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Protein

S-adenosylmethionine synthase 3

Gene

SAMS3

more
Organism
Atriplex nummularia (Old man saltbush) (Atriplex johnstonii)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate (By similarity). May be involved in the synthesis of betain in response to abiotic stress such as high salinity (PubMed:15695433).By similarity1 Publication

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Mn2+By similarity, Mg2+By similarity, Co2+By similarityNote: Binds 2 divalent ions per subunit. The metal ions interact primarily with the substrate (By similarity). Can utilize magnesium, manganese or cobalt (in vitro) (By similarity).By similarity
  • K+By similarityNote: Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate (By similarity).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.By similarity
Proteins known to be involved in this subpathway in this organism are:
  1. S-adenosylmethionine synthase 2 (SAMS2), S-adenosylmethionine synthase 3 (SAMS3), S-adenosylmethionine synthase 1 (SAMS1), S-adenosylmethionine synthase 4 (SAMS4)
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
Metal bindingi13MagnesiumBy similarity1
Binding sitei19ATPBy similarity1
Metal bindingi47PotassiumBy similarity1
Binding sitei60MethionineBy similarity1
Binding sitei103MethionineBy similarity1
Binding sitei250ATPBy similarity1
Binding sitei250Methionine; shared with neighboring subunitBy similarity1
Binding sitei273ATP; via amide nitrogen; shared with neighboring subunitBy similarity1
Binding sitei277ATP; shared with neighboring subunitBy similarity1
Binding sitei281ATP; shared with neighboring subunitBy similarity1
Binding sitei281MethionineBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi171 – 173ATPBy similarity3
Nucleotide bindingi239 – 242ATPBy similarity4
Nucleotide bindingi256 – 257ATPBy similarity2

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processOne-carbon metabolism
LigandATP-binding, Cobalt, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BRENDAi2.5.1.6 7740
UniPathwayiUPA00315; UER00080

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine synthase 3 (EC:2.5.1.6By similarity)
Short name:
AdoMet synthase 3
Alternative name(s):
Methionine adenosyltransferase 3
Short name:
MAT 3
Gene namesi
Name:SAMS3
AND
Name:SAMS5
OrganismiAtriplex nummularia (Old man saltbush) (Atriplex johnstonii)
Taxonomic identifieri3553 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesChenopodiaceaeChenopodioideaeAtripliceaeAtriplex

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003630071 – 396S-adenosylmethionine synthase 3Add BLAST396

Proteomic databases

PRIDEiQ6F3F0

Expressioni

Tissue specificityi

Expressed in roots, stems and leaves (at protein level).1 Publication

Inductioni

By salt stress, in stems and leaves (at protein level). Follow a circadian regulation with higher levels in the light.1 Publication

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ6F3F0
SMRiQ6F3F0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AdoMet synthase family.Curated

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.

Q6F3F0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAVDTFLF TSESVNEGHP DKLCDQISDA VLDACLAQDP ESKVACETCT
60 70 80 90 100
KTNLVMVFGE ITTKANVDYE KIVRQTCRDI GFVSADVGLD ADNCKVLVNI
110 120 130 140 150
EQQSPDIAQG VHGHLTRRPE EIGAGDQGHM FGYATDETPE LMPLSHVLAT
160 170 180 190 200
KLGARLTEVR KNGTCPWLRP DGKTQVTVEY YNENGAMVPI RVHTVLISTQ
210 220 230 240 250
HDETVTNDEI AADLKEHVIK PVIPEKYLDE KTIFHLNPSG RFVIGGPHGD
260 270 280 290 300
AGLTGRKIII DTYGGWGAHG GGAFSGKDPT KVDRSGAYIA RQAAKSIVAA
310 320 330 340 350
GLARRCIVQI SYAIGVPEPL SVFVDTYGTG KIPDKEILKI VKESFDFRPG
360 370 380 390
MIAINLDLLK GGSRYLKTAA YGHFGRDDAD FTWETVKPLK WEKPQA
Length:396
Mass (Da):43,139
Last modified:August 16, 2004 - v1
Checksum:i794719818031915B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB183563 mRNA Translation: BAD29709.1
AB183565 mRNA Translation: BAD29711.1

Similar proteinsi

Entry informationi

Entry nameiMETK3_ATRNU
AccessioniPrimary (citable) accession number: Q6F3F0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: August 16, 2004
Last modified: March 15, 2017
This is version 67 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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