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Protein

S-adenosylmethionine synthase isoform type-1

Gene

Mat1a

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.3 Publications

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Mg2+1 PublicationNote: Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate.1 Publication
  • K+1 PublicationNote: Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate.1 Publication

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. 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
Metal bindingi24MagnesiumCombined sources1
Binding sitei30ATPCombined sources1 Publication1
Metal bindingi58PotassiumBy similarity1
Binding sitei71MethionineBy similarity1
Binding sitei114MethionineBy similarity1
Binding sitei259ATPCombined sources1
Binding sitei259Methionine; shared with neighboring subunitBy similarity1
Binding sitei282ATP; via amide nitrogen; shared with neighboring subunitCombined sources1
Binding sitei286ATP; shared with neighboring subunitCombined sources1 Publication1
Binding sitei290ATP; shared with neighboring subunitCombined sources1 Publication1
Binding sitei290MethionineBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi180 – 182ATPCombined sources1 Publication3
Nucleotide bindingi248 – 251ATPCombined sources2 Publications4
Nucleotide bindingi265 – 266ATPCombined sources1 Publication2

GO - Molecular functioni

  • ADP binding Source: RGD
  • amino acid binding Source: RGD
  • ATP binding Source: RGD
  • magnesium ion binding Source: RGD
  • methionine adenosyltransferase activity Source: RGD
  • protein dimerization activity Source: RGD
  • protein homodimerization activity Source: RGD

GO - Biological processi

  • methionine catabolic process Source: UniProtKB
  • one-carbon metabolic process Source: UniProtKB-KW
  • protein homooligomerization Source: RGD
  • protein homotetramerization Source: RGD
  • protein tetramerization 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, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-8568.
BRENDAi2.5.1.6. 5301.
UniPathwayiUPA00315; UER00080.

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine synthase isoform type-1 (EC:2.5.1.63 Publications)
Short name:
AdoMet synthase 1
Alternative name(s):
Methionine adenosyltransferase 1
Short name:
MAT 1
Methionine adenosyltransferase I/III
Short name:
MAT-I/III
Gene namesi
Name:Mat1a
Synonyms:Ams1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3050. Mat1a.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • nuclear matrix Source: RGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi180D → G: Loss of S-adenosylmethionine synthase activity, but does not abolish polyphosphatase activity. 1 Publication1
Mutagenesisi182K → G: Loss of S-adenosylmethionine synthase activity, but does not abolish polyphosphatase activity. 1 Publication1
Mutagenesisi251F → D or G: Loss of S-adenosylmethionine synthase activity, but does not abolish polyphosphatase activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL2195.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001744341 – 397S-adenosylmethionine synthase isoform type-1Add BLAST397

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi35 ↔ 611 Publication1 Publication
Modified residuei121S-nitrosocysteine1 Publication1

Post-translational modificationi

S-nitrosylation of Cys-121 inactivates the enzyme.2 Publications
An intrachain disulfide bond can be formed (PubMed:10601859). The protein structure shows that the relevant Cys residues are in a position that would permit formation of a disulfide bond (PubMed:10873471).2 Publications

Keywords - PTMi

Disulfide bond, S-nitrosylation

Proteomic databases

PaxDbiP13444.
PRIDEiP13444.

PTM databases

iPTMnetiP13444.
PhosphoSitePlusiP13444.

Expressioni

Tissue specificityi

Detected in liver (at protein level) (PubMed:1517209). Expressed in liver (PubMed:2806235).2 Publications

Interactioni

Subunit structurei

Homotetramer (MAT-I); dimer of dimers (PubMed:1517209, PubMed:9755242, PubMed:10873471, PubMed:12888348). Homodimer (MAT-III) (PubMed:1517209, PubMed:9755242).1 Publication3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-961260,EBI-961260

GO - Molecular functioni

  • protein dimerization activity Source: RGD
  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015190.

Chemistry databases

BindingDBiP13444.

Structurei

Secondary structure

1397
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi19 – 26Combined sources8
Helixi31 – 47Combined sources17
Beta strandi54 – 61Combined sources8
Beta strandi63 – 73Combined sources11
Helixi80 – 91Combined sources12
Turni96 – 99Combined sources4
Turni102 – 104Combined sources3
Beta strandi105 – 109Combined sources5
Beta strandi112 – 114Combined sources3
Beta strandi137 – 144Combined sources8
Helixi153 – 171Combined sources19
Beta strandi172 – 174Combined sources3
Beta strandi177 – 190Combined sources14
Beta strandi197 – 210Combined sources14
Beta strandi212 – 214Combined sources3
Helixi216 – 225Combined sources10
Turni226 – 231Combined sources6
Turni234 – 236Combined sources3
Beta strandi242 – 246Combined sources5
Turni256 – 259Combined sources4
Turni267 – 274Combined sources8
Helixi291 – 308Combined sources18
Beta strandi313 – 321Combined sources9
Beta strandi331 – 335Combined sources5
Helixi347 – 354Combined sources8
Helixi359 – 365Combined sources7
Turni366 – 369Combined sources4
Helixi373 – 376Combined sources4
Beta strandi377 – 379Combined sources3
Beta strandi381 – 383Combined sources3
Helixi388 – 390Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1O90X-ray3.10A/B1-397[»]
1O92X-ray3.19A/B1-397[»]
1O93X-ray3.49A/B1-397[»]
1O9TX-ray2.90A/B1-397[»]
1QM4X-ray2.66A/B1-397[»]
ProteinModelPortaliP13444.
SMRiP13444.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13444.

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.
HOVERGENiHBG001562.
InParanoidiP13444.
KOiK00789.
PhylomeDBiP13444.

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.

P13444-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGPVDGLCD HSLSEEGAFM FTSESVGEGH PDKICDQISD AVLDAHLKQD
60 70 80 90 100
PNAKVACETV CKTGMVLLCG EITSMAMIDY QRVVRDTIKH IGYDDSAKGF
110 120 130 140 150
DFKTCNVLVA LEQQSPDIAQ CVHLDRNEED VGAGDQGLMF GYATDETEEC
160 170 180 190 200
MPLTIVLAHK LNTRMADLRR SGVLPWLRPD SKTQVTVQYV QDNGAVIPVR
210 220 230 240 250
VHTIVISVQH NEDITLEAMR EALKEQVIKA VVPAKYLDED TIYHLQPSGR
260 270 280 290 300
FVIGGPQGDA GVTGRKIIVD TYGGWGAHGG GAFSGKDYTK VDRSAAYAAR
310 320 330 340 350
WVAKSLVKAG LCRRVLVQVS YAIGVAEPLS ISIFTYGTSK KTERDELLEV
360 370 380 390
VNKNFDLRPG VIVRDLDLKK PIYQKTACYG HFGRSEFPWE VPKKLVF
Length:397
Mass (Da):43,698
Last modified:November 1, 1990 - v2
Checksum:iA847A8CCBB2007BA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti345Missing in AAH89770 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15734 mRNA. Translation: CAA33754.1.
X60822 mRNA. No translation available.
BC089770 mRNA. Translation: AAH89770.1.
PIRiS06114.
RefSeqiNP_036992.2. NM_012860.2.
UniGeneiRn.10418.

Genome annotation databases

GeneIDi25331.
KEGGirno:25331.
UCSCiRGD:3050. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15734 mRNA. Translation: CAA33754.1.
X60822 mRNA. No translation available.
BC089770 mRNA. Translation: AAH89770.1.
PIRiS06114.
RefSeqiNP_036992.2. NM_012860.2.
UniGeneiRn.10418.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1O90X-ray3.10A/B1-397[»]
1O92X-ray3.19A/B1-397[»]
1O93X-ray3.49A/B1-397[»]
1O9TX-ray2.90A/B1-397[»]
1QM4X-ray2.66A/B1-397[»]
ProteinModelPortaliP13444.
SMRiP13444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015190.

Chemistry databases

BindingDBiP13444.
ChEMBLiCHEMBL2195.

PTM databases

iPTMnetiP13444.
PhosphoSitePlusiP13444.

Proteomic databases

PaxDbiP13444.
PRIDEiP13444.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25331.
KEGGirno:25331.
UCSCiRGD:3050. rat.

Organism-specific databases

CTDi4143.
RGDi3050. Mat1a.

Phylogenomic databases

eggNOGiKOG1506. Eukaryota.
COG0192. LUCA.
HOVERGENiHBG001562.
InParanoidiP13444.
KOiK00789.
PhylomeDBiP13444.

Enzyme and pathway databases

UniPathwayiUPA00315; UER00080.
BioCyciMetaCyc:MONOMER-8568.
BRENDAi2.5.1.6. 5301.

Miscellaneous databases

EvolutionaryTraceiP13444.
PROiP13444.

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_RAT
AccessioniPrimary (citable) accession number: P13444
Secondary accession number(s): Q5FVU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 1, 1990
Last modified: November 2, 2016
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.