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Q8K9E5 (METK_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Short name=AdoMet synthase
EC=2.5.1.6
Alternative name(s):
MAT
Methionine adenosyltransferase
Gene names
Name:metK
Ordered Locus Names:BUsg_393
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length379 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. HAMAP-Rule MF_00086

Catalytic activity

ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine. HAMAP-Rule MF_00086

Cofactor

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

Binds 1 potassium ion per subunit By similarity. HAMAP-Rule MF_00086

Pathway

Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. HAMAP-Rule MF_00086

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00086

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00086.

Sequence similarities

Belongs to the AdoMet synthase family.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   Cellular componentCytoplasm
   LigandATP-binding
Cobalt
Magnesium
Metal-binding
Nucleotide-binding
Potassium
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processS-adenosylmethionine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

one-carbon metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

methionine adenosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 379379S-adenosylmethionine synthase HAMAP-Rule MF_00086
PRO_0000174503

Regions

Nucleotide binding260 – 2678ATP Potential

Sites

Metal binding171Magnesium By similarity
Metal binding431Potassium By similarity
Metal binding2641Potassium By similarity
Metal binding2721Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8K9E5 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 8D5576799F7DAFE7

FASTA37942,003
        10         20         30         40         50         60 
MTEYLFTSES VSEGHPDKIA DQISDALLDE IIKQDLKARV ACETYVKTGM VLIGGEITTT 

        70         80         90        100        110        120 
AWVDVEEITR NTINNIGYIN SETGFDANSC AVLSTIGKQS PDITQGVDRC NPLEQGAGDQ 

       130        140        150        160        170        180 
GIIFGYATNE TEVLMPAPIT YAHLLVKKQS ELRKKNILHW LRPDAKSQVT FKYKNGRIIG 

       190        200        210        220        230        240 
IDTVVFSTQH KESITQDVLK EAVMEEIIKP VLPNKWLTKN TKFFINPTGR FVIGGPMGDC 

       250        260        270        280        290        300 
GLTGRKIIVD TYGGMSRHGG GAFSGKDPSK VDRSAAYAAR YVAKNIVAAG LADRCEIQLS 

       310        320        330        340        350        360 
YAIGIAEPTS IMIETFRTGK ISNKSLINLV RNIFDLRPYG LIEMLDLLRP IYLNTAVYGH 

       370 
FGREEFPWEK LDKVDELLQ 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67945.1.
RefSeqNP_660734.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K9E5.
SMRQ8K9E5. Positions 3-377.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg393.

Proteomic databases

PRIDEQ8K9E5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67945; AAM67945; BUsg_393.
GeneID1005765.
KEGGbas:BUsg393.
PATRIC21247606. VBIBucAph100086_0406.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0192.
KOK00789.
OMAGYVNSEM.
OrthoDBEOG68WR6M.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-413-MONOMER.
UniPathwayUPA00315; UER00080.

Family and domain databases

HAMAPMF_00086. S_AdoMet_synth1.
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. PTHR11964. 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. SSF55973. 3 hits.
TIGRFAMsTIGR01034. metK. 1 hit.
PROSITEPS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMETK_BUCAP
AccessionPrimary (citable) accession number: Q8K9E5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: May 14, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names