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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)DescriptionActionsGraphical viewLength
Binding sitei18S-adenosyl-L-methionine1
Binding sitei18Substrate1
Binding sitei60S-adenosyl-L-methionine; via carbonyl oxygen1
Binding sitei66S-adenosyl-L-methionine1
Binding sitei237Substrate1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00004084701 – 3843,7-dimethylxanthine N-methyltransferaseAdd BLAST384

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1384
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni4 – 6Combined sources3
Helixi18 – 21Combined sources4
Turni24 – 27Combined sources4
Helixi28 – 44Combined sources17
Turni48 – 52Combined sources5
Beta strandi53 – 60Combined sources8
Helixi65 – 78Combined sources14
Beta strandi93 – 99Combined sources7
Helixi106 – 123Combined sources18
Beta strandi130 – 135Combined sources6
Beta strandi150 – 157Combined sources8
Beta strandi163 – 165Combined sources3
Beta strandi182 – 184Combined sources3
Helixi190 – 214Combined sources25
Beta strandi215 – 226Combined sources12
Turni230 – 232Combined sources3
Helixi237 – 250Combined sources14
Helixi256 – 260Combined sources5
Helixi271 – 281Combined sources11
Beta strandi283 – 295Combined sources13
Turni296 – 299Combined sources4
Helixi315 – 341Combined sources27
Helixi346 – 363Combined sources18
Beta strandi367 – 377Combined sources11

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiA4GE70.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni99 – 101S-adenosyl-L-methionine binding3
Regioni139 – 140S-adenosyl-L-methionine binding2
Regioni156 – 158S-adenosyl-L-methionine binding3
Regioni157 – 161Substrate binding5

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EFJX-ray2.00A1-384[»]
ProteinModelPortaliA4GE70.
SMRiA4GE70.
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...

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: November 30, 2016
This is version 34 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.