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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.

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarity, Co2+By similarityNote: Binds 2 divalent ions per subunit. Magnesium or cobalt.By similarity
  • K+By similarityNote: Binds 1 potassium ion per subunit.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.
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)
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi31 – 311MagnesiumBy similarity
Metal bindingi57 – 571PotassiumBy similarity
Binding sitei159 – 1591ATPSequence analysis
Metal bindingi283 – 2831PotassiumBy similarity
Metal bindingi291 – 2911MagnesiumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi131 – 1366ATPSequence analysis

GO - Molecular functioni

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

GO - Biological processi

  • circadian rhythm Source: RGD
  • one-carbon metabolic process Source: UniProtKB-KW
  • 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...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

ATP-binding, Cobalt, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BRENDAi2.5.1.6. 5301.
SABIO-RKP18298.
UniPathwayiUPA00315; UER00080.

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine synthase isoform type-2 (EC:2.5.1.6)
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619985. Mat2a.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2111450.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 395395S-adenosylmethionine synthase isoform type-2PRO_0000174439Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei81 – 811N6-acetyllysineBy similarity
Modified residuei114 – 1141PhosphoserineBy similarity

Post-translational modificationi

The alpha' subunit is a post-translationally modified version of MAT2A.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP18298.
PRIDEiP18298.

PTM databases

iPTMnetiP18298.

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

Heterotetramer composed of 2 catalytic alpha subunits (alpha and alpha') (MAT2A) and 1 copy of beta subunit (MAT2B).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018170.

Chemistry

BindingDBiP18298.

Structurei

3D structure databases

ProteinModelPortaliP18298.
SMRiP18298. Positions 16-395.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

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.
InterProiIPR022631. 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]
PANTHERiPTHR11964. PTHR11964. 1 hit.
PfamiPF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000497. MAT. 1 hit.
SUPFAMiSSF55973. SSF55973. 3 hits.
TIGRFAMsiTIGR01034. metK. 1 hit.
PROSITEiPS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP18298.
SMRiP18298. Positions 16-395.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018170.

Chemistry

BindingDBiP18298.
ChEMBLiCHEMBL2111450.

PTM databases

iPTMnetiP18298.

Proteomic databases

PaxDbiP18298.
PRIDEiP18298.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4144.
RGDi619985. Mat2a.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00315; UER00080.
BRENDAi2.5.1.6. 5301.
SABIO-RKP18298.

Miscellaneous databases

NextBioi622114.
PROiP18298.

Family and domain databases

HAMAPiMF_00086. S_AdoMet_synth1.
InterProiIPR022631. 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]
PANTHERiPTHR11964. PTHR11964. 1 hit.
PfamiPF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000497. MAT. 1 hit.
SUPFAMiSSF55973. SSF55973. 3 hits.
TIGRFAMsiTIGR01034. metK. 1 hit.
PROSITEiPS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION.
  4. Cited for: TISSUE SPECIFICITY, INDUCTION.

Entry informationi

Entry nameiMETK2_RAT
AccessioniPrimary (citable) accession number: P18298
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: May 11, 2016
This is version 137 of the entry and version 1 of the sequence. [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

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.