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Reviewed, UniProtKB/Swiss-Prot Q2RVX7 (METK1_RHORT)

Last modified November 3, 2009. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    S-adenosylmethionine synthetase 1
    EC=2.5.1.6
Alternative name(s):
    Methionine adenosyltransferase 1
    AdoMet synthetase 1
    MAT 1
Gene names
Name: metK1
Ordered Locus Names: Rru_A0917
OrganismRhodospirillum rubrum (strain ATCC 11170 / NCIB 8255) [Complete proteome] [HAMAP]
Taxonomic identifier269796 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum

Protein attributes

Sequence length383 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

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

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm. HAMAP MF_00086

Sequence similarities

Belongs to the AdoMet synthetase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 383383S-adenosylmethionine synthetase 1 HAMAP MF_00086
PRO_0000241030

Regions

Nucleotide binding258 – 2658ATP Potential

Sites

Metal binding171Magnesium By similarity
Metal binding431Potassium By similarity
Metal binding2621Potassium By similarity
Metal binding2701Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2RVX7-1 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 6FF9276010CF87FA

FASTA38340,867
        10         20         30         40         50         60 
MRAYCVTSES VTEGHPDKVC DQISDGILDA CLAQDPAARV AVETLVSGNT VFIAGEITTT 

        70         80         90        100        110        120 
ARLDAVRTAR EVIEDIGYAD PALGFDSGSC FILTNLRTQS PDIDLGVSRG AELGAGDQGV 

       130        140        150        160        170        180 
LYGYACDETA SLMPAPIHMA HGLSLRLAAA RHGGVLPWLR PDGKTQVTVR YDGEGRPEAL 

       190        200        210        220        230        240 
TSVIVSTQHD EGVDRETLVR GIIEAVIYPE VGGWLKPETR VLINPTGRFV IGGPAGDTGV 

       250        260        270        280        290        300 
TGRKLMVDTY GGCARHGGGA FSGKDSTKVD RTAAYMARYA AKNVVAAGLA RRCEVALAYA 

       310        320        330        340        350        360 
IGERLPEMVS VETFGTETID VDRLTAAVRE TFPFSVSGMI AALDLRRPIF RKTAAYGHFG 

       370        380 
RENKGFQWEK TDRVDALRAV CGL 

« Hide

References

[1]"Complete sequence of the chromosome of Rhodospirillum rubrum ATCC 11170."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., Reslewic S., Zhou S., Schwartz D.C.
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000230 Genomic DNA. Translation: ABC21718.1.
RefSeqYP_426005.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ2RVX7.

Genome annotation databases

GeneID3833953.
GenomeReviewsGene locus Rru_A0917 in contig CP000230_GR.
KEGGrru:Rru_A0917.
NMPDRfig|1085.1.peg.3455.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2RVX7.
OMAPWEVPKN.

Enzyme and pathway databases

BioCycRRUB269796:RRU_A0917-MON.

Family and domain databases

HAMAPMF_00086.
[Tree]
InterProIPR002133. S-AdoMet_synthetase.
[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.
TIGRFAMsTIGR01034. metK. 1 hit.
PROSITEPS00376. ADOMET_SYNTHETASE_1. 1 hit.
PS00377. ADOMET_SYNTHETASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMETK1_RHORT
AccessionPrimary (citable) accession number: Q2RVX7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: January 24, 2006
Last modified: November 3, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents