Reviewed, UniProtKB/Swiss-Prot P31155 (METK1_PETCR)

Names and origin

Protein names

Recommended name:
    S-adenosylmethionine synthetase 1
      Short name=AdoMet synthetase 1
    EC=2.5.1.6
Alternative name(s):
    Methionine adenosyltransferase 1
      Short name=MAT 1

Gene names

Name:

SMS-1

Organism

Petroselinum crispum (Parsley) (Petroselinum hortense)

Taxonomic identifier

4043 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › campanulids › Apiales › Apiaceae › Apioideae › apioid superclade › Apium clade › Petroselinum

Protein attributes

Sequence length	234 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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.
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	Mainly in floral buds and roots.
Induction	By fungal elicitor.
Sequence similarities	Belongs to the AdoMet synthetase 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	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 cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW methionine adenosyltransferase activity Inferred from electronic annotation. Source: EC potassium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 234	›234	S-adenosylmethionine synthetase 1		PRO_0000174474
Regions
	Nucleotide binding	110 – 117	8	ATP Potential
Sites
	Metal binding	114	1	Potassium By similarity
	Metal binding	122	1	Magnesium By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P31155-1 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 8491086FA5D16BDA	FASTA	234	25,652
	10 20 30 40 50 60 NGTCAWLRPD GKTQVTVEYQ NDHGAMVPIR VHTILISTQH DETVTNDEIA ADLKEHVIKP 70 80 90 100 110 120 VVPENYLDEK TIFHLNPSGR FVIGGPHGDA GLTGRKIIID TYGGWGAHGG GAFSGKDPTK 130 140 150 160 170 180 VDRSGAYIVR QAAKSIVASG LARRCIVQVS YAIGVPEPLS VFVDTYGTGK IPDREILKIV 190 200 210 220 230 KETFDFRPGM ISINLDLKRG GNGRFLKTAA YGHFGREDPD FTWEVVKPLK WEKA

References

[1]

"Induction by fungal elicitor of S-adenosyl-L-methionine synthetase and S-adenosyl-L-homocysteine hydrolase mRNAs in cultured cells and leaves of Petroselinum crispum." Kawalleck P., Plesch G., Hahlbrock K., Somssich I.E. Proc. Natl. Acad. Sci. U.S.A. 89:4713-4717(1992) [PubMed: 1374911] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Leaf.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M62758 mRNA. Translation: AAA33857.1.
3D structure databases
HSSP	HSSP built from PDB template 1QM4 based on UniProtKB P13444.
ModBase	Search...
Genome annotation databases
UCSC	H21P03.3a. c. elegans.
Enzyme and pathway databases
BRENDA	2.5.1.6. 2662.
Family and domain databases
InterPro	IPR002133. S-AdoMet_synthetase. [Graphical view]
PANTHER	PTHR11964. S-AdoMet_synt. 1 hit.
Pfam	PF02773. S-AdoMet_synt_C. 1 hit. PF02772. S-AdoMet_synt_M. 1 hit. [Graphical view]
PROSITE	PS00376. ADOMET_SYNTHETASE_1. Partial match. PS00377. ADOMET_SYNTHETASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

METK1_PETCR

Accession

Primary (citable) accession number: P31155

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	September 22, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)