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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei18 – 181S-adenosyl-L-methionine
Binding sitei61 – 611S-adenosyl-L-methionine; via carbonyl oxygen
Binding sitei316 – 3161Substrate
Binding sitei321 – 3211Substrate
Binding sitei356 – 3561Substrate

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3723727-methylxanthosine synthase 1PRO_0000408469Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
372
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 183Combined sources
Helixi25 – 4521Combined sources
Turni49 – 535Combined sources
Beta strandi54 – 618Combined sources
Helixi66 – 8217Combined sources
Beta strandi94 – 1007Combined sources
Helixi107 – 1126Combined sources
Helixi114 – 12512Combined sources
Beta strandi131 – 1366Combined sources
Beta strandi151 – 1588Combined sources
Beta strandi164 – 1663Combined sources
Turni168 – 1725Combined sources
Helixi191 – 21525Combined sources
Beta strandi216 – 22813Combined sources
Helixi238 – 25114Combined sources
Beta strandi253 – 2553Combined sources
Turni259 – 2624Combined sources
Helixi272 – 28211Combined sources
Beta strandi284 – 29613Combined sources
Turni297 – 3004Combined sources
Helixi309 – 32921Combined sources
Helixi331 – 3333Combined sources
Helixi334 – 34815Combined sources
Helixi349 – 3513Combined sources
Beta strandi354 – 36512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EG5X-ray2.20A/C/E/G1-372[»]
ProteinModelPortaliA4GE69.
SMRiA4GE69. Positions 14-367.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA4GE69.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 255Substrate binding
Regioni99 – 1013S-adenosyl-L-methionine binding
Regioni140 – 1412S-adenosyl-L-methionine binding
Regioni157 – 1593S-adenosyl-L-methionine binding
Regioni161 – 1622Substrate binding

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2EG5X-ray2.20A/C/E/G1-372[»]
ProteinModelPortaliA4GE69.
SMRiA4GE69. Positions 14-367.
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: 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.