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P50301 (METK1_ACTCH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 66. 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 1

Short name=AdoMet synthase 1
EC=2.5.1.6
Alternative name(s):
Methionine adenosyltransferase 1
Short name=MAT 1
Gene names
Name:SAM1
OrganismActinidia chinensis (Kiwi) (Yangtao)
Taxonomic identifier3625 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridsEricalesActinidiaceaeActinidia

Protein attributes

Sequence length390 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 – 390390S-adenosylmethionine synthase 1
PRO_0000174453

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
P50301 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: E3B66B10112B1E31

FASTA39042,519
        10         20         30         40         50         60 
MDTFLFTSES VNEGHPDKLC DQVSDAILDA CLKQDPESKV ACESCTKTNM VMVFGEITTK 

        70         80         90        100        110        120 
AQVNYEKIVR DTCRGIGFTS PDVGLDADHC KVLVNIEQQS PDIAQGVHGH LTKKPEEIGA 

       130        140        150        160        170        180 
GDQGHMFGYA TDETPELMPL THVLATKLGA KLTEVRKNST CPWLRPDGKT QVTVEYRNEG 

       190        200        210        220        230        240 
GAMVPIRVHT VLISTQHDET VTNDQIANDL KKHVIKPVVP AQYLDDNTIF HLNPSGRFVI 

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

       310        320        330        340        350        360 
RCLVQVSYAI GVAEPLSVFV DTYKTGKIAD KDILALIKEN FDFRPGMIAI NLDLKRGGNL 

       370        380        390 
RYQKTAAYGH FGRDDPDFTW ETVKILKPKA 

« Hide

References

[1]"Three cDNAs encoding S-adenosyl-L-methionine synthetase from Actinidia chinensis."
Whittaker D.J., Smith G.S., Gardner R.C.
Plant Physiol. 108:1307-1308(1995) [PubMed: 7630953] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fruit.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U17240 mRNA. Translation: AAA81378.1.

3D structure databases

ProteinModelPortalP50301.
SMRP50301. Positions 3-387.
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 nameMETK1_ACTCH
AccessionPrimary (citable) accession number: P50301
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 28, 2011
This is version 66 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