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P0A820 (METK_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 65. 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

Short name=AdoMet synthase
EC=2.5.1.6
Alternative name(s):
MAT
Methionine adenosyltransferase
Gene names
Name:metK
Ordered Locus Names:SF2933, S3137
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

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.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the AdoMet synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 384383S-adenosylmethionine synthase HAMAP-Rule MF_00086
PRO_0000174584

Regions

Nucleotide binding260 – 2678ATP Potential
Region239 – 24810Pyrophosphate binding By similarity

Sites

Metal binding171Magnesium By similarity
Metal binding431Potassium By similarity
Metal binding2641Potassium By similarity
Metal binding2721Magnesium By similarity
Binding site1191Methionine By similarity
Binding site2391Methionine By similarity

Amino acid modifications

Modified residue31N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A820 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 97FA8CF17B542941

FASTA38441,952
        10         20         30         40         50         60 
MAKHLFTSES VSEGHPDKIA DQISDAVLDA ILEQDPKARV ACETYVKTGM VLVGGEITTS 

        70         80         90        100        110        120 
AWVDIEEITR NTVREIGYVH SDMGFDANSC AVLSAIGKQS PDINQGVDRA DPLEQGAGDQ 

       130        140        150        160        170        180 
GLMFGYATNE TDVLMPAPIT YAHRLVQRQA EVRKNGTLPW LRPDAKSQVT FQYDDGKIVG 

       190        200        210        220        230        240 
IDAVVLSTQH SEEIDQKSLQ EAVMEEIIKP ILPAEWLTSA TKFFINPTGR FVIGGPMGDC 

       250        260        270        280        290        300 
GLTGRKIIVD TYGGMARHGG GAFSGKDPSK VDRSAAYAAR YVAKNIVAAG LADRCEIQVS 

       310        320        330        340        350        360 
YAIGVAEPTS IMVETFGTEK VPSEQLTLLV REFFDLRPYG LIQMLDLLHP IYKETAAYGH 

       370        380 
FGREHFPWEK TDKAQLLRDA AGLK 

« Hide

References

[1]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005674 Genomic DNA. Translation: AAN44414.2.
AE014073 Genomic DNA. Translation: AAP18239.1.
RefSeqNP_708707.2. NC_004337.2.
NP_838429.1. NC_004741.1.

3D structure databases

ProteinModelPortalP0A820.
SMRP0A820. Positions 2-384.
ModBaseSearch...

Protein-protein interaction databases

STRING198214.SF2933.

Proteomic databases

PaxDbP0A820.
PRIDEP0A820.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN44414; AAN44414; SF2933.
AAP18239; AAP18239; S3137.
GeneID1025940.
1079402.
KEGGsfl:SF2933.
sfx:S3137.
PATRIC18707967. VBIShiFle31049_3433.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0192.
HOGENOMHOG000245710.
KOK00789.
ProtClustDBPRK05250.

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. 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 nameMETK_SHIFL
AccessionPrimary (citable) accession number: P0A820
Secondary accession number(s): P04384, P30869
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families