P50303 (METK3_ACTCH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
S-adenosylmethionine synthase 3
Short name=AdoMet synthase 3
EC=2.5.1.6

Alternative name(s):
Methionine adenosyltransferase 3
Short name=MAT 3

Gene names

Name:

SAM3

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	360 AA.
Sequence status	Fragment.
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 – 360	›360	S-adenosylmethionine synthase 3		PRO_0000174455
Regions
	Nucleotide binding	86 – 91	6	ATP Potential
	Nucleotide binding	234 – 241	8	ATP Potential
Sites
	Metal binding	10	1	Potassium By similarity
	Metal binding	238	1	Potassium By similarity
	Metal binding	246	1	Magnesium By similarity
	Binding site	114	1	ATP Potential
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P50303 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: E8B2626FE6E71171	FASTA	360	39,513
	10 20 30 40 50 60 QDPDSKVACE TCTKTNMVMV FGEITTKGNI DYEKIVRDTC RNIGFVSDDV GLDADNCKVL 70 80 90 100 110 120 VNIEQQSPDI AQGVHGHLTK RPEEIGAGDQ GHMFGYATDE TPELMPLSHV LATKLGARLT 130 140 150 160 170 180 EVRKDGTCPW LRPDGKTQVT IEYYNENGAM VPIRVHTVLI STQHDETVTN DKIAADLKEH 190 200 210 220 230 240 VIRPVIPEKY LDEKTIFHLN PSGRFVIGGP HGDAGLTGRK IIIDTYGGWG AHGGGAFSGK 250 260 270 280 290 300 DPTKVDRSGA YIVRQAAKSI VASGLARRCI VQVSYAIGVP EPLSVFVDTY GTGKIPDKEI 310 320 330 340 350 360 LKIVKESFDF RPGMIAIHLD LKRGGNGRFL KTAAYGHFGR DDADFTWEVV KPLKWEKPQD

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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U17241 mRNA. Translation: AAA81379.1.
3D structure databases
ProteinModelPortal	P50303.
SMR	P50303. Positions 1-355.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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

METK3_ACTCH

Accession

Primary (citable) accession number: P50303

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 28, 2011
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program