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Protein

S-adenosylmethionine synthase

Gene

metK

Organism
Mycobacterium avium (strain 104)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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 sitei104MethionineUniRule annotation1
Binding sitei259ATP; shared with neighboring subunitUniRule annotation1
Binding sitei259Methionine; shared with neighboring subunitUniRule annotation1
Binding sitei282ATP; via amide nitrogen; shared with neighboring subunitUniRule annotation1
Binding sitei286ATP; shared with neighboring subunitUniRule annotation1
Binding sitei290MethionineUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi179 – 181ATPUniRule annotation3
Nucleotide bindingi250 – 251ATPUniRule annotation2
Nucleotide bindingi265 – 266ATPUniRule 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:MAV_3382
OrganismiMycobacterium avium (strain 104)
Taxonomic identifieri243243 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)
Proteomesi
  • UP000001574 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_00003029391 – 403S-adenosylmethionine synthaseAdd BLAST403

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.UniRule annotation

Structurei

Secondary structure

1403
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 13Combined sources8
Helixi18 – 36Combined sources19
Beta strandi41 – 49Combined sources9
Beta strandi52 – 60Combined sources9
Helixi64 – 68Combined sources5
Helixi70 – 81Combined sources12
Helixi86 – 88Combined sources3
Turni92 – 94Combined sources3
Beta strandi95 – 104Combined sources10
Beta strandi136 – 143Combined sources8
Helixi152 – 169Combined sources18
Beta strandi171 – 173Combined sources3
Beta strandi176 – 189Combined sources14
Beta strandi192 – 205Combined sources14
Turni211 – 214Combined sources4
Helixi215 – 222Combined sources8
Helixi224 – 231Combined sources8
Beta strandi242 – 246Combined sources5
Turni255 – 258Combined sources4
Beta strandi259 – 262Combined sources4
Turni267 – 274Combined sources8
Helixi291 – 308Combined sources18
Beta strandi313 – 321Combined sources9
Beta strandi329 – 334Combined sources6
Helixi343 – 353Combined sources11
Helixi358 – 364Combined sources7
Beta strandi368 – 370Combined sources3
Helixi373 – 375Combined sources3
Beta strandi376 – 378Combined sources3
Beta strandi380 – 382Combined sources3
Beta strandi384 – 386Combined sources3
Helixi389 – 391Combined sources3
Helixi396 – 402Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3S82X-ray1.73A/B1-403[»]
ProteinModelPortaliA0QI26.
SMRiA0QI26.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA0QI26.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni104 – 114Flexible loopUniRule annotationAdd BLAST11

Sequence similaritiesi

Belongs to the AdoMet synthase family.UniRule annotation

Phylogenomic databases

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.

A0QI26-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEKGRLFTS ESVTEGHPDK ICDAISDSVL DALLAQDPRS RVAVETLVTT
60 70 80 90 100
GQVHVVGEVT TTAKEAFADI TNTVRERILD IGYDSSDKGF DGASCGVNIG
110 120 130 140 150
IGAQSPDIAQ GVDTAHETRV EGAADPLDAQ GAGDQGLMFG YAINDTPERM
160 170 180 190 200
PLPIALAHRL SRRLTEVRKN GVLPYLRPDG KTQVTIEFED DVPVRLDTVV
210 220 230 240 250
ISTQHAADID LENTLTPDIR EKVLNTVLND LAHDTLDTSS TRLLVNPTGK
260 270 280 290 300
FVVGGPMGDA GLTGRKIIVD TYGGWARHGG GAFSGKDPSK VDRSAAYAMR
310 320 330 340 350
WVAKNIVAAG LAERVEVQVA YAIGKAAPVG LFIETFGTAT VDPVKIEKIV
360 370 380 390 400
PEVFDLRPGA IIRDLDLLRP IYAQTAAYGH FGRTDVELPW EQLNKVDDLK

RAI
Length:403
Mass (Da):43,306
Last modified:January 9, 2007 - v1
Checksum:i8BB763DF835F67E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000479 Genomic DNA. Translation: ABK67721.1.
RefSeqiWP_008258192.1. NC_008595.1.

Genome annotation databases

EnsemblBacteriaiABK67721; ABK67721; MAV_3382.
GeneIDi11909961.
KEGGimav:MAV_3382.
PATRICi17988453. VBIMycAvi38287_3311.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000479 Genomic DNA. Translation: ABK67721.1.
RefSeqiWP_008258192.1. NC_008595.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3S82X-ray1.73A/B1-403[»]
ProteinModelPortaliA0QI26.
SMRiA0QI26.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK67721; ABK67721; MAV_3382.
GeneIDi11909961.
KEGGimav:MAV_3382.
PATRICi17988453. VBIMycAvi38287_3311.

Phylogenomic databases

HOGENOMiHOG000245710.
KOiK00789.
OMAiDNFLAFD.

Enzyme and pathway databases

UniPathwayiUPA00315; UER00080.

Miscellaneous databases

EvolutionaryTraceiA0QI26.

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_MYCA1
AccessioniPrimary (citable) accession number: A0QI26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: January 9, 2007
Last modified: November 2, 2016
This is version 72 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

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.