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Protein

S-adenosylmethionine synthase

Gene

metK

Organism
Mycobacterium marinum (strain ATCC BAA-535 / M)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionTransferase
Biological processOne-carbon metabolism
LigandATP-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: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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000930651 – 403S-adenosylmethionine synthaseAdd BLAST403

Proteomic databases

PRIDEiB2HP50

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi216594.MMAR_2205

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 strandi311 – 321Combined sources11
Beta strandi329 – 334Combined sources6
Beta strandi339 – 341Combined sources3
Helixi343 – 353Combined sources11
Helixi358 – 364Combined sources7
Beta strandi368 – 370Combined sources3
Helixi373 – 376Combined sources4
Beta strandi380 – 382Combined sources3
Beta strandi384 – 386Combined sources3
Helixi389 – 391Combined sources3
Helixi396 – 402Combined sources7

3D structure databases

SMRiB2HP50
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiENOG4105CPH Bacteria
COG0192 LUCA
HOGENOMiHOG000245710
KOiK00789
OMAiSEFPWEI
OrthoDBiPOG091H00IO

Family and domain databases

HAMAPiMF_00086 S_AdoMet_synth1, 1 hit
InterProiView protein in InterPro
IPR022631 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
PANTHERiPTHR11964 PTHR11964, 1 hit
PfamiView protein in Pfam
PF02773 S-AdoMet_synt_C, 1 hit
PF02772 S-AdoMet_synt_M, 1 hit
PF00438 S-AdoMet_synt_N, 1 hit
PIRSFiPIRSF000497 MAT, 1 hit
SUPFAMiSSF55973 SSF55973, 3 hits
TIGRFAMsiTIGR01034 metK, 1 hit
PROSITEiView protein in PROSITE
PS00376 ADOMET_SYNTHASE_1, 1 hit
PS00377 ADOMET_SYNTHASE_2, 1 hit

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
GeneIDi34341123
KEGGimmi:MMAR_2205

Similar proteinsi

Entry informationi

Entry nameiMETK_MYCMM
AccessioniPrimary (citable) accession number: B2HP50
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: November 22, 2017
This is version 59 of the entry and version 1 of the sequence. See 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

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