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Protein

S-adenosylmethionine synthase isoform type-2

Gene

MAT2A

Organism
Homo sapiens (Human)
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.3 Publications

Catalytic activityi

ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine.3 Publications

Cofactori

Protein has several cofactor binding sites:

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.3 Publications
Proteins known to be involved in this subpathway in this organism are:
  1. Methionine adenosyltransferase 2 subunit beta (MAT2B), S-adenosylmethionine synthase isoform type-1 (MAT1A), S-adenosylmethionine synthase, S-adenosylmethionine synthase, S-adenosylmethionine synthase isoform type-2 (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 sitei29ATPCombined sources2 Publications1
Metal bindingi31MagnesiumCombined sources2 Publications1
Metal bindingi57PotassiumBy similarity1
Binding sitei70MethionineCombined sources1 Publication1
Binding sitei113Methionine1 Publication1
Binding sitei258ATPCombined sources2 Publications1
Binding sitei258Methionine; shared with neighboring subunitCombined sources2 Publications1
Binding sitei281ATP; via amide nitrogen; shared with neighboring subunitCombined sources1 Publication1
Binding sitei285ATP; shared with neighboring subunitCombined sources2 Publications1
Binding sitei289MethionineBy similarity1
Binding sitei291ATP; shared with neighboring subunitCombined sources2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi179 – 181ATPCombined sources2 Publications3
Nucleotide bindingi247 – 250ATPCombined sources2 Publications4
Nucleotide bindingi264 – 265ATPCombined sources2 Publications2

GO - Molecular functioni

GO - Biological processi

  • methylation Source: Reactome
  • one-carbon metabolic process Source: UniProtKB-KW
  • protein heterooligomerization Source: UniProtKB
  • protein hexamerization Source: UniProtKB
  • S-adenosylmethionine biosynthetic process Source: UniProtKB
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

BioCyciZFISH:HS09847-MONOMER.
BRENDAi2.5.1.6. 2681.
ReactomeiR-HSA-156581. Methylation.
UniPathwayiUPA00315; UER00080.

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine synthase isoform type-2 (EC:2.5.1.63 Publications)
Short name:
AdoMet synthase 2
Alternative name(s):
Methionine adenosyltransferase 2
Short name:
MAT 21 Publication
Methionine adenosyltransferase II
Short name:
MAT-II
Gene namesi
Name:MAT2A
Synonyms:AMS2, MATA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:6904. MAT2A.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

DisGeNETi4144.
OpenTargetsiENSG00000168906.
PharmGKBiPA30647.

Chemistry databases

ChEMBLiCHEMBL3313835.
DrugBankiDB00134. L-Methionine.
DB00118. S-Adenosylmethionine.

Polymorphism and mutation databases

BioMutaiMAT2A.
DMDMi400245.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001744351 – 395S-adenosylmethionine synthase isoform type-2Add BLAST395

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei81N6-acetyllysineCombined sources1
Modified residuei114PhosphoserineCombined sources1
Modified residuei384PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP31153.
MaxQBiP31153.
PaxDbiP31153.
PeptideAtlasiP31153.
PRIDEiP31153.

2D gel databases

REPRODUCTION-2DPAGEIPI00010157.

PTM databases

iPTMnetiP31153.
PhosphoSitePlusiP31153.
SwissPalmiP31153.

Expressioni

Tissue specificityi

Detected in kidney.1 Publication

Gene expression databases

BgeeiENSG00000168906.
CleanExiHS_MAT2A.
ExpressionAtlasiP31153. baseline and differential.
GenevisibleiP31153. HS.

Organism-specific databases

HPAiCAB009968.
HPA043028.

Interactioni

Subunit structurei

Heterotrimer; composed of a catalytic MAT2A homodimer that binds one regulatory MAT2B chain (PubMed:10644686, PubMed:23189196). Heterohexamer; composed of a central, catalytic MAT2A homotetramer flanked on either side by a regulatory MAT2B chain (PubMed:25075345).1 Publication2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1050743,EBI-1050743
MAT1AQ002664EBI-1050743,EBI-967087
MAT2BQ9NZL93EBI-1050743,EBI-10317491

Protein-protein interaction databases

BioGridi110314. 40 interactors.
IntActiP31153. 25 interactors.
STRINGi9606.ENSP00000303147.

Structurei

Secondary structure

1395
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi17 – 25Combined sources9
Helixi30 – 48Combined sources19
Beta strandi53 – 61Combined sources9
Beta strandi64 – 72Combined sources9
Helixi79 – 90Combined sources12
Helixi95 – 97Combined sources3
Turni101 – 103Combined sources3
Beta strandi104 – 111Combined sources8
Helixi115 – 121Combined sources7
Turni122 – 124Combined sources3
Helixi127 – 129Combined sources3
Beta strandi132 – 134Combined sources3
Beta strandi136 – 143Combined sources8
Helixi152 – 169Combined sources18
Beta strandi171 – 173Combined sources3
Beta strandi176 – 191Combined sources16
Beta strandi194 – 209Combined sources16
Beta strandi211 – 213Combined sources3
Helixi215 – 225Combined sources11
Helixi227 – 230Combined sources4
Helixi233 – 235Combined sources3
Beta strandi241 – 245Combined sources5
Helixi254 – 256Combined sources3
Turni266 – 273Combined sources8
Helixi290 – 307Combined sources18
Beta strandi312 – 320Combined sources9
Beta strandi328 – 333Combined sources6
Helixi342 – 352Combined sources11
Helixi357 – 363Combined sources7
Turni364 – 367Combined sources4
Helixi371 – 374Combined sources4
Beta strandi375 – 377Combined sources3
Beta strandi379 – 382Combined sources4
Helixi386 – 388Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2P02X-ray1.21A1-395[»]
4KTTX-ray2.59A/B/C/D1-395[»]
4KTVX-ray3.30A/B/C/D1-395[»]
4NDNX-ray2.34A/B/C/D1-395[»]
5A19X-ray2.34A1-395[»]
5A1GX-ray1.83A1-395[»]
5A1IX-ray1.09A1-395[»]
ProteinModelPortaliP31153.
SMRiP31153.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31153.

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.
GeneTreeiENSGT00500000044811.
HOGENOMiHOG000245710.
HOVERGENiHBG001562.
InParanoidiP31153.
KOiK00789.
OMAiKTIWHIN.
OrthoDBiEOG091G08Z2.
PhylomeDBiP31153.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P31153-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNGQLNGFHE AFIEEGTFLF TSESVGEGHP DKICDQISDA VLDAHLQQDP
60 70 80 90 100
DAKVACETVA KTGMILLAGE ITSRAAVDYQ KVVREAVKHI GYDDSSKGFD
110 120 130 140 150
YKTCNVLVAL EQQSPDIAQG VHLDRNEEDI GAGDQGLMFG YATDETEECM
160 170 180 190 200
PLTIVLAHKL NAKLAELRRN GTLPWLRPDS KTQVTVQYMQ DRGAVLPIRV
210 220 230 240 250
HTIVISVQHD EEVCLDEMRD ALKEKVIKAV 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
KNFDLRPGVI VRDLDLKKPI YQRTAAYGHF GRDSFPWEVP KKLKY
Length:395
Mass (Da):43,661
Last modified:July 1, 1993 - v1
Checksum:i2E7D1B91CC4F7BDD
GO
Isoform 2 (identifier: P31153-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-63: Missing.
     363-395: Missing.

Note: No experimental confirmation available.
Show »
Length:299
Mass (Da):32,965
Checksum:i3E3903C0EFD85F00
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0561861 – 63Missing in isoform 2. 1 PublicationAdd BLAST63
Alternative sequenceiVSP_056187363 – 395Missing in isoform 2. 1 PublicationAdd BLAST33

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68836 mRNA. Translation: CAA48726.1.
DQ083239 mRNA. Translation: AAY85355.1.
AK291126 mRNA. Translation: BAF83815.1.
AK297758 mRNA. Translation: BAG60107.1.
AK316411 mRNA. Translation: BAH14782.1.
AC016753 Genomic DNA. Translation: AAY24339.1.
CH471053 Genomic DNA. Translation: EAW99511.1.
CH471053 Genomic DNA. Translation: EAW99513.1.
BC001686 mRNA. Translation: AAH01686.1.
BC001854 mRNA. Translation: AAH01854.1.
CCDSiCCDS1977.1. [P31153-1]
PIRiS27257.
RefSeqiNP_005902.1. NM_005911.5. [P31153-1]
UniGeneiHs.516157.

Genome annotation databases

EnsembliENST00000306434; ENSP00000303147; ENSG00000168906. [P31153-1]
ENST00000409017; ENSP00000386353; ENSG00000168906. [P31153-2]
GeneIDi4144.
KEGGihsa:4144.
UCSCiuc002spr.4. human. [P31153-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X68836 mRNA. Translation: CAA48726.1.
DQ083239 mRNA. Translation: AAY85355.1.
AK291126 mRNA. Translation: BAF83815.1.
AK297758 mRNA. Translation: BAG60107.1.
AK316411 mRNA. Translation: BAH14782.1.
AC016753 Genomic DNA. Translation: AAY24339.1.
CH471053 Genomic DNA. Translation: EAW99511.1.
CH471053 Genomic DNA. Translation: EAW99513.1.
BC001686 mRNA. Translation: AAH01686.1.
BC001854 mRNA. Translation: AAH01854.1.
CCDSiCCDS1977.1. [P31153-1]
PIRiS27257.
RefSeqiNP_005902.1. NM_005911.5. [P31153-1]
UniGeneiHs.516157.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2P02X-ray1.21A1-395[»]
4KTTX-ray2.59A/B/C/D1-395[»]
4KTVX-ray3.30A/B/C/D1-395[»]
4NDNX-ray2.34A/B/C/D1-395[»]
5A19X-ray2.34A1-395[»]
5A1GX-ray1.83A1-395[»]
5A1IX-ray1.09A1-395[»]
ProteinModelPortaliP31153.
SMRiP31153.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110314. 40 interactors.
IntActiP31153. 25 interactors.
STRINGi9606.ENSP00000303147.

Chemistry databases

ChEMBLiCHEMBL3313835.
DrugBankiDB00134. L-Methionine.
DB00118. S-Adenosylmethionine.

PTM databases

iPTMnetiP31153.
PhosphoSitePlusiP31153.
SwissPalmiP31153.

Polymorphism and mutation databases

BioMutaiMAT2A.
DMDMi400245.

2D gel databases

REPRODUCTION-2DPAGEIPI00010157.

Proteomic databases

EPDiP31153.
MaxQBiP31153.
PaxDbiP31153.
PeptideAtlasiP31153.
PRIDEiP31153.

Protocols and materials databases

DNASUi4144.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000306434; ENSP00000303147; ENSG00000168906. [P31153-1]
ENST00000409017; ENSP00000386353; ENSG00000168906. [P31153-2]
GeneIDi4144.
KEGGihsa:4144.
UCSCiuc002spr.4. human. [P31153-1]

Organism-specific databases

CTDi4144.
DisGeNETi4144.
GeneCardsiMAT2A.
H-InvDBHIX0117562.
HGNCiHGNC:6904. MAT2A.
HPAiCAB009968.
HPA043028.
MIMi601468. gene.
neXtProtiNX_P31153.
OpenTargetsiENSG00000168906.
PharmGKBiPA30647.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1506. Eukaryota.
COG0192. LUCA.
GeneTreeiENSGT00500000044811.
HOGENOMiHOG000245710.
HOVERGENiHBG001562.
InParanoidiP31153.
KOiK00789.
OMAiKTIWHIN.
OrthoDBiEOG091G08Z2.
PhylomeDBiP31153.
TreeFamiTF300511.

Enzyme and pathway databases

UniPathwayiUPA00315; UER00080.
BioCyciZFISH:HS09847-MONOMER.
BRENDAi2.5.1.6. 2681.
ReactomeiR-HSA-156581. Methylation.

Miscellaneous databases

ChiTaRSiMAT2A. human.
EvolutionaryTraceiP31153.
GenomeRNAii4144.
PROiP31153.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000168906.
CleanExiHS_MAT2A.
ExpressionAtlasiP31153. baseline and differential.
GenevisibleiP31153. HS.

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 nameiMETK2_HUMAN
AccessioniPrimary (citable) accession number: P31153
Secondary accession number(s): A8K511
, B4DN45, D6W5L1, Q53SP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 30, 2016
This is version 176 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.