Q7XZR1 (METK1_ATRNU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
S-adenosylmethionine synthase 1
Short name=AdoMet synthase 1
EC=2.5.1.6

Alternative name(s):
Methionine adenosyltransferase 1
Short name=MAT 1

Gene names

Name:

SAMS1

Organism

Atriplex nummularia (Old man saltbush) (Atriplex johnstonii)

Taxonomic identifier

3553 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Atriplex

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. May be involved in the synthesis of betain in response to abiotic stress such as high salinity. Ref.1
Catalytic activity	ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine.
Cofactor	Binds 2 divalent ions per subunit. Magnesium or cobalt By similarity. Binds 1 potassium ion per subunit By similarity.
Pathway	Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Expressed in roots, stems and leaves (at protein level). Ref.1
Induction	By salt stress, in stems and leaves (at protein level). Follow a circadian regulation with higher levels in the light. Ref.1
Sequence similarities	Belongs to the AdoMet synthase family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Cellular component	Cytoplasm
Ligand	ATP-binding Cobalt Magnesium Metal-binding Nucleotide-binding Potassium
Molecular function	Transferase
Gene Ontology (GO)
Biological process	S-adenosylmethionine biosynthetic process Inferred from electronic annotation. Source: InterPro one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW methionine adenosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 396	396	S-adenosylmethionine synthase 1		PRO_0000363005
Regions
	Nucleotide binding	123 – 128	6	ATP Potential
	Nucleotide binding	271 – 278	8	ATP Potential
Sites
	Metal binding	21	1	Magnesium By similarity
	Metal binding	47	1	Potassium By similarity
	Metal binding	275	1	Potassium By similarity
	Metal binding	283	1	Magnesium By similarity
	Binding site	151	1	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q7XZR1 [UniParc]. Last modified May 15, 2007. Version 2. Checksum: 9AC20060AA5D3C72	FASTA	396	43,188
	10 20 30 40 50 60 MAAAVDTFLF TSESVNEGHP DKLCDQISDA VLDACLAQDP ESKVACETCT KTNLVMVFGE 70 80 90 100 110 120 ITTKANVDYE KIVRQTCRDI GFVSADVGLD ADNCKVLVYI EQQSPDIAQG VHGHLSRRPE 130 140 150 160 170 180 EIGAGDQGHM FGYATDETPE LMPLSHVLAT KLGARLTEVR KNGTCPWLRP DGKTQVTVEY 190 200 210 220 230 240 YNENGAMVPI RVHTVLISTQ HDETVTNDEI AADLKEHVIK PVIPEKYLDE KTIFHLNPSG 250 260 270 280 290 300 RFVIGGPHGD AGLTGRKIII DTYGGWGAHG GGAFSGKDPT KVDRSGAYIA RQAAKSIVAA 310 320 330 340 350 360 GLARRCIVQI SYAIGVPEPL SVFVDTYGTG KIPDKEILKI VKETFDFRPG MIAINLDLLK 370 380 390 GGSRYLKTAA YGHFGRDDAD FTWETVKPLK WEKPQA

References

[1]

"Similar regulation patterns of choline monooxygenase, phosphoethanolamine N-methyltransferase and S-adenosyl-L-methionine synthetase in leaves of the halophyte Atriplex nummularia L." Tabuchi T., Kawaguchi Y., Azuma T., Nanmori T., Yasuda T. Plant Cell Physiol. 46:505-513(2005) [PubMed: 15695433] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION. Tissue: Shoot.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB112480 mRNA. Translation: BAC77697.2. AB183561 mRNA. Translation: BAD29707.1.
3D structure databases
HSSP	HSSP built from PDB template 1QM4 based on UniProtKB P13444.
ProteinModelPortal	Q7XZR1.
SMR	Q7XZR1. Positions 7-391.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	2.5.1.6. 7740.
Family and domain databases
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. [Graphical view]
PANTHER	PTHR11964. S-AdoMet_synt. 1 hit.
Pfam	PF02773. S-AdoMet_synt_C. 1 hit. PF02772. S-AdoMet_synt_M. 1 hit. PF00438. S-AdoMet_synt_N. 1 hit. [Graphical view]
PIRSF	PIRSF000497. MAT. 1 hit.
SUPFAM	SSF55973. S-AdoMet_synt. 3 hits.
TIGRFAMs	TIGR01034. MetK. 1 hit.
PROSITE	PS00376. ADOMET_SYNTHASE_1. 1 hit. PS00377. ADOMET_SYNTHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

METK1_ATRNU

Accession

Primary (citable) accession number: Q7XZR1
Secondary accession number(s): Q6F3F4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	May 15, 2007
Last modified:	June 28, 2011
This is version 51 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program