the anthracyclines rhodomycin D (10-carbomethoxy-13-deoxycarminomycin) and 13-deoxy-carminomycin at the 4-hydroxyl position. It is quite specific with respect to the length of the carbohydrate chain at the C7 position, but it can accept substrates with bulky substituent at C10 position.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + carminomycin = S-adenosyl-L-homocysteine + daunorubicin.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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei153S-adenosyl-L-methionine1
Binding sitei163Substrate1
Binding sitei187S-adenosyl-L-methionine; via carbonyl oxygen1
Binding sitei210S-adenosyl-L-methionine1
Binding sitei252S-adenosyl-L-methionine1
Binding sitei257Substrate1
Binding sitei303Substrate1

GO - Molecular functioni

  • methyltransferase activity Source: UniProtKB
  • O-methyltransferase activity Source: InterPro

GO - Biological processi

  • daunorubicin biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18173.
BRENDAi2.1.1.292. 6073.
UniPathwayiUPA00054.
UPA01040.

Names & Taxonomyi

Protein namesi
Recommended name:
Carminomycin 4-O-methyltransferase DnrK (EC:2.1.1.292)
Short name:
COMT
Alternative name(s):
Anthracycline 4-O-methyltransferase
Gene namesi
Name:dnrK
OrganismiStreptomyces peucetius
Taxonomic identifieri1950 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000898812 – 356Carminomycin 4-O-methyltransferase DnrKAdd BLAST355

Interactioni

Subunit structurei

Homodimer and homotetramer in equilibrium.1 Publication

Structurei

Secondary structure

1356
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 24Combined sources11
Helixi27 – 37Combined sources11
Helixi40 – 45Combined sources6
Helixi51 – 58Combined sources8
Helixi62 – 74Combined sources13
Beta strandi77 – 82Combined sources6
Beta strandi85 – 88Combined sources4
Helixi92 – 95Combined sources4
Helixi103 – 106Combined sources4
Helixi112 – 116Combined sources5
Helixi117 – 122Combined sources6
Helixi123 – 129Combined sources7
Helixi134 – 138Combined sources5
Helixi142 – 148Combined sources7
Helixi150 – 160Combined sources11
Turni161 – 163Combined sources3
Helixi164 – 167Combined sources4
Helixi169 – 173Combined sources5
Beta strandi181 – 186Combined sources6
Helixi192 – 200Combined sources9
Beta strandi205 – 210Combined sources6
Helixi214 – 224Combined sources11
Turni228 – 230Combined sources3
Beta strandi231 – 235Combined sources5
Beta strandi246 – 253Combined sources8
Helixi255 – 257Combined sources3
Helixi260 – 272Combined sources13
Beta strandi274 – 284Combined sources11
Helixi289 – 291Combined sources3
Helixi295 – 308Combined sources14
Helixi315 – 324Combined sources10
Beta strandi327 – 334Combined sources8
Beta strandi338 – 340Combined sources3
Beta strandi345 – 351Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TW2X-ray2.50A/B2-356[»]
1TW3X-ray2.35A/B2-356[»]
4WXHX-ray1.90A/B2-356[»]
5EEGX-ray2.25A/B1-356[»]
5EEHX-ray1.82A/B/C1-356[»]
5JR3X-ray1.84A/B/C10-353[»]
ProteinModelPortaliQ06528.
SMRiQ06528.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06528.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni237 – 238S-adenosyl-L-methionine binding2

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family.PROSITE-ProRule annotation

Phylogenomic databases

KOiK15954.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR016461. O-MeTrfase_COMT.
IPR001077. O_MeTrfase_2.
IPR029063. SAM-dependent_MTases.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00891. Methyltransf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005739. O-mtase. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51683. SAM_OMT_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q06528-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAEPTVAAR PQQIDALRTL IRLGSLHTPM VVRTAATLRL VDHILAGART
60 70 80 90 100
VKALAARTDT RPEALLRLIR HLVAIGLLEE DAPGEFVPTE VGELLADDHP
110 120 130 140 150
AAQRAWHDLT QAVARADISF TRLPDAIRTG RPTYESIYGK PFYEDLAGRP
160 170 180 190 200
DLRASFDSLL ACDQDVAFDA PAAAYDWTNV RHVLDVGGGK GGFAAAIARR
210 220 230 240 250
APHVSATVLE MAGTVDTARS YLKDEGLSDR VDVVEGDFFE PLPRKADAII
260 270 280 290 300
LSFVLLNWPD HDAVRILTRC AEALEPGGRI LIHERDDLHE NSFNEQFTEL
310 320 330 340 350
DLRMLVFLGG ALRTREKWDG LAASAGLVVE EVRQLPSPTI PYDLSLLVLA

PAATGA
Length:356
Mass (Da):38,782
Last modified:January 23, 2007 - v2
Checksum:i2969EC5C6117ECF7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13453 Genomic DNA. Translation: AAA26712.1.
L40425 Genomic DNA. Translation: AAA99001.1.
PIRiA47128.

Genome annotation databases

KEGGiag:AAA26712.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13453 Genomic DNA. Translation: AAA26712.1.
L40425 Genomic DNA. Translation: AAA99001.1.
PIRiA47128.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TW2X-ray2.50A/B2-356[»]
1TW3X-ray2.35A/B2-356[»]
4WXHX-ray1.90A/B2-356[»]
5EEGX-ray2.25A/B1-356[»]
5EEHX-ray1.82A/B/C1-356[»]
5JR3X-ray1.84A/B/C10-353[»]
ProteinModelPortaliQ06528.
SMRiQ06528.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA26712.

Phylogenomic databases

KOiK15954.

Enzyme and pathway databases

UniPathwayiUPA00054.
UPA01040.
BioCyciMetaCyc:MONOMER-18173.
BRENDAi2.1.1.292. 6073.

Miscellaneous databases

EvolutionaryTraceiQ06528.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR016461. O-MeTrfase_COMT.
IPR001077. O_MeTrfase_2.
IPR029063. SAM-dependent_MTases.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00891. Methyltransf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005739. O-mtase. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51683. SAM_OMT_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDNRK_STRPE
AccessioniPrimary (citable) accession number: Q06528
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 87 of the entry and version 2 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
  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.