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Protein

S-adenosylmethionine synthase

Gene

metK

Organism
Rickettsia prowazekii (strain Madrid E)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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 sitei15ATPUniRule annotation1
Metal bindingi17MagnesiumUniRule annotation1
Metal bindingi43PotassiumUniRule annotation1
Binding sitei56MethionineUniRule annotation1
Binding sitei99MethionineUniRule annotation1
Binding sitei239ATP; shared with neighboring subunitUniRule annotation1
Binding sitei239Methionine; shared with neighboring subunitUniRule annotation1
Binding sitei266ATP; shared with neighboring subunitUniRule annotation1
Binding sitei270MethionineUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi164 – 166ATPUniRule annotation3
Nucleotide bindingi230 – 231ATPUniRule annotation2
Nucleotide bindingi245 – 246ATPUniRule annotation2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

ATP-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:RP777
OrganismiRickettsia prowazekii (strain Madrid E)
Taxonomic identifieri272947 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group
Proteomesi
  • UP000002480 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001745781 – 380S-adenosylmethionine synthaseAdd BLAST380

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP56878.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni99 – 109Flexible loopUniRule annotationAdd BLAST11

Sequence similaritiesi

Belongs to the AdoMet synthase family.UniRule annotation

Family and domain databases

HAMAPiMF_00086. S_AdoMet_synth1. 1 hit.
InterProiIPR022631. 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]
PANTHERiPTHR11964. PTHR11964. 1 hit.
PfamiPF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000497. MAT. 1 hit.
SUPFAMiSSF55973. SSF55973. 3 hits.
TIGRFAMsiTIGR01034. metK. 1 hit.
PROSITEiPS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P56878-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNFVFTSES VSEGHPDKIA DQISDAVLDE ILKHDPNGRV ACETFVTTGL
60 70 80 90 100
VLVGGEITTN TYVDIEQVVR NKIQEIGYNN PNYGFDGSCC AVISSIIKQS
110 120 130 140 150
PDIAMGIDNE NEEEIGAGDQ GMVFGYACNE TKSLMPAPIY YAHLLMKRQA
160 170 180 190 200
YLRKQNILSW LRPDAKSQVT LRYENNKPIV IDSVVLSTQH HPEIQQKDLI
210 220 230 240 250
EAVIEEIIKP TLPTNLLHKD TKYLINPTGR FVIGGPVADC GLTGRKIIVD
260 270 280 290 300
SYGGMAKHGG GCFSGKDPTK IDRSAAYMAR YIAKNIVGAG LADRCEIQIS
310 320 330 340 350
YAIGVADPVS VYAETFGTSK LSNEQTTKLI TEHFDMRPGK IIKNLKLHTQ
360 370 380
CYQKTATYGH FGREDENFTW EQLDKVDIFK
Length:380
Mass (Da):42,149
Last modified:May 30, 2000 - v1
Checksum:iD1B29BB64481FBCA
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ235273 Genomic DNA. No translation available.
AJ238756 Genomic DNA. Translation: CAB56090.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ235273 Genomic DNA. No translation available.
AJ238756 Genomic DNA. Translation: CAB56090.1.

3D structure databases

ProteinModelPortaliP56878.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00315; UER00080.

Family and domain databases

HAMAPiMF_00086. S_AdoMet_synth1. 1 hit.
InterProiIPR022631. 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]
PANTHERiPTHR11964. PTHR11964. 1 hit.
PfamiPF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000497. MAT. 1 hit.
SUPFAMiSSF55973. SSF55973. 3 hits.
TIGRFAMsiTIGR01034. metK. 1 hit.
PROSITEiPS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMETK_RICPR
AccessioniPrimary (citable) accession number: P56878
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: November 2, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Non-functional in strain Madrid E.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Rickettsia prowazekii
    Rickettsia prowazekii (strain Madrid E): entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.