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UniProtKB - P18298 (METK2_RAT)

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Protein

S-adenosylmethionine synthase isoform type-2

Gene

Mat2a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

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:
  1. 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), 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 keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei29ATPBy similarity1
Metal bindingi31MagnesiumBy similarity1
Metal bindingi57PotassiumBy similarity1
Binding sitei70MethionineBy similarity1
Binding sitei113MethionineBy similarity1
Binding sitei258ATP; shared with neighboring subunitBy similarity1
Binding sitei258Methionine; shared with neighboring subunitBy similarity1
Binding sitei281ATP; via amide nitrogen; shared with neighboring subunitBy similarity1
Binding sitei285ATP; shared with neighboring subunitBy similarity1
Binding sitei289MethionineBy similarity1
Binding sitei291ATP; shared with neighboring subunitBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi179 – 181ATPBy similarity3
Nucleotide bindingi247 – 250ATPBy similarity4
Nucleotide bindingi264 – 265ATPBy similarity2

GO - Molecular functioni

  • amino acid binding Source: RGD
  • ATP binding Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • methionine adenosyltransferase activity Source: RGD
Complete GO annotation...

GO - Biological processi

  • 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
Complete GO annotation...

Keywordsi

Molecular functionTransferase
Biological processOne-carbon metabolism
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BRENDAi2.5.1.6. 5301.
SABIO-RKiP18298.
UniPathwayiUPA00315; 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619985. Mat2a.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • methionine adenosyltransferase complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2838.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001744391 – 395S-adenosylmethionine synthase isoform type-2Add BLAST395

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei81N6-acetyllysineBy similarity1
Modified residuei114PhosphoserineBy similarity1
Modified residuei384PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP18298.
PRIDEiP18298.

PTM databases

iPTMnetiP18298.
PhosphoSitePlusiP18298.

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

BioGridi251193. 1 interactor.
STRINGi10116.ENSRNOP00000018170.

Chemistry databases

BindingDBiP18298.

Structurei

3D structure databases

ProteinModelPortaliP18298.
SMRiP18298.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni113 – 125Flexible loopBy similarityAdd BLAST13

Sequence similaritiesi

Belongs to the AdoMet synthase family.Curated

Phylogenomic databases

eggNOGiKOG1506. Eukaryota.
COG0192. LUCA.
HOGENOMiHOG000245710.
HOVERGENiHBG001562.
InParanoidiP18298.
KOiK00789.
PhylomeDBiP18298.

Family and domain databases

HAMAPiMF_00086. S_AdoMet_synth1. 1 hit.
InterProiView 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.
PANTHERiPTHR11964. PTHR11964. 1 hit.
PfamiView protein in Pfam
PF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
PIRSFiPIRSF000497. MAT. 1 hit.
SUPFAMiSSF55973. SSF55973. 3 hits.
TIGRFAMsiTIGR01034. metK. 1 hit.
PROSITEiView protein in PROSITE
PS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.

Sequencei

Sequence statusi: Complete.

P18298-1 [UniParc]FASTAAdd 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.
PIRiA37118.
RefSeqiNP_599178.1. NM_134351.1.
UniGeneiRn.144658.
Rn.41420.

Genome annotation databases

GeneIDi171347.
KEGGirno:171347.
UCSCiRGD:619985. rat.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiMETK2_RAT
AccessioniPrimary (citable) accession number: P18298
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: May 10, 2017
This is version 145 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families