Reviewed, UniProtKB/Swiss-Prot Q96552 (METK2_CATRO)

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:

SAMS2

Organism

Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)

Taxonomic identifier

4058 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Gentianales › Apocynaceae › Rauvolfioideae › Vinceae › Catharanthus

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine.
Cofactor	Binds 2 divalent ions per subunit. Manganese, magnesium or cobalt. Ref.1 Binds 1 potassium ion per subunit. Can be replaced by NH4. Ref.1
Enzyme regulation	Inhibited by products of SAMS reaction (SAM, Pi, PPi), substrate analogs (cycloleucine and ethionine), and alternative nucleotides (GTP, CTP and ADP). Strongly repressed by PPPi. Ref.1
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	Mostly expressed in roots, and, to a lower extent, in hypocotyls and cotyledons. Ref.1
Induction	Transiently induced by elicitors from Phytophthora megasperma, salt stress, and sucrose. Ref.1
Sequence similarities	Belongs to the AdoMet synthetase family.
Biophysicochemical properties	Kinetic parameters: KM=109 µM for L-methionine KM=181 µM for ATP pH dependence: Optimum pH is 7-8.3. Temperature dependence: Optimum temperature is 37-45 degrees Celsius.

Ontologies

Keywords
Biological process	One-carbon metabolism
Cellular component	Cytoplasm
Ligand	ATP-binding Cobalt Magnesium Manganese 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 manganese 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 – 393	393	S-adenosylmethionine synthetase 2		PRO_0000174460
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)
	Q96552-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 4A9070FB5B9B783D	FASTA	393	43,004
	10 20 30 40 50 60 METFLFTSES VNEGHPDKLC DQISDAVLDA CLAQDPESKV ACETCTKTNM VMVFGEITTK 70 80 90 100 110 120 AQVDYEKIVR DTCRAIGFVS DDVGLDADNC KVLVNIEQQS PDIAQGVHGH LTKRPEEIGA 130 140 150 160 170 180 GDQGHMFGYA TDETPELMPL SHVLATKLGA RLTEVRKNGT CPWLRPDGKT QVTVEYYNDN 190 200 210 220 230 240 GAMVPIRVHT VLISTQHDET VTNDEIAADL KEHVIKPVVP EKYLDEKTIF HLNPSGRFVI 250 260 270 280 290 300 GGPHGDAGLT GRKIIIDTYG GWGAHGGGAF SGKDPTKVDR SGAYIVRQAA KSIVASGLAR 310 320 330 340 350 360 RCIVQVSYAI GVPEPLSVFV DTYGTGKIPD KEILKIVKEN FDFRPGMIAI NLDLKRGGNS 370 380 390 RFLKTAAYGH FGREDPDFTW EVVKPLKFEK VEA

References

[1]

"Three differentially expressed S-adenosylmethionine synthetases from Catharanthus roseus: molecular and functional characterization." Schroeder G., Eichel J., Breinig S., Schroeder J. Plant Mol. Biol. 33:211-222(1997) [PubMed: 9037140] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY, INDUCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z71272 mRNA. Translation: CAA95857.1.
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. 20471.
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_CATRO

Accession

Primary (citable) accession number: Q96552

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	February 1, 1997
Last modified:	September 22, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)