Mat2a

Functionⁱ

Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.By similarity

Catalytic activityⁱ

ATP + L-methionine + H₂O = phosphate + diphosphate + S-adenosyl-L-methionine.By similarity

Cofactorⁱ

Protein has several cofactor binding sites:

Mg²⁺
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:P0A817 (METK_ECOLI)
Note: Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate.
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:P31153 (METK2_HUMAN)
K⁺
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:P0A817 (METK_ECOLI)
Note: Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate.
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:P31153 (METK2_HUMAN)

Pathwayⁱ: S-adenosyl-L-methionine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes S-adenosyl-L-methionine from L-methionine.By similarity
Proteins known to be involved in this subpathway in this organism are:

S-adenosylmethionine synthase (Mat1a), Methionine adenosyltransferase 2 subunit beta (Mat2b), S-adenosylmethionine synthase (Mat1a), S-adenosylmethionine synthase isoform type-2 (Mat2a), S-adenosylmethionine synthase isoform type-1 (Mat1a), S-adenosylmethionine synthase (Mat2a), Methionine adenosyltransferase 2 subunit beta (Mat2b), S-adenosylmethionine synthase (Mat2a)

This subpathway is part of the pathway S-adenosyl-L-methionine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes S-adenosyl-L-methionine from L-methionine, the pathway S-adenosyl-L-methionine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	29	ATPBy similarity	1
Metal bindingⁱ	31	MagnesiumBy similarity	1
Metal bindingⁱ	57	PotassiumBy similarity	1
Binding siteⁱ	70	MethionineBy similarity	1
Binding siteⁱ	113	MethionineBy similarity	1
Binding siteⁱ	258	ATP; shared with neighboring subunitBy similarity	1
Binding siteⁱ	258	Methionine; shared with neighboring subunitBy similarity	1
Binding siteⁱ	281	ATP; via amide nitrogen; shared with neighboring subunitBy similarity	1
Binding siteⁱ	285	ATP; shared with neighboring subunitBy similarity	1
Binding siteⁱ	289	MethionineBy similarity	1
Binding siteⁱ	291	ATP; shared with neighboring subunitBy similarity	1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	179 – 181	ATPBy similarity	3
Nucleotide bindingⁱ	247 – 250	ATPBy similarity	4
Nucleotide bindingⁱ	264 – 265	ATPBy similarity	2

GO - Molecular functionⁱ

amino acid binding
Source: RGD
Inferred from direct assayⁱ
- 12029623
ATP binding
Source: RGD
Inferred from direct assayⁱ
- 12029623
metal ion binding Source: UniProtKB-KW
methionine adenosyltransferase activity
Source: RGD
Inferred from direct assayⁱ
- 10898761
- 12029623

Complete GO annotation...

GO - Biological processⁱ

circadian rhythm
Source: RGD
Inferred from direct assayⁱ
- 15504733
one-carbon metabolic process Source: UniProtKB-KW
protein heterooligomerization Source: UniProtKB
protein hexamerization Source: UniProtKB
response to cAMP
Source: RGD
Inferred from direct assayⁱ
- 15504733
response to drug
Source: RGD
Inferred from direct assayⁱ
- 15504733
response to hormone
Source: RGD
Inferred from direct assayⁱ
- 15504733
response to light stimulus
Source: RGD
Inferred from expression patternⁱ
- 15504733
S-adenosylmethionine biosynthetic process
Source: RGD
Inferred from direct assayⁱ
- 10898761
- 12029623

Complete GO annotation...

Keywordsⁱ

Molecular function	Transferase
Biological process	One-carbon metabolism
Ligand	ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BRENDAⁱ	2.5.1.6. 5301.
SABIO-RKⁱ	P18298.
UniPathwayⁱ	UPA00315; UER00080.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: S-adenosylmethionine synthase isoform type-2 (EC:2.5.1.6By similarity) Short name: AdoMet synthase 2 Alternative name(s): Methionine adenosyltransferase 2 Short name: MAT 2 Methionine adenosyltransferase II Short name: MAT-II
Gene namesⁱ	Name:Mat2a Synonyms:Ams2
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Unplaced

Organism-specific databases

Rat genome database More...RGDⁱ	619985. Mat2a.

RGDⁱ

619985. Mat2a.

Subcellular locationⁱ

GO - Cellular componentⁱ

cytosol
Source: RGD
Inferred from direct assayⁱ
- 10898761
methionine adenosyltransferase complex Source: UniProtKB

Complete GO annotation...

Pathology & Biotechⁱ

Chemistry databases

ChEMBLⁱ	CHEMBL2838.

ChEMBLⁱ

CHEMBL2838.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000174439	1 – 395	S-adenosylmethionine synthase isoform type-2Add BLAST		395

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	81	N6-acetyllysineBy similarity	1
Modified residueⁱ	114	PhosphoserineBy similarity	1
Cross-linkⁱ	228	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linkⁱ	234	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residueⁱ	384	PhosphoserineBy similarity	1

Keywords - PTMⁱ

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbⁱ	P18298.
PRIDEⁱ	P18298.

PTM databases

iPTMnetⁱ	P18298.
PhosphoSitePlusⁱ	P18298.

Expressionⁱ

Tissue specificityⁱ

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.2 Publications

Inductionⁱ

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.2 Publications

Interactionⁱ

Subunit structureⁱ

Heterotrimer; composed of a catalytic MAT2A homodimer that binds one regulatory MAT2B chain. Heterohexamer; composed of a central, catalytic MAT2A homotetramer flanked on either side by a regulatory MAT2B chain.By similarity

Protein-protein interaction databases

BioGridⁱ	251193. 1 interactor.
STRINGⁱ	10116.ENSRNOP00000018170.

Chemistry databases

BindingDBⁱ

P18298.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P18298.
SMRⁱ	P18298.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	113 – 125	Flexible loopBy similarityAdd BLAST		13

Sequence similaritiesⁱ

Belongs to the AdoMet synthase family.Curated

Phylogenomic databases

eggNOGⁱ	KOG1506. Eukaryota. COG0192. LUCA.
HOGENOMⁱ	HOG000245710.
HOVERGENⁱ	HBG001562.
InParanoidⁱ	P18298.
KEGG Orthology (KO) More...KOⁱ	K00789.
PhylomeDBⁱ	P18298.

Family and domain databases

HAMAPⁱ	MF_00086. S_AdoMet_synth1. 1 hit.
InterProⁱ	View protein in 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.
PANTHERⁱ	PTHR11964. PTHR11964. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02773. S-AdoMet_synt_C. 1 hit. PF02772. S-AdoMet_synt_M. 1 hit. PF00438. S-AdoMet_synt_N. 1 hit.
PIRSFⁱ	PIRSF000497. MAT. 1 hit.
SUPFAMⁱ	SSF55973. SSF55973. 3 hits.
TIGRFAMsⁱ	TIGR01034. metK. 1 hit.
PROSITEⁱ	View protein in PROSITE PS00376. ADOMET_SYNTHASE_1. 1 hit. PS00377. ADOMET_SYNTHASE_2. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

P18298-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MNGQLNGFHE AFIEEGTFLF TSESVGEGHP DKICDQINDA VLDAHLQQDP 
        60         70         80         90        100
DAKVACETVA KTGMILLAGE ITSRAAIDYQ KVVREAIKHI GYDDSSKGFD 
       110        120        130        140        150
YKTCNVLVAL EQQSPDIAQG VHLDRNEEDI GAGDQGLMFG YATDETEECM 
       160        170        180        190        200
PLTIVLAHKL NAKLAELRRN GTLPWLRPDS KTQVTVQYMQ DRGAVIPIRV 
       210        220        230        240        250
HTIVISVQHD EEVCLDEMRD ALKEKLIKAV VPAKYLDEDT IYHLQPSGRF 
       260        270        280        290        300
VIGGPQGDAG LTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW 
       310        320        330        340        350
VAKSLVKGGL CRRVLVQVSY AIGVSHPLSI SIFHYGTSQK SERELLEIVK 
       360        370        380        390 
NNFDLRPGVI VRDLDLKKPI YQRTAAYGHF GRDSFPWEVP KKLKY

Length:395

Mass (Da):43,716

Last modified:November 1, 1990 - v1

Checksum:ⁱ4DA9AFABF7D09C79

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J05571 mRNA. Translation: AAA42106.1. AB000717 Genomic DNA. Translation: BAA19170.1.
PIRⁱ	A37118.
NCBI Reference Sequences More...RefSeqⁱ	NP_599178.1. NM_134351.1.
UniGeneⁱ	Rn.144658. Rn.41420.

Genome annotation databases

GeneIDⁱ	171347.
KEGGⁱ	rno:171347.
UCSC genome browser More...UCSCⁱ	RGD:619985. rat.

Similar proteinsⁱ

Entry	Cluster members	Organisms	Length	Cluster ID	Cluster name	Size
P18298	P31153 Q4R924 Q5R5H1 A0A140VJP5 H9FUH5 H2QI93 F7F996 G3QQH2 A0A0D9RUF1 A0A096NZT8 +29	Homo sapiens (Human) Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) Macaca mulatta (Rhesus macaque) Pan troglodytes (Chimpanzee) Callithrix jacchus (White-tufted-ear marmoset) Gorilla gorilla gorilla (Western lowland gorilla) Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus) Papio anubis (Olive baboon) Mus musculus (Mouse) And more	395	UniRef90_P31153	Cluster: S-adenosylmethionine synthase isoform type-2	40

Entry	Cluster members	Organisms	Length	Cluster ID	Cluster name	Size
P18298	P23686 A0A178WES1 A0A199V9N7 UPI0009818F1D M0TE03 Q9FPL6 M1HIR3 A0A0K9P096 I1HF17 UPI0004E54C62 +2097	Arabidopsis thaliana (Mouse-ear cress) Ananas comosus (Pineapple) (Ananas ananas) Musa acuminata subsp. malaccensis (Wild banana) (Musa malaccensis) Suaeda salsa (Seepweed) (Chenopodium salsum) Senecio scandens Zostera marina (Eelgrass) Brachypodium distachyon (Purple false brome) (Trachynia distachya) Phoenix dactylifera (Date palm) Pyrus x bretschneideri (Chinese white pear) Hordeum vulgare (Barley) And more	393	UniRef50_P23686	Cluster: S-adenosylmethionine synthase 1	2,108

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J05571 mRNA. Translation: AAA42106.1. AB000717 Genomic DNA. Translation: BAA19170.1.
PIRⁱ	A37118.
NCBI Reference Sequences More...RefSeqⁱ	NP_599178.1. NM_134351.1.
UniGeneⁱ	Rn.144658. Rn.41420.

3D structure databases

ProteinModelPortalⁱ	P18298.
SMRⁱ	P18298.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	251193. 1 interactor.
STRINGⁱ	10116.ENSRNOP00000018170.

Chemistry databases

BindingDBⁱ	P18298.
ChEMBLⁱ	CHEMBL2838.

PTM databases

iPTMnetⁱ	P18298.
PhosphoSitePlusⁱ	P18298.

Proteomic databases

PaxDbⁱ	P18298.
PRIDEⁱ	P18298.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	171347.
KEGGⁱ	rno:171347.
UCSC genome browser More...UCSCⁱ	RGD:619985. rat.

Organism-specific databases

CTDⁱ	4144.
Rat genome database More...RGDⁱ	619985. Mat2a.

Phylogenomic databases

eggNOGⁱ	KOG1506. Eukaryota. COG0192. LUCA.
HOGENOMⁱ	HOG000245710.
HOVERGENⁱ	HBG001562.
InParanoidⁱ	P18298.
KEGG Orthology (KO) More...KOⁱ	K00789.
PhylomeDBⁱ	P18298.

Enzyme and pathway databases

UniPathwayⁱ	UPA00315; UER00080.
BRENDAⁱ	2.5.1.6. 5301.
SABIO-RKⁱ	P18298.

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P18298.

PROⁱ

PR:P18298.

Family and domain databases

HAMAPⁱ	MF_00086. S_AdoMet_synth1. 1 hit.
InterProⁱ	View protein in 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.
PANTHERⁱ	PTHR11964. PTHR11964. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02773. S-AdoMet_synt_C. 1 hit. PF02772. S-AdoMet_synt_M. 1 hit. PF00438. S-AdoMet_synt_N. 1 hit.
PIRSFⁱ	PIRSF000497. MAT. 1 hit.
SUPFAMⁱ	SSF55973. SSF55973. 3 hits.
TIGRFAMsⁱ	TIGR01034. metK. 1 hit.
PROSITEⁱ	View protein in PROSITE PS00376. ADOMET_SYNTHASE_1. 1 hit. PS00377. ADOMET_SYNTHASE_2. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	METK2_RAT
Accessionⁱ	P18298Primary (citable) accession number: P18298
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
	Last sequence update:	November 1, 1990
	Last modified:	August 30, 2017
	This is version 146 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

UniProtKB

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UniProtKB - P18298 (METK2_RAT)

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S-adenosylmethionine synthase isoform type-2

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: S-adenosyl-L-methionine biosynthesis

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

Pathwayⁱ: S-adenosyl-L-methionine biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ