Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

3,7-dimethylxanthine N-methyltransferase

Gene

DXMT1

Organism
Coffea canephora (Robusta coffee)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of caffeine. Catalyzes the conversion of 7-methylxanthine to theobromine and of theobromine to caffeine, but no sequential conversion of 7-methylxanthine to caffeine was detected.

Catalytic activityi

S-adenosyl-L-methionine + 3,7-dimethylxanthine = S-adenosyl-L-homocysteine + 1,3,7-trimethylxanthine.1 Publication
S-adenosyl-L-methionine + 1,7-dimethylxanthine = S-adenosyl-L-homocysteine + 1,3,7-trimethylxanthine.1 Publication
S-adenosyl-L-methionine + 7-methylxanthine = S-adenosyl-L-homocysteine + 3,7-dimethylxanthine.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei18 – 181S-adenosyl-L-methionine
Binding sitei18 – 181Substrate
Binding sitei60 – 601S-adenosyl-L-methionine; via carbonyl oxygen
Binding sitei66 – 661S-adenosyl-L-methionine
Binding sitei237 – 2371Substrate

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Alkaloid metabolism

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.159. 7042.
2.1.1.160. 7042.

Names & Taxonomyi

Protein namesi
Recommended name:
3,7-dimethylxanthine N-methyltransferase (EC:2.1.1.160)
Short name:
DXMT
Gene namesi
Name:DXMT1
OrganismiCoffea canephora (Robusta coffee)
Taxonomic identifieri49390 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsGentianalesRubiaceaeIxoroideaeCoffeeaeCoffea

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3843843,7-dimethylxanthine N-methyltransferasePRO_0000408470Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
384
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 63Combined sources
Helixi18 – 214Combined sources
Turni24 – 274Combined sources
Helixi28 – 4417Combined sources
Turni48 – 525Combined sources
Beta strandi53 – 608Combined sources
Helixi65 – 7814Combined sources
Beta strandi93 – 997Combined sources
Helixi106 – 12318Combined sources
Beta strandi130 – 1356Combined sources
Beta strandi150 – 1578Combined sources
Beta strandi163 – 1653Combined sources
Beta strandi182 – 1843Combined sources
Helixi190 – 21425Combined sources
Beta strandi215 – 22612Combined sources
Turni230 – 2323Combined sources
Helixi237 – 25014Combined sources
Helixi256 – 2605Combined sources
Helixi271 – 28111Combined sources
Beta strandi283 – 29513Combined sources
Turni296 – 2994Combined sources
Helixi315 – 34127Combined sources
Helixi346 – 36318Combined sources
Beta strandi367 – 37711Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EFJX-ray2.00A1-384[»]
ProteinModelPortaliA4GE70.
SMRiA4GE70. Positions 3-379.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA4GE70.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni99 – 1013S-adenosyl-L-methionine binding
Regioni139 – 1402S-adenosyl-L-methionine binding
Regioni156 – 1583S-adenosyl-L-methionine binding
Regioni157 – 1615Substrate binding

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.150. 3 hits.
InterProiIPR005299. MeTrfase_7.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF03492. Methyltransf_7. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

A4GE70-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELQEVLHMN GGEGDTSYAK NSSYNLFLIR VKPVLEQCIQ ELLRANLPNI
60 70 80 90 100
NKCFKVGDLG CASGPNTFST VRDIVQSIDK VGQEKKNELE RPTIQIFLND
110 120 130 140 150
LFQNDFNSVF KLLPSFYRNL EKENGRKIGS CLIGAMPGSF YSRLFPEESM
160 170 180 190 200
HFLHSCYCLH WLSQVPSGLV TELGISVNKG CIYSSKASRP PIQKAYLDQF
210 220 230 240 250
TKDFTTFLRI HSEELISRGR MLLTFICKED EFDHPNSMDL LEMSINDLVI
260 270 280 290 300
EGHLEEEKLD SFNVPIYAPS TEEVKRIVEE EGSFEILYLE TFNAPYDAGF
310 320 330 340 350
SIDDDYQGRS HSPVSCDEHA RAAHVASVVR SIYEPILASH FGEAILPDLS
360 370 380
HRIAKNAAKV LRSGKGFYDS VIISLAKKPE KADM
Length:384
Mass (Da):43,354
Last modified:April 17, 2007 - v1
Checksum:iCDEB633A499EF3CB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ422955 mRNA. Translation: ABD90686.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ422955 mRNA. Translation: ABD90686.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EFJX-ray2.00A1-384[»]
ProteinModelPortaliA4GE70.
SMRiA4GE70. Positions 3-379.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.1.1.159. 7042.
2.1.1.160. 7042.

Miscellaneous databases

EvolutionaryTraceiA4GE70.

Family and domain databases

Gene3Di3.40.50.150. 3 hits.
InterProiIPR005299. MeTrfase_7.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF03492. Methyltransf_7. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning, expression, crystallization and preliminary X-ray analysis of the XMT and DXMT N-methyltransferases from Coffea canephora (robusta)."
    McCarthy A.A., Biget L., Lin C., Petiard V., Tanksley S.D., McCarthy J.G.
    Acta Crystallogr. F 63:304-307(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CRYSTALLIZATION.
  2. "The structure of two N-methyltransferases from the caffeine biosynthetic pathway."
    McCarthy A.A., McCarthy J.G.
    Plant Physiol. 144:879-889(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE AND THEOBROMINE, SUBUNIT, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiDXMT1_COFCA
AccessioniPrimary (citable) accession number: A4GE70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: April 17, 2007
Last modified: December 9, 2015
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.