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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.

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
Binding sitei30 – 301SubstrateBy similarity
Metal bindingi32 – 321MagnesiumBy similarity
Metal bindingi58 – 581PotassiumBy similarity
Binding sitei160 – 1601ATPSequence analysis
Binding sitei180 – 1801SubstrateBy similarity
Binding sitei248 – 2481SubstrateBy similarity
Binding sitei250 – 2501Substrate; via carbonyl oxygenBy similarity
Binding sitei259 – 2591SubstrateBy similarity
Metal bindingi284 – 2841PotassiumBy similarity
Metal bindingi292 – 2921MagnesiumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi132 – 1376ATPSequence analysis

GO - Molecular functioni

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

GO - Biological processi

  • 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, Cobalt, 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:2.5.1.6)
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

Chemistry

ChEMBLiCHEMBL2111450.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 397397S-adenosylmethionine synthase isoform type-1PRO_0000174434Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi35 ↔ 611 Publication
Modified residuei121 – 1211S-nitrosocysteine1 Publication

Post-translational modificationi

S-nitrosylation of Cys-121 inactivates the enzyme.2 Publications

Keywords - PTMi

Disulfide bond, S-nitrosylation

Proteomic databases

PaxDbiP13444.
PRIDEiP13444.

PTM databases

iPTMnetiP13444.
PhosphoSiteiP13444.

Expressioni

Tissue specificityi

Expressed in liver.1 Publication

Interactioni

Subunit structurei

Homotetramer (MAT-I) or homodimer (MAT-III).

Binary interactionsi

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

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein dimerization activity Source: RGD
  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015190.

Chemistry

BindingDBiP13444.

Structurei

Secondary structure

1
397
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 268Combined sources
Helixi31 – 4717Combined sources
Beta strandi54 – 618Combined sources
Beta strandi63 – 7311Combined sources
Helixi80 – 9112Combined sources
Turni96 – 994Combined sources
Turni102 – 1043Combined sources
Beta strandi105 – 1095Combined sources
Beta strandi112 – 1143Combined sources
Beta strandi137 – 1448Combined sources
Helixi153 – 17119Combined sources
Beta strandi172 – 1743Combined sources
Beta strandi177 – 19014Combined sources
Beta strandi197 – 21014Combined sources
Beta strandi212 – 2143Combined sources
Helixi216 – 22510Combined sources
Turni226 – 2316Combined sources
Turni234 – 2363Combined sources
Beta strandi242 – 2465Combined sources
Turni256 – 2594Combined sources
Turni267 – 2748Combined sources
Helixi291 – 30818Combined sources
Beta strandi313 – 3219Combined sources
Beta strandi331 – 3355Combined sources
Helixi347 – 3548Combined sources
Helixi359 – 3657Combined sources
Turni366 – 3694Combined sources
Helixi373 – 3764Combined sources
Beta strandi377 – 3793Combined sources
Beta strandi381 – 3833Combined sources
Helixi388 – 3903Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 17-397.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13444.

Family & Domainsi

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.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti345 – 3451Missing in AAH89770 (PubMed:15489334).Curated

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
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. Positions 17-397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015190.

Chemistry

BindingDBiP13444.
ChEMBLiCHEMBL2111450.

PTM databases

iPTMnetiP13444.
PhosphoSiteiP13444.

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.
NextBioi606211.
PROiP13444.

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

« Hide 'large scale' publications
  1. "Isolation of a cDNA encoding the rat liver S-adenosylmethionine synthetase."
    Horikawa S., Ishikawa M., Ozasa H., Tsukada K.
    Eur. J. Biochem. 184:497-501(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: Wistar.
    Tissue: Liver.
  2. "Analysis of the 5' non-coding region of rat liver S-adenosylmethionine synthetase mRNA and comparison of the Mr deduced from the cDNA sequence and the purified enzyme."
    Alvarez L., Asuncion M., Corrales F., Pajares M.A., Mato J.M.
    FEBS Lett. 290:142-146(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Spleen.
  4. "Nitric oxide inactivates rat hepatic methionine adenosyltransferase In vivo by S-nitrosylation."
    Ruiz F., Corrales F.J., Miqueo C., Mato J.M.
    Hepatology 28:1051-1057(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: S-NITROSYLATION.
  5. "Methionine adenosyltransferase S-nitrosylation is regulated by the basic and acidic amino acids surrounding the target thiol."
    Perez-Mato I., Castro C., Ruiz F.A., Corrales F.J., Mato J.M.
    J. Biol. Chem. 274:17075-17079(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: S-NITROSYLATION AT CYS-121.
  6. "Assignment of a single disulfide bridge in rat liver methionine adenosyltransferase."
    Martinez-Chantar M.L., Pajares M.A.
    Eur. J. Biochem. 267:132-137(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BOND.
  7. "Crystal structures of methionine adenosyltransferase complexed with substrates and products reveal the methionine-ATP recognition and give insights into the catalytic mechanism."
    Gonzalez B., Pajares M.A., Hermoso J.A., Guillerm D., Guillerm G., Sanz-Aparicio J.
    J. Mol. Biol. 331:407-416(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).

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: January 20, 2016
This is version 146 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.