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P24260 (METK2_DIACA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
S-adenosylmethionine synthase 2

Short name=AdoMet synthase 2
EC=2.5.1.6
Alternative name(s):
Methionine adenosyltransferase 2
Short name=MAT 2
Gene names
Name:SAM2
OrganismDianthus caryophyllus (Carnation) (Clove pink)
Taxonomic identifier3570 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsCaryophyllalesCaryophyllaceaeDianthus

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
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 synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 396396S-adenosylmethionine synthase 2
PRO_0000174462

Regions

Nucleotide binding123 – 1286ATP Potential
Nucleotide binding271 – 2788ATP Potential

Sites

Metal binding211Magnesium By similarity
Metal binding471Potassium By similarity
Metal binding2751Potassium By similarity
Metal binding2831Magnesium By similarity
Binding site1511ATP Potential

Sequences

Sequence LengthMass (Da)Tools
P24260 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: 959024A69865E2D9

FASTA39643,189
        10         20         30         40         50         60 
MAAAADTFLF TSESVNEGHP DKLCDQISDA VLDACLAQDA ESKVACETCT KTNLVMVFGE 

        70         80         90        100        110        120 
ITTKANVDYE KIVADTCREI GFVSPDVGLD ADNCKVLVYI EQQSPDIAQG VHGHLTKRPE 

       130        140        150        160        170        180 
DIGAGDQGHM FGYATDETPE LMPLSHVLAT KLGARLTEVR KNGTCAWLRP DGKTQVTVEY 

       190        200        210        220        230        240 
YNENGAMVPI RVHTVLISTQ HDETVTNDEI AADLKEHVIK PVIPEKYLDE NTIFHLNPSG 

       250        260        270        280        290        300 
RFVIGGPHGD AGLTGRKIII DTYGGWGAHG GGAFSRKDPT KVDRSGAYIA RQAAKSIVAS 

       310        320        330        340        350        360 
GLARRCIVQI SYAIGVPEPL SVFVDTYGTG KIHDREILKI VKENFDFRPG MIAIALDLKK 

       370        380        390 
GGNRYLKTAA YGHFGREDPD FTWEAAKTLK WEKPQA 

« Hide

References

[1]"Cloning and nucleotide sequence of a S-adenosylmethionine synthetase cDNA clone from carnation."
Larsen P.B., Woodson W.R.
Plant Physiol. 96:997-999(1991) [PubMed: 16668288] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M61882 mRNA. Translation: AAA33274.1.
PIRT10710.

3D structure databases

ProteinModelPortalP24260.
SMRP24260. Positions 7-391.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR022631. ADOMET_SYNTHASE_CS.
IPR022630. S-AdoMet_synt_C.
IPR022629. S-AdoMet_synt_central.
IPR022628. S-AdoMet_synt_N.
IPR002133. S-AdoMet_synthetase.
IPR022636. S-AdoMet_synthetase_sfam.
[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.
SUPFAMSSF55973. S-AdoMet_synt. 3 hits.
TIGRFAMsTIGR01034. MetK. 1 hit.
PROSITEPS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMETK2_DIACA
AccessionPrimary (citable) accession number: P24260
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: June 28, 2011
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families