Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

S-adenosylmethionine synthase isoform type-1

Gene

Mat1a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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.1 Publication

Catalytic activityi

ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine.1 Publication

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.1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. S-adenosylmethionine synthase (Mat2a), S-adenosylmethionine synthase isoform type-2 (Mat2a), S-adenosylmethionine synthase (Mat2a), S-adenosylmethionine synthase (Mat2a), Methionine adenosyltransferase 2 subunit beta (Mat2b), S-adenosylmethionine synthase isoform type-1 (Mat1a), S-adenosylmethionine synthase (Mat2a), S-adenosylmethionine synthase (Mat2a), S-adenosylmethionine synthase (Mat2a), 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
Metal bindingi24MagnesiumBy similarity1
Binding sitei30ATPBy similarity1
Metal bindingi58PotassiumBy similarity1
Binding sitei71MethionineBy similarity1
Binding sitei114MethionineBy similarity1
Binding sitei259ATPBy similarity1
Binding sitei259Methionine; shared with neighboring subunitBy similarity1
Binding sitei282ATP; via amide nitrogen; shared with neighboring subunitBy similarity1
Binding sitei286ATP; shared with neighboring subunitBy similarity1
Binding sitei290ATP; shared with neighboring subunitBy similarity1
Binding sitei290MethionineBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi180 – 182ATPBy similarity3
Nucleotide bindingi248 – 251ATPBy similarity4
Nucleotide bindingi265 – 266ATPBy similarity2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiR-MMU-156581. Methylation.
R-MMU-1614635. Sulfur amino acid metabolism.
R-MMU-2408508. Metabolism of ingested SeMet, Sec, MeSec into H2Se.
UniPathwayiUPA00315; UER00080.

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine synthase isoform type-1 (EC:2.5.1.61 Publication)
Short name:
AdoMet synthase 1
Alternative name(s):
Methionine adenosyltransferase 1
Short name:
MAT 1
Gene namesi
Name:Mat1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:88017. Mat1a.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001744331 – 396S-adenosylmethionine synthase isoform type-1Add BLAST396

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi35 ↔ 61By similarity
Modified residuei121S-nitrosocysteineBy similarity1

Post-translational modificationi

S-nitrosylation of Cys-121 inactivates the enzyme.By similarity
An intrachain disulfide bond can be formed. The protein structure shows that the relevant Cys residues are in a position that would permit formation of a disulfide bond.By similarity

Keywords - PTMi

Disulfide bond, S-nitrosylation

Proteomic databases

MaxQBiQ91X83.
PaxDbiQ91X83.
PeptideAtlasiQ91X83.
PRIDEiQ91X83.

2D gel databases

REPRODUCTION-2DPAGEQ91X83.

PTM databases

iPTMnetiQ91X83.
PhosphoSitePlusiQ91X83.
SwissPalmiQ91X83.

Expressioni

Gene expression databases

BgeeiENSMUSG00000037798.
CleanExiMM_MAT1A.
GenevisibleiQ91X83. MM.

Interactioni

Subunit structurei

Homotetramer (MAT-I); dimer of dimers. Homodimer (MAT-III).By similarity

Protein-protein interaction databases

DIPiDIP-45874N.
IntActiQ91X83. 3 interactors.
MINTiMINT-1855350.
STRINGi10090.ENSMUSP00000044288.

Structurei

3D structure databases

ProteinModelPortaliQ91X83.
SMRiQ91X83.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni114 – 126Flexible loopBy similarityAdd BLAST13

Sequence similaritiesi

Belongs to the AdoMet synthase family.Curated

Phylogenomic databases

eggNOGiKOG1506. Eukaryota.
COG0192. LUCA.
GeneTreeiENSGT00500000044811.
HOGENOMiHOG000245710.
HOVERGENiHBG001562.
InParanoidiQ91X83.
KOiK00789.
OMAiIQDNGAV.
OrthoDBiEOG091G08Z2.
PhylomeDBiQ91X83.
TreeFamiTF300511.

Family and domain databases

HAMAPiMF_00086. S_AdoMet_synth1. 1 hit.
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.

Q91X83-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGPVDGLCD HSLSEEGAFM FTSESVGEGH PDKICDQISD AVLDAHLKQD
60 70 80 90 100
PNAKVACETV CKTGMVLLCG EITSVAMVDY QRVVRDTIKH IGYDDSAKGF
110 120 130 140 150
DFKTCNVLVA LEQQSPDIAQ CVHLDRNEED VGAGDQGLMF GYATDETEEC
160 170 180 190 200
MPLTIVLAHK LNTRIADLRR SGVLPWLRPD SKTQVTVQYM QDNGAVIPVR
210 220 230 240 250
IHTIVISVQH NEDITLEAMQ EALKEQVIKA VVPAKYLDED TVYHLQPSGR
260 270 280 290 300
FVIGGPQGDA GVTGRKIIVD TYGGWGAHGG GAFSGKDYTK VDRSAAYAAR
310 320 330 340 350
WVAKSLVKAG LCRRVLVQVS YAIGVAEPLS ISIFTYGTSN KTERELLEVV
360 370 380 390
NKNFDLRPGV IVRDLDLKKP IYQKTACYGH FGRSEFPWEV PKKLVF
Length:396
Mass (Da):43,509
Last modified:December 1, 2001 - v1
Checksum:iAAA593A669551EB8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK149542 mRNA. Translation: BAE28947.1.
AK153832 mRNA. Translation: BAE32202.1.
BC011211 mRNA. Translation: AAH11211.1.
CCDSiCCDS26959.1.
PIRiA47151.
RefSeqiNP_598414.1. NM_133653.3.
XP_006518513.1. XM_006518450.2.
UniGeneiMm.14064.
Mm.486779.

Genome annotation databases

EnsembliENSMUST00000047286; ENSMUSP00000044288; ENSMUSG00000037798.
GeneIDi11720.
KEGGimmu:11720.
UCSCiuc007tcm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK149542 mRNA. Translation: BAE28947.1.
AK153832 mRNA. Translation: BAE32202.1.
BC011211 mRNA. Translation: AAH11211.1.
CCDSiCCDS26959.1.
PIRiA47151.
RefSeqiNP_598414.1. NM_133653.3.
XP_006518513.1. XM_006518450.2.
UniGeneiMm.14064.
Mm.486779.

3D structure databases

ProteinModelPortaliQ91X83.
SMRiQ91X83.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-45874N.
IntActiQ91X83. 3 interactors.
MINTiMINT-1855350.
STRINGi10090.ENSMUSP00000044288.

PTM databases

iPTMnetiQ91X83.
PhosphoSitePlusiQ91X83.
SwissPalmiQ91X83.

2D gel databases

REPRODUCTION-2DPAGEQ91X83.

Proteomic databases

MaxQBiQ91X83.
PaxDbiQ91X83.
PeptideAtlasiQ91X83.
PRIDEiQ91X83.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000047286; ENSMUSP00000044288; ENSMUSG00000037798.
GeneIDi11720.
KEGGimmu:11720.
UCSCiuc007tcm.2. mouse.

Organism-specific databases

CTDi4143.
MGIiMGI:88017. Mat1a.

Phylogenomic databases

eggNOGiKOG1506. Eukaryota.
COG0192. LUCA.
GeneTreeiENSGT00500000044811.
HOGENOMiHOG000245710.
HOVERGENiHBG001562.
InParanoidiQ91X83.
KOiK00789.
OMAiIQDNGAV.
OrthoDBiEOG091G08Z2.
PhylomeDBiQ91X83.
TreeFamiTF300511.

Enzyme and pathway databases

UniPathwayiUPA00315; UER00080.
ReactomeiR-MMU-156581. Methylation.
R-MMU-1614635. Sulfur amino acid metabolism.
R-MMU-2408508. Metabolism of ingested SeMet, Sec, MeSec into H2Se.

Miscellaneous databases

PROiQ91X83.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000037798.
CleanExiMM_MAT1A.
GenevisibleiQ91X83. MM.

Family and domain databases

HAMAPiMF_00086. S_AdoMet_synth1. 1 hit.
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...

Entry informationi

Entry nameiMETK1_MOUSE
AccessioniPrimary (citable) accession number: Q91X83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: December 1, 2001
Last modified: November 30, 2016
This is version 128 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.