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Protein

S-adenosylmethionine synthase

Gene

metK

Organism
Mycobacterium marinum (strain ATCC BAA-535 / M)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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.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 annotation, Co2+UniRule annotationNote: Binds 2 divalent ions per subunit. Magnesium or cobalt.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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi19 – 191MagnesiumUniRule annotation
Metal bindingi45 – 451PotassiumUniRule annotation
Metal bindingi284 – 2841PotassiumUniRule annotation
Metal bindingi292 – 2921MagnesiumUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi280 – 2878ATPUniRule annotation

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

BioCyciMMAR216594:GJOB-2220-MONOMER.
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:MMAR_2205
OrganismiMycobacterium marinum (strain ATCC BAA-535 / M)
Taxonomic identifieri216594 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000001190 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403S-adenosylmethionine synthasePRO_1000093065Add
BLAST

Proteomic databases

PRIDEiB2HP50.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi216594.MMAR_2205.

Structurei

Secondary structure

1
403
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 138Combined sources
Helixi18 – 3619Combined sources
Beta strandi41 – 499Combined sources
Beta strandi52 – 609Combined sources
Helixi64 – 685Combined sources
Helixi70 – 8112Combined sources
Helixi86 – 883Combined sources
Turni92 – 943Combined sources
Beta strandi95 – 10410Combined sources
Beta strandi136 – 1438Combined sources
Helixi152 – 16918Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi176 – 18914Combined sources
Beta strandi192 – 20514Combined sources
Turni211 – 2144Combined sources
Helixi215 – 2228Combined sources
Helixi224 – 2318Combined sources
Beta strandi242 – 2465Combined sources
Turni255 – 2584Combined sources
Beta strandi259 – 2624Combined sources
Turni267 – 2748Combined sources
Helixi291 – 30818Combined sources
Beta strandi311 – 32111Combined sources
Beta strandi329 – 3346Combined sources
Beta strandi339 – 3413Combined sources
Helixi343 – 35311Combined sources
Helixi358 – 3647Combined sources
Beta strandi368 – 3703Combined sources
Helixi373 – 3764Combined sources
Beta strandi380 – 3823Combined sources
Beta strandi384 – 3863Combined sources
Helixi389 – 3913Combined sources
Helixi396 – 4027Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RV2X-ray2.00A/B1-403[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AdoMet synthase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CPH. Bacteria.
COG0192. LUCA.
HOGENOMiHOG000245710.
KOiK00789.
OMAiCETQIAY.
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.

B2HP50-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEKGRLFTS ESVTEGHPDK ICDAVSDSVL DALLAADPRS RVAVETLVTT
60 70 80 90 100
GQVHVVGEVT TTAKEAFADI TNIVRERILD IGYDSSDKGF DGASCGVNIG
110 120 130 140 150
IGAQSPDIAQ GVDTAHEARV EGAADPLDAQ GAGDQGLMFG YAINDTPELM
160 170 180 190 200
PLPIALAHRL SRRLTEVRKN GVLPYLRPDG KTQVTIAYED RVPVRLDTVV
210 220 230 240 250
ISTQHADDID LVKTLDPDIR EQVLKTVLDD LAHDTLDASA VRVLVNPTGK
260 270 280 290 300
FVLGGPMGDA GLTGRKIIVD TYGGWARHGG GAFSGKDPSK VDRSAAYAMR
310 320 330 340 350
WVAKNVVAAG LAERVEVQVA YAIGKAAPVG LFVETFGSEA VDPVKIEKAI
360 370 380 390 400
GEVFDLRPGA IIRDLNLLRP IYAPTAAYGH FGRTDVDLPW ERLDKVDDLK

RAI
Length:403
Mass (Da):43,083
Last modified:June 10, 2008 - v1
Checksum:i927899FAF3BDCECD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA. Translation: ACC40654.1.
RefSeqiWP_012393969.1. NC_010612.1.

Genome annotation databases

EnsemblBacteriaiACC40654; ACC40654; MMAR_2205.
KEGGimmi:MMAR_2205.
PATRICi18065349. VBIMycMar75906_2356.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000854 Genomic DNA. Translation: ACC40654.1.
RefSeqiWP_012393969.1. NC_010612.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RV2X-ray2.00A/B1-403[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi216594.MMAR_2205.

Proteomic databases

PRIDEiB2HP50.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACC40654; ACC40654; MMAR_2205.
KEGGimmi:MMAR_2205.
PATRICi18065349. VBIMycMar75906_2356.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00315; UER00080.
BioCyciMMAR216594:GJOB-2220-MONOMER.

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: ATCC BAA-535 / M.

Entry informationi

Entry nameiMETK_MYCMM
AccessioniPrimary (citable) accession number: B2HP50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: November 11, 2015
This is version 53 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.