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Protein

S-adenosylmethionine synthase

Gene

metK

Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Status
Reviewed-Annotation score: Annotation score: 3 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 sitei16ATPUniRule annotation1
Metal bindingi18MagnesiumUniRule annotation1
Metal bindingi44PotassiumUniRule annotation1
Binding sitei57MethionineUniRule annotation1
Binding sitei100MethionineUniRule annotation1
Binding sitei240ATP; shared with neighboring subunitUniRule annotation1
Binding sitei240Methionine; shared with neighboring subunitUniRule annotation1
Binding sitei267ATP; shared with neighboring subunitUniRule annotation1
Binding sitei271MethionineUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi165 – 167ATPUniRule annotation3
Nucleotide bindingi231 – 232ATPUniRule annotation2
Nucleotide bindingi246 – 247ATPUniRule 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:CBU_2030
OrganismiCoxiella burnetii (strain RSA 493 / Nine Mile phase I)
Taxonomic identifieri227377 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
Proteomesi
  • UP000002671 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_00001745141 – 393S-adenosylmethionine synthaseAdd BLAST393

Proteomic databases

PRIDEiQ83A78.

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi227377.CBU_2030.

Structurei

3D structure databases

ProteinModelPortaliQ83A78.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni100 – 110Flexible loopUniRule annotationAdd BLAST11

Sequence similaritiesi

Belongs to the AdoMet synthase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CPH. Bacteria.
COG0192. LUCA.
HOGENOMiHOG000245710.
KOiK00789.
OMAiDNFLAFD.

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.

Q83A78-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHTTLFTSE SVSEGHPDKV ADQISDAVLD ALIGQDPNCR VACEAVVKSG
60 70 80 90 100
MVFVAGEITT NAWADVEQIT RNTVLQIGYN DPHLGFDGET CAVVTAIGKQ
110 120 130 140 150
SPDIVMGVDG REDQELGAGD QGLMFGYASR ETNVFMPAPI TYAHRLVRQQ
160 170 180 190 200
ALLRKNGRLP WLRPDAKSQV TLRYENGKPV AADCIVLSTQ HSPEISQESL
210 220 230 240 250
REAVIDEIIK PIMPPHWLDK HTRFLVNPTG RFVIGGPVGD CGLTGRKIIV
260 270 280 290 300
DTYGGMARHG GGCFSGKDPS KVDRSGAYAA RYVAKNIVAG GLADRCEIQV
310 320 330 340 350
SYAIGVAEPT SISVETFGTG KIDEVRIQQL IKEHFDLRPG KIIEELNLLR
360 370 380 390
SIYKATATYG HFGREEPEFT WERTDKAEIL REAAGLAAAN VTN
Length:393
Mass (Da):42,777
Last modified:June 1, 2003 - v1
Checksum:i9AFBE2DA6A03929D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016828 Genomic DNA. Translation: AAO91517.1.
RefSeqiNP_821003.1. NC_002971.3.
WP_010958613.1. NC_002971.3.

Genome annotation databases

EnsemblBacteriaiAAO91517; AAO91517; CBU_2030.
GeneIDi1209943.
KEGGicbu:CBU_2030.
PATRICi17932813. VBICoxBur82552_2023.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016828 Genomic DNA. Translation: AAO91517.1.
RefSeqiNP_821003.1. NC_002971.3.
WP_010958613.1. NC_002971.3.

3D structure databases

ProteinModelPortaliQ83A78.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi227377.CBU_2030.

Proteomic databases

PRIDEiQ83A78.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO91517; AAO91517; CBU_2030.
GeneIDi1209943.
KEGGicbu:CBU_2030.
PATRICi17932813. VBICoxBur82552_2023.

Phylogenomic databases

eggNOGiENOG4105CPH. Bacteria.
COG0192. LUCA.
HOGENOMiHOG000245710.
KOiK00789.
OMAiDNFLAFD.

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_COXBU
AccessioniPrimary (citable) accession number: Q83A78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Coxiella burnetii
    Coxiella burnetii (strain RSA 493): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.