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P56878 (METK_RICPR) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 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:RP777
OrganismRickettsia prowazekii (strain Madrid E) [Reference proteome] [HAMAP]
Taxonomic identifier272947 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length380 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.

Caution

Non-functional in strain Madrid E.

Sequence caution

The sequence AJ235273 differs from that shown. Reason: Erroneous termination at position 141. Translated as Tyr.

Ontologies

Keywords
   Biological processOne-carbon metabolism
   Cellular componentCytoplasm
   LigandATP-binding
Cobalt
Magnesium
Metal-binding
Nucleotide-binding
Potassium
   Molecular functionTransferase
   Technical termComplete proteome
Reference 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 – 380380S-adenosylmethionine synthase HAMAP-Rule MF_00086
PRO_0000174578

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
P56878 [UniParc].

Last modified May 30, 2000. Version 1.
Checksum: D1B29BB64481FBCA

FASTA38042,149
        10         20         30         40         50         60 
MKNFVFTSES VSEGHPDKIA DQISDAVLDE ILKHDPNGRV ACETFVTTGL VLVGGEITTN 

        70         80         90        100        110        120 
TYVDIEQVVR NKIQEIGYNN PNYGFDGSCC AVISSIIKQS PDIAMGIDNE NEEEIGAGDQ 

       130        140        150        160        170        180 
GMVFGYACNE TKSLMPAPIY YAHLLMKRQA YLRKQNILSW LRPDAKSQVT LRYENNKPIV 

       190        200        210        220        230        240 
IDSVVLSTQH HPEIQQKDLI EAVIEEIIKP TLPTNLLHKD TKYLINPTGR FVIGGPVADC 

       250        260        270        280        290        300 
GLTGRKIIVD SYGGMAKHGG GCFSGKDPTK IDRSAAYMAR YIAKNIVGAG LADRCEIQIS 

       310        320        330        340        350        360 
YAIGVADPVS VYAETFGTSK LSNEQTTKLI TEHFDMRPGK IIKNLKLHTQ CYQKTATYGH 

       370        380 
FGREDENFTW EQLDKVDIFK 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Rickettsia prowazekii and the origin of mitochondria."
Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G.
Nature 396:133-140(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Madrid E.
[2]"Genome degradation is an ongoing process in Rickettsia."
Andersson J.O., Andersson S.G.E.
Mol. Biol. Evol. 16:1178-1191(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ235273 Genomic DNA. No translation available.
AJ238756 Genomic DNA. Translation: CAB56090.1.

3D structure databases

ProteinModelPortalP56878.
SMRP56878. Positions 5-380.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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_RICPR
AccessionPrimary (citable) accession number: P56878
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: July 9, 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

Rickettsia prowazekii

Rickettsia prowazekii (strain Madrid E): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways