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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei153 – 1531S-adenosyl-L-methionine
Binding sitei163 – 1631Substrate
Binding sitei187 – 1871S-adenosyl-L-methionine; via carbonyl oxygen
Binding sitei210 – 2101S-adenosyl-L-methionine
Binding sitei252 – 2521S-adenosyl-L-methionine
Binding sitei257 – 2571Substrate
Binding sitei303 – 3031Substrate

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 356355Carminomycin 4-O-methyltransferase DnrKPRO_0000089881Add
BLAST

Interactioni

Subunit structurei

Homodimer and homotetramer in equilibrium.1 Publication

Structurei

Secondary structure

1
356
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 2411Combined sources
Helixi27 – 3711Combined sources
Helixi40 – 456Combined sources
Helixi51 – 588Combined sources
Helixi62 – 7413Combined sources
Beta strandi77 – 826Combined sources
Beta strandi85 – 884Combined sources
Helixi92 – 954Combined sources
Helixi103 – 1064Combined sources
Helixi112 – 1165Combined sources
Helixi117 – 1226Combined sources
Helixi123 – 1297Combined sources
Helixi134 – 1385Combined sources
Helixi142 – 1487Combined sources
Helixi150 – 16011Combined sources
Turni161 – 1633Combined sources
Helixi164 – 1674Combined sources
Helixi169 – 1735Combined sources
Beta strandi181 – 1866Combined sources
Helixi192 – 2009Combined sources
Beta strandi205 – 2106Combined sources
Helixi214 – 22411Combined sources
Turni228 – 2303Combined sources
Beta strandi231 – 2355Combined sources
Beta strandi246 – 2538Combined sources
Helixi255 – 2573Combined sources
Helixi260 – 27213Combined sources
Beta strandi274 – 28411Combined sources
Helixi289 – 2913Combined sources
Helixi295 – 30814Combined sources
Helixi315 – 32410Combined sources
Beta strandi327 – 3348Combined sources
Beta strandi338 – 3403Combined sources
Beta strandi345 – 3517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 4-353.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06528.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni237 – 2382S-adenosyl-L-methionine binding

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
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. Positions 4-353.
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: September 7, 2016
This is version 85 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.