S-adenosylmethionine synthase isoform type-2

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P18298 (METK2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 105. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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

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

Gene names

Name:	Mat2a
Synonyms:	Ams2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	395 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
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	Heterotetramer composed of 2 catalytic alpha subunits (alpha and alpha') (MAT2A) and 1 copy of beta subunit (MAT2B) By similarity.
Tissue specificity	In mammalian tissues, there are three distinct forms of AdoMet synthases designated as alpha, beta, and gamma. Alpha and beta are expressed only in adult liver, while gamma is widely distributed in extrahepatic tissues. In addition, the gamma form predominantly exists in fetal rat liver and is progressively replaced by the alpha and beta forms during development. In the brain, highly expressed at night in pinealocytes (at protein level). Low expression in the medial habenular nucleus, granular layer of the cerebellum, layer II of the neocortex and the pyramidal cells and granular cells of the hippocampal formation. Ref.3 Ref.4
Induction	Exhibits night/day variations with a 5-fold increased expression at night in the pineal gland (at protein level). Up-regulation is due to a large degree to the release of norepinephrine from nerve terminals in the pineal gland and cAMP signaling pathway. Ref.3 Ref.4
Post-translational modification	The alpha' subunit is a post-translationally modified version of MAT2A By similarity.
Sequence similarities	Belongs to the AdoMet synthase family.

Ontologies

Keywords
Biological process	One-carbon metabolism
Ligand	ATP-binding Cobalt Magnesium Metal-binding Nucleotide-binding Potassium
Molecular function	Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	S-adenosylmethionine biosynthetic process Traceable author statement. Source: RGD circadian rhythm Inferred from direct assay Ref.3. Source: RGD one-carbon metabolic process Inferred from electronic annotation. Source: UniProtKB-KW response to cAMP Inferred from direct assay Ref.3. Source: RGD response to drug Inferred from direct assay Ref.3. Source: RGD response to hormone stimulus Inferred from direct assay Ref.3. Source: RGD response to light stimulus Inferred from expression pattern Ref.3. Source: RGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW methionine adenosyltransferase activity Traceable author statement. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 395

395

S-adenosylmethionine synthase isoform type-2

PRO_0000174439

Regions

Nucleotide binding

131 – 136

ATP Potential

Sites

Metal binding

Magnesium By similarity

Metal binding

Potassium By similarity

Metal binding

283

Potassium By similarity

Metal binding

291

Magnesium By similarity

Binding site

159

ATP Potential

Amino acid modifications

Modified residue

N6-acetyllysine By similarity

Modified residue

114

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P18298 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 4DA9AFABF7D09C79
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FASTA

395

43,716

        10         20         30         40         50         60 
MNGQLNGFHE AFIEEGTFLF TSESVGEGHP DKICDQINDA VLDAHLQQDP DAKVACETVA 

        70         80         90        100        110        120 
KTGMILLAGE ITSRAAIDYQ KVVREAIKHI GYDDSSKGFD YKTCNVLVAL EQQSPDIAQG 

       130        140        150        160        170        180 
VHLDRNEEDI GAGDQGLMFG YATDETEECM PLTIVLAHKL NAKLAELRRN GTLPWLRPDS 

       190        200        210        220        230        240 
KTQVTVQYMQ DRGAVIPIRV HTIVISVQHD EEVCLDEMRD ALKEKLIKAV VPAKYLDEDT 

       250        260        270        280        290        300 
IYHLQPSGRF VIGGPQGDAG LTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW 

       310        320        330        340        350        360 
VAKSLVKGGL CRRVLVQVSY AIGVSHPLSI SIFHYGTSQK SERELLEIVK NNFDLRPGVI 

       370        380        390 
VRDLDLKKPI YQRTAAYGHF GRDSFPWEVP KKLKY

« Hide

References

[1]	"Molecular cloning and nucleotide sequence of cDNA encoding the rat kidney S-adenosylmethionine synthetase." Horikawa S., Sasuga J., Shimizu K., Ozasa H., Tsukada K. J. Biol. Chem. 265:13683-13686(1990) [PubMed: 1696256] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Wistar. Tissue: Kidney.
[2]	"Structure of the rat methionine adenosyltransferase 2A gene and its promoter." Hiroki T., Horikawa S., Tsukada K. Eur. J. Biochem. 250:653-660(1997) [PubMed: 9461287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Methionine adenosyltransferase:adrenergic-cAMP mechanism regulates a daily rhythm in pineal expression." Kim J.S., Coon S.L., Blackshaw S., Cepko C.L., Moller M., Mukda S., Zhao W.Q., Charlton C.G., Klein D.C. J. Biol. Chem. 280:677-684(2005) [PubMed: 15504733] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[4]	"Night/day changes in pineal expression of >600 genes: central role of adrenergic/cAMP signaling." Bailey M.J., Coon S.L., Carter D.A., Humphries A., Kim J.S., Shi Q., Gaildrat P., Morin F., Ganguly S., Hogenesch J.B., Weller J.L., Rath M.F., Moller M., Baler R., Sugden D., Rangel Z.G., Munson P.J., Klein D.C. J. Biol. Chem. 284:7606-7622(2009) [PubMed: 19103603] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J05571 mRNA. Translation: AAA42106.1. AB000717 Genomic DNA. Translation: BAA19170.1.
IPI	IPI00189991.
PIR	A37118.
RefSeq	NP_599178.1. NM_134351.1.
UniGene	Rn.144658. Rn.41420.
3D structure databases
ProteinModelPortal	P18298.
SMR	P18298. Positions 16-395.
ModBase	Search...
Protein-protein interaction databases
STRING	P18298.
Proteomic databases
PRIDE	P18298.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	171347.
KEGG	rno:171347.
Organism-specific databases
CTD	4144.
RGD	619985. Mat2a.
Phylogenomic databases
eggNOG	roNOG11914.
HOVERGEN	HBG001562.
InParanoid	P18298.
OrthoDB	EOG4QVCC3.
PhylomeDB	P18298.
Gene expression databases
ArrayExpress	P18298.
Genevestigator	P18298.
GermOnline	ENSRNOG00000013520. Rattus norvegicus.
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]
KO	K00789.
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...
Other
NextBio	622114.

Entry information

Entry name

METK2_RAT

Accession

Primary (citable) accession number: P18298

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	January 25, 2012
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents