Reviewed, UniProtKB/Swiss-Prot P50302 (METK2_ACTCH)

Names and origin

Protein names

Recommended name:
    S-adenosylmethionine synthetase 2
      Short name=AdoMet synthetase 2
    EC=2.5.1.6
Alternative name(s):
    Methionine adenosyltransferase 2
      Short name=MAT 2

Gene names

Name:

SAM2

Organism

Actinidia chinensis (Kiwi) (Yangtao)

Taxonomic identifier

3625 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › Ericales › Actinidiaceae › Actinidia

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
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.
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 – 390	390	S-adenosylmethionine synthetase 2		PRO_0000174454
Regions
	Nucleotide binding	119 – 124	6	ATP Potential
	Nucleotide binding	267 – 274	8	ATP Potential
Sites
	Metal binding	17	1	Magnesium By similarity
	Metal binding	43	1	Potassium By similarity
	Metal binding	271	1	Potassium By similarity
	Metal binding	279	1	Magnesium By similarity
	Binding site	147	1	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	P50302-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: ABB76AE7FD87270F	FASTA	390	42,607
	10 20 30 40 50 60 MESFLFTSES VNEGHPDKLC DQVSDAILDA CLEQDPESKV ACETCTKTNM VMVFGEITTK 70 80 90 100 110 120 AKVNYEKIVR DTCRGIGFTS PDVGLDADHC KVLVNIEQQS PDIAQGVHGH LSKKPEEIGA 130 140 150 160 170 180 GDQGHMFGYA TDETPELMPL THVLATKLGA KLTEVRKNNT CPWLRPDGKT QVTVEYRNEG 190 200 210 220 230 240 GAMVPVRVHT VLISTQHDET VTNEQIAKDL KEHVIKPVIP AQYMDDDTIF HLNPSGRFVI 250 260 270 280 290 300 GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYVVRQAA KSVVASGLAR 310 320 330 340 350 360 RCIVQVSYAI GVPEPLSVFV DTYKTGKIPD KDILALIKEN FDFRPGMIAI NLDLKRGGNF 370 380 390 RYQKTAAYGH FGRDDADLTW ETVKILKPKA

References

[1]	"Three cDNAs encoding S-adenosyl-L-methionine synthetase from Actinidia chinensis." Whittaker D.J., Smith G.S., Gardner R.C. Plant Physiol. 108:1307-1308(1995) [PubMed: 7630953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fruit.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U17239 mRNA. Translation: AAA81377.1.
3D structure databases
HSSP	HSSP built from PDB template 1QM4 based on UniProtKB P13444.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.5.1.6. 67098.
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. PF00438. S-AdoMet_synt_N. 1 hit. [Graphical view]
PIRSF	PIRSF000497. MAT. 1 hit.
TIGRFAMs	TIGR01034. metK. 1 hit.
PROSITE	PS00376. ADOMET_SYNTHETASE_1. 1 hit. PS00377. ADOMET_SYNTHETASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

METK2_ACTCH

Accession

Primary (citable) accession number: P50302

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	September 22, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)