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Protein

S-adenosylmethionine synthase

Gene

metK

Organism
Rhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalyzes the formation of S-adenosylmethionine (AdoMet) 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.UniRule annotation

Catalytic activityi

ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotationNote: Binds 2 divalent ions per subunit.UniRule annotation
  • K+UniRule annotationNote: Binds 1 potassium ion per subunit.UniRule annotation

Pathwayi: S-adenosyl-L-methionine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes S-adenosyl-L-methionine from L-methionine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. S-adenosylmethionine synthase (metK)
This subpathway is part of the pathway S-adenosyl-L-methionine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes S-adenosyl-L-methionine from L-methionine, the pathway S-adenosyl-L-methionine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei17ATPUniRule annotation1
Metal bindingi19MagnesiumUniRule annotation1
Metal bindingi45PotassiumUniRule annotation1
Binding sitei58MethionineUniRule annotation1
Binding sitei106MethionineUniRule annotation1
Binding sitei241ATP; shared with neighboring subunitUniRule annotation1
Binding sitei241Methionine; shared with neighboring subunitUniRule annotation1
Binding sitei264ATP; via amide nitrogen; shared with neighboring subunitUniRule annotation1
Binding sitei268ATP; shared with neighboring subunitUniRule annotation1
Binding sitei272MethionineUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi166 – 168ATPUniRule annotation3
Nucleotide bindingi247 – 248ATPUniRule annotation2

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processOne-carbon metabolism
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

UniPathwayiUPA00315; UER00080

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine synthaseUniRule annotation (EC:2.5.1.6UniRule annotation)
Short name:
AdoMet synthaseUniRule annotation
Alternative name(s):
MATUniRule annotation
Methionine adenosyltransferaseUniRule annotation
Gene namesi
Name:metKUniRule annotation
Ordered Locus Names:Rsph17029_3280
OrganismiRhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9)
Taxonomic identifieri349101 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
Proteomesi
  • UP000002606 Componenti: Chromosome 2

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003029701 – 388S-adenosylmethionine synthaseAdd BLAST388

Proteomic databases

PRIDEiA3PPW0

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA3PPW0
SMRiA3PPW0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni106 – 116Flexible loopUniRule annotationAdd BLAST11

Sequence similaritiesi

Belongs to the AdoMet synthase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000245710
KOiK00789
OMAiPGHFLFT

Family and domain databases

HAMAPiMF_00086 S_AdoMet_synth1, 1 hit
InterProiView protein in InterPro
IPR022631 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
PANTHERiPTHR11964 PTHR11964, 1 hit
PfamiView protein in Pfam
PF02773 S-AdoMet_synt_C, 1 hit
PF02772 S-AdoMet_synt_M, 1 hit
PF00438 S-AdoMet_synt_N, 1 hit
PIRSFiPIRSF000497 MAT, 1 hit
SUPFAMiSSF55973 SSF55973, 3 hits
TIGRFAMsiTIGR01034 metK, 1 hit
PROSITEiView protein in PROSITE
PS00376 ADOMET_SYNTHASE_1, 1 hit
PS00377 ADOMET_SYNTHASE_2, 1 hit

Sequencei

Sequence statusi: Complete.

A3PPW0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRMNYVFTS ESVSEGHPDK LCDRVSDAVL DTFLAEEPTA RVACETFATT
60 70 80 90 100
GRVVVGGEVG LSDPQKLDEF MERVDGIVRD CVKDIGYEQQ EFHWRTIEVQ
110 120 130 140 150
NFLHRQSAHI AQGVDKDGAG DQGIMFGYAC RETPELMPAP IQYSHAILRR
160 170 180 190 200
LAEVRKSGQE PDLRPDAKSQ LSLRYENGKP VEVRSIVLST QHAHEEQTSD
210 220 230 240 250
DIRAIVEPYI REVLPEGWIT EATEWWVNPT GTFVIGGPDG DAGLTGRKII
260 270 280 290 300
VDTYGGAAPH GGGAFSGKDP TKVDRSAAYA ARYLAKNVVA AGLAERCTLQ
310 320 330 340 350
VSYAIGVAKP LSIYVDTHGT GQVDAAQIEK AVADCMDLTP RGIREHLNLC
360 370 380
RPIYARTSAY GHFGRAPEAD GGFSWERTDL TDALLKAV
Length:388
Mass (Da):42,467
Last modified:April 3, 2007 - v1
Checksum:i4ECB93898D565610
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000578 Genomic DNA Translation: ABN78376.1
RefSeqiWP_002724558.1, NC_009050.1

Genome annotation databases

EnsemblBacteriaiABN78376; ABN78376; Rsph17029_3280
KEGGirsh:Rsph17029_3280

Similar proteinsi

Entry informationi

Entry nameiMETK_RHOS1
AccessioniPrimary (citable) accession number: A3PPW0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: April 3, 2007
Last modified: June 7, 2017
This is version 71 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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