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Reviewed, UniProtKB/Swiss-Prot A9PDZ7 (METK2_POPTR)

Last modified October 13, 2009. Version 13. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    S-adenosylmethionine synthetase 2
      Short name=AdoMet synthetase 2
    EC=2.5.1.6
Alternative name(s):
    Methionine adenosyltransferase 2
      Short name=MAT 2
Gene names
Name: METK2
OrganismPopulus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa)
Taxonomic identifier3694 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IMalpighialesSalicaceaeSaliceaePopulus

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme By similarity.

Catalytic activity

ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine.

Cofactor

Binds 2 divalent ions per subunit. Magnesium or cobalt By similarity.

Binds 1 potassium ion per subunit By similarity.

Pathway

Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the AdoMet synthetase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393S-adenosylmethionine synthetase 2
PRO_0000363043

Regions

Nucleotide binding119 – 1246ATP Potential
Nucleotide binding267 – 2748ATP Potential

Sites

Metal binding171Magnesium By similarity
Metal binding431Potassium By similarity
Metal binding2711Potassium By similarity
Metal binding2791Magnesium By similarity
Binding site1471ATP Potential

Sequences

Sequence LengthMass (Da)Tools
A9PDZ7-1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 9D2A40A1CFED0396

FASTA39342,923
        10         20         30         40         50         60 
METFLFTSES VNEGHPDKLC DQVSDAILDA CLEQDPDSKV ACETCTKTNM VMVFGEITTK 

        70         80         90        100        110        120 
ANVDYEKIVR STCRSIGFVS DDVGLDADKC NVLVNIEQQS PDIAQGVHGH LTKRPEEIGA 

       130        140        150        160        170        180 
GDQGHMFGYA TDETPELMPL SHVLATKLGA RLTEVRKNGT CPWLRPDGKT QVTVEYLNEN 

       190        200        210        220        230        240 
GAMVPIRVHT VLISTQHDET VTNDEIAADL KEHVIKPVIP EKYLDEKTIF HLNPSGRFVI 

       250        260        270        280        290        300 
GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSIVASGLAR 

       310        320        330        340        350        360 
RCIVQVSYAI GVPEPLSVFV DTYGTGKIPD KEILNIVKEK FDFRPGMIAI SLDLKRGGNG 

       370        380        390 
RFLKTAAYGH FGRDDPDFTW EVVKPLKSEK PQQ 

« Hide

References

[1]"The poplar transcriptome: Analysis of ca. 4,700 sequence-verified full-length cDNAs."
Ralph S.G., Chun H.J.E., Cooper D., Kirkpatrick R., Palmquist D., Wynhoven B., Kolosova N., Oddy C., Jancsik S., Douglas C.J., Liu J., Butterfield Y.S.N., Stott J., Yang G., Holt R.A., Siddiqui A., Jones S.J.M., Marra M.A., Ritland K., Bohlmann J.
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Nisqually.
Tissue: Cambium and Phloem.

Cross-references

Sequence databases

EF146533 mRNA. Translation: ABK94600.1.

3D structure databases

ModBaseSearch...

Family and domain databases

InterProIPR002133. S-AdoMet_synthetase.
[Graphical view]
PANTHERPTHR11964. S-AdoMet_synt. 1 hit.
PfamPF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]
PIRSFPIRSF000497. MAT. 1 hit.
TIGRFAMsTIGR01034. metK. 1 hit.
PROSITEPS00376. ADOMET_SYNTHETASE_1. 1 hit.
PS00377. ADOMET_SYNTHETASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMETK2_POPTR
AccessionPrimary (citable) accession number: A9PDZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: February 5, 2008
Last modified: October 13, 2009
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents