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Protein

7-methylxanthosine synthase 1

Gene

XMT1

Organism
Coffea canephora (Robusta coffee)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of caffeine. Specific for xanthosine. Cannot use xanthosine 5'-monophosphate (XMP) as substrate. Directly produces 7-methylxanthine, and therefore the methyl transfer and nucleoside cleavage may be coupled. Catalyzes the 7-N-methylation of xanthosine, but does not have 1-N- or 3-N-methylation activity.

Catalytic activityi

S-adenosyl-L-methionine + xanthosine = S-adenosyl-L-homocysteine + 7-methylxanthosine.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei18S-adenosyl-L-methionine1
Binding sitei61S-adenosyl-L-methionine; via carbonyl oxygen1
Binding sitei316Substrate1
Binding sitei321Substrate1
Binding sitei356Substrate1

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

BRENDAi2.1.1.158. 7042.

Names & Taxonomyi

Protein namesi
Recommended name:
7-methylxanthosine synthase 1 (EC:2.1.1.158)
Alternative name(s):
Xanthosine methyltransferase
Short name:
XMT
Gene namesi
Name:XMT1
OrganismiCoffea canephora (Robusta coffee)
Taxonomic identifieri49390 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsGentianalesRubiaceaeIxoroideaeCoffeeaeCoffea

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004084691 – 3727-methylxanthosine synthase 1Add BLAST372

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1372
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 18Combined sources3
Helixi25 – 45Combined sources21
Turni49 – 53Combined sources5
Beta strandi54 – 61Combined sources8
Helixi66 – 82Combined sources17
Beta strandi94 – 100Combined sources7
Helixi107 – 112Combined sources6
Helixi114 – 125Combined sources12
Beta strandi131 – 136Combined sources6
Beta strandi151 – 158Combined sources8
Beta strandi164 – 166Combined sources3
Turni168 – 172Combined sources5
Helixi191 – 215Combined sources25
Beta strandi216 – 228Combined sources13
Helixi238 – 251Combined sources14
Beta strandi253 – 255Combined sources3
Turni259 – 262Combined sources4
Helixi272 – 282Combined sources11
Beta strandi284 – 296Combined sources13
Turni297 – 300Combined sources4
Helixi309 – 329Combined sources21
Helixi331 – 333Combined sources3
Helixi334 – 348Combined sources15
Helixi349 – 351Combined sources3
Beta strandi354 – 365Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EG5X-ray2.20A/C/E/G1-372[»]
ProteinModelPortaliA4GE69.
SMRiA4GE69.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA4GE69.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni21 – 25Substrate binding5
Regioni99 – 101S-adenosyl-L-methionine binding3
Regioni140 – 141S-adenosyl-L-methionine binding2
Regioni157 – 159S-adenosyl-L-methionine binding3
Regioni161 – 162Substrate binding2

Sequence similaritiesi

Phylogenomic databases

KOiK12729.

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.

A4GE69-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELQEVLRMN GGEGDTSYAK NSAYNQLVLA KVKPVLEQCV RELLRANLPN
60 70 80 90 100
INKCIKVADL GCASGPNTLL TVRDIVQSID KVGQEKKNEL ERPTIQIFLN
110 120 130 140 150
DLFPNDFNSV FKLLPSFYRK LEKENGRKIG SCLIGAMPGS FYSRLFPEES
160 170 180 190 200
MHFLHSCYCL QWLSQVPSGL VTELGIGTNK GSIYSSKASR LPVQKAYLDQ
210 220 230 240 250
FTKDFTTFLR IHSEELFSHG RMLLTCICKG VELDARNAID LLEMAINDLV
260 270 280 290 300
VEGHLEEEKL DSFNLPVYIP SAEEVKCIVE EEGSFEILYL ETFKVLYDAG
310 320 330 340 350
FSIDDEHIKA EYVASSVRAV YEPILASHFG EAIIPDIFHR FAKHAAKVLP
360 370
LGKGFYNNLI ISLAKKPEKS DM
Length:372
Mass (Da):41,844
Last modified:April 17, 2007 - v1
Checksum:iC7493C1BBFF4BD9A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ422954 mRNA. Translation: ABD90685.1.

Genome annotation databases

KEGGiag:ABD90685.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ422954 mRNA. Translation: ABD90685.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EG5X-ray2.20A/C/E/G1-372[»]
ProteinModelPortaliA4GE69.
SMRiA4GE69.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:ABD90685.

Phylogenomic databases

KOiK12729.

Enzyme and pathway databases

BRENDAi2.1.1.158. 7042.

Miscellaneous databases

EvolutionaryTraceiA4GE69.

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 nameiXMT1_COFCA
AccessioniPrimary (citable) accession number: A4GE69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: April 17, 2007
Last modified: November 2, 2016
This is version 33 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.