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Protein

S-adenosylmethionine synthase

Gene

metK

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarity, Co2+By similarityNote: Binds 2 divalent ions per subunit. Magnesium or cobalt.By similarity
  • K+By similarityNote: Binds 1 potassium ion per subunit.By similarity

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.
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi19 – 191MagnesiumBy similarity
Metal bindingi45 – 451PotassiumBy similarity
Metal bindingi284 – 2841PotassiumBy similarity
Metal bindingi292 – 2921MagnesiumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi280 – 2878ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

ATP-binding, Cobalt, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

UniPathwayiUPA00315; UER00080.

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine synthase (EC:2.5.1.6)
Short name:
AdoMet synthase
Alternative name(s):
MAT
Methionine adenosyltransferase
Gene namesi
Name:metK
Ordered Locus Names:ML0544
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000000806 Componenti: Chromosome

Organism-specific databases

LepromaiML0544.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403S-adenosylmethionine synthasePRO_0000174555Add
BLAST

Proteomic databases

PRIDEiQ9CCQ4.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

STRINGi272631.ML0544.

Structurei

3D structure databases

ProteinModelPortaliQ9CCQ4.
SMRiQ9CCQ4. Positions 5-403.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AdoMet synthase family.Curated

Phylogenomic databases

eggNOGiENOG4105CPH. Bacteria.
COG0192. LUCA.
HOGENOMiHOG000245710.
KOiK00789.
OMAiDNFLAFD.
OrthoDBiEOG68WR6M.

Family and domain databases

HAMAPiMF_00086. S_AdoMet_synth1.
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.

Q9CCQ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEKGRLFTS ESVTEGHPDK ICDAISDSIL DALLAEDPCS RVAVETLVTT
60 70 80 90 100
GQVHVVGEVT TLAKTAFADI SNTVRERILD IGYDSSDKGF DGASCGVNIG
110 120 130 140 150
IGAQSSDIAQ GVNTAHEVRV EGAADPLDAQ GAGDQGLMFG YAINDTPELM
160 170 180 190 200
PLPIALAHRL ARRLTEVRKN GVLPYLRSDG KTQVTIAYED NVPVRLDTVV
210 220 230 240 250
ISTQHAAGVD LDATLAPDIR EKVLNTVIDD LSHDTLDVSS VRVLVNPTGK
260 270 280 290 300
FVLGGPMGDA GLTGRKIIVD TYGGWARHGG GAFSGKDPSK VDRSAAYAMR
310 320 330 340 350
WVAKNIVAAG LAERIEVQVA YAIGKAAPVG LFVETFGTEA VDPAKIEKAI
360 370 380 390 400
GEVFDLRPGA IIRDLHLLRP IYAQTAAYGH FGRTDVELPW EQLNKVDDLK

RAI
Length:403
Mass (Da):42,921
Last modified:June 1, 2001 - v1
Checksum:iF9171EFE6B502A6B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL583918 Genomic DNA. Translation: CAC30052.1.
PIRiH86976.
RefSeqiNP_301463.1. NC_002677.1.
WP_010907787.1. NC_002677.1.

Genome annotation databases

EnsemblBacteriaiCAC30052; CAC30052; CAC30052.
GeneIDi909312.
KEGGimle:ML0544.
PATRICi18051996. VBIMycLep78757_0945.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL583918 Genomic DNA. Translation: CAC30052.1.
PIRiH86976.
RefSeqiNP_301463.1. NC_002677.1.
WP_010907787.1. NC_002677.1.

3D structure databases

ProteinModelPortaliQ9CCQ4.
SMRiQ9CCQ4. Positions 5-403.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272631.ML0544.

Proteomic databases

PRIDEiQ9CCQ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC30052; CAC30052; CAC30052.
GeneIDi909312.
KEGGimle:ML0544.
PATRICi18051996. VBIMycLep78757_0945.

Organism-specific databases

LepromaiML0544.

Phylogenomic databases

eggNOGiENOG4105CPH. Bacteria.
COG0192. LUCA.
HOGENOMiHOG000245710.
KOiK00789.
OMAiDNFLAFD.
OrthoDBiEOG68WR6M.

Enzyme and pathway databases

UniPathwayiUPA00315; UER00080.

Family and domain databases

HAMAPiMF_00086. S_AdoMet_synth1.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TN.

Entry informationi

Entry nameiMETK_MYCLE
AccessioniPrimary (citable) accession number: Q9CCQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: June 1, 2001
Last modified: November 11, 2015
This is version 99 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.