UniProtKB - P18298 (METK2_RAT)
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Protein
S-adenosylmethionine synthase isoform type-2
Gene
Mat2a
Organism
Rattus norvegicus (Rat)
Status
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 similarityNote: Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate.By similarity
- K+By similarityNote: Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate.By similarity
: S-adenosyl-L-methionine biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes S-adenosyl-L-methionine from L-methionine.By similarityProteins 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)
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 | Graphical view | 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 | Graphical view | 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
- ATP binding Source: RGD
- identical protein binding Source: RGD
- metal ion binding Source: UniProtKB-KW
- methionine adenosyltransferase activity Source: RGD
GO - Biological processi
- cellular response to leukemia inhibitory factor Source: RGD
- circadian rhythm Source: RGD
- one-carbon metabolic process Source: UniProtKB-KW
- protein heterooligomerization Source: UniProtKB
- protein hexamerization Source: UniProtKB
- response to cAMP Source: RGD
- response to drug Source: RGD
- response to hormone Source: RGD
- response to light stimulus Source: RGD
- S-adenosylmethionine biosynthetic process Source: RGD
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 | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 619985. Mat2a. |
Subcellular locationi
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 | Graphical view | 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 conjugationProteomic databases
PaxDbi | P18298. |
PRIDEi | P18298. |
PTM databases
CarbonylDBi | P18298. |
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
GO - Molecular functioni
- identical protein binding Source: RGD
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. |
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. |
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. |
i Sequence
Sequence statusi: Complete.
P18298-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J05571 mRNA. Translation: AAA42106.1. AB000717 Genomic DNA. Translation: BAA19170.1. |
PIRi | A37118. |
RefSeqi | NP_599178.1. NM_134351.1. |
UniGenei | Rn.144658. Rn.41420. |
Genome annotation databases
GeneIDi | 171347. |
KEGGi | rno:171347. |
UCSCi | RGD:619985. rat. |
Similar proteinsi
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: | February 28, 2018 | |
This is version 148 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |