P93438 (METK2_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
S-adenosylmethionine synthase 2
Short name=AdoMet synthase 2
EC=2.5.1.6

Alternative name(s):
Methionine adenosyltransferase 2
Short name=MAT 2

Gene names

Name:	SAM2
Synonyms:	SAMS2
Ordered Locus Names:	Os01g0323600, LOC_Os01g22010
ORF Names:	OSJNBa0011P19.8

Organism

Oryza sativa subsp. japonica (Rice)

Taxonomic identifier

39947 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza

Protein attributes

Sequence length	394 AA.
Sequence status	Complete.
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 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 – 394	394	S-adenosylmethionine synthase 2		PRO_0000174471
Regions
	Nucleotide binding	121 – 126	6	ATP Potential
	Nucleotide binding	269 – 276	8	ATP Potential
Sites
	Metal binding	19	1	Magnesium By similarity
	Metal binding	45	1	Potassium By similarity
	Metal binding	273	1	Potassium By similarity
	Metal binding	281	1	Magnesium By similarity
	Binding site	149	1	ATP Potential

Sequences

	Sequence		Length	Mass (Da)
	P93438 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 081E9F3E65694EB7	FASTA	394	42,901
	10 20 30 40 50 60 MAAETFLFTS ESVNEGHPDK LCDQVSDAVL DACLAQDPDS KVACETCTKT NMVMVFGEIT 70 80 90 100 110 120 TKATVDYEKI VRDTCRGIGF VSDDVGLDAD RCKVLVNIEQ QSPDIAQGVH GHFTKRPEEI 130 140 150 160 170 180 GAGDQGHMFG YATDETPELM PLSHVLATKL GARLTEVRKN GTCAWLRPDG KTQVTVEYLN 190 200 210 220 230 240 DAGAMVPVRV HTVLISTQHD ETVTNDEIAA DLKEHVIKPV IPDKYLDEKT IFHLNPSGRF 250 260 270 280 290 300 VIGGPHGDAG LTGRKIIIDT YGGWGAHGGG AFSGKDPTKV DRSGAYIARQ AAKSIVASGL 310 320 330 340 350 360 ARRCIVQVSY AIGVPEPLSV FVDSYGTGKI PDKEILKIVK ENFDFRPGMM TINLDLKRGG 370 380 390 NRFIKTAAYG HFGREDPDFT WEVVKPLKYE KASS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and expression of two cDNAs encoding S-adenosyl-L-methionine synthetase of rice (Oryza sativa L.)." Lee J.-H., Chae H.S., Lee J.-H., Hwang B., Hahn K.W., Kang B.G., Kim W.T. Biochim. Biophys. Acta 1354:13-18(1997) [PubMed: 9375784] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The genome sequence and structure of rice chromosome 1." Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y., Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H., Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M. , Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S., Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H., Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S., Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y., Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S., Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H., Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T. Nature 420:312-316(2002) [PubMed: 12447438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U82833 mRNA. Translation: AAC05590.1. AP003211 Genomic DNA. Translation: BAC65881.1.
3D structure databases
ProteinModelPortal	P93438.
SMR	P93438. Positions 5-389.
ModBase	Search...
Protein-protein interaction databases
STRING	P93438.
2D gel databases
ANU-2DPAGE	P93438.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	LOC_Os01g22010.1; LOC_Os01g22010.1; LOC_Os01g22010. LOC_Os01g22010.2; LOC_Os01g22010.2; LOC_Os01g22010. LOC_Os01g22010.3; LOC_Os01g22010.3; LOC_Os01g22010. LOC_Os01g22010.4; LOC_Os01g22010.4; LOC_Os01g22010.
NMPDR	fig|39947.1.peg.305.
Organism-specific databases
Gramene	P93438.
Phylogenomic databases
GeneTree	EPGT00050000019410.
OMA	NRFIKTA.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13932.
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

METK2_ORYSJ

Accession

Primary (citable) accession number: P93438
Secondary accession number(s): Q7F660

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	May 1, 1997
Last modified:	September 21, 2011
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program