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Reviewed, UniProtKB/Swiss-Prot A9P2P4 (METK3_PICSI)

Last modified September 22, 2009. Version 11. 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 3
      Short name=AdoMet synthetase 3
    EC=2.5.1.6
Alternative name(s):
    Methionine adenosyltransferase 3
      Short name=MAT 3
Gene names
Name: METK3
OrganismPicea sitchensis (Sitka spruce)
Taxonomic identifier3332 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaConiferopsidaConiferalesPinaceaePicea

Protein attributes

Sequence length394 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 – 394394S-adenosylmethionine synthetase 3
PRO_0000363039

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
A9P2P4-1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: A85E6CD628CA3121

FASTA39443,097
        10         20         30         40         50         60 
METFLFTSES VNEGHPDKLC DQISDAVLDA CLTQDPDSKV ACETCTKTNM VMVFGEITTK 

        70         80         90        100        110        120 
ADVDYEQIVR KTCREIGFIS DDVGLDADHC KVLVNIEQQS PDIAQGVHGH FTKRPEEIGA 

       130        140        150        160        170        180 
GYQGHMFGYA TDETPELMPL THVLATKLGA KLTEVRKNGT CAWLRPDGKT QVTIEYRNDG 

       190        200        210        220        230        240 
GAMVPERVHT VLISTQHDET VTNDQIAADL KQHVIKPVIP EKYLDENTIF HLNPSGRFVI 

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

       310        320        330        340        350        360 
RCLVQVSYAI GVPEPLSVFV DSYGTGTIPD KVILELIKKN FDFRPGMITI NLDLKRGGNG 

       370        380        390 
RFQKTAAYGH FGRDDPDFTW EIVKPLKQEK ALPA 

« Hide

References

[1]"The spruce transcriptome: analysis of ca. 6,500 sequence-verified full-length cDNAs."
Ralph S.G., Kirkpatrick R., Chun H.J.E., Palmquist D., Wynhoven B., Kolosova N., Cooper N., Oddy C., Jancsik S., Ritland C.E., Douglas C.J., Butterfield Y.S.N., Liu J., Stott J., Yang G., Barber S., Holt R.A., Siddiqui A. expand/collapse author list , Jones S.J.M., Marra M.A., Ritland K., Bohlmann J.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. FB3-425.
Tissue: Shoot.

Cross-references

Sequence databases

EF087924 mRNA. Translation: ABK27155.1.

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. False negative.
PS00377. ADOMET_SYNTHETASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMETK3_PICSI
AccessionPrimary (citable) accession number: A9P2P4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: February 5, 2008
Last modified: September 22, 2009
This is version 11 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