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Protein

S-adenosylmethionine synthase isoform type-1

Gene

MAT1A

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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.By similarity

Catalytic activityi

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

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.By similarity
Proteins known to be involved in this subpathway in this organism are:
  1. S-adenosylmethionine synthase (MAT1A), S-adenosylmethionine synthase (MAT2A), Methionine adenosyltransferase 2 subunit beta (MAT2B), S-adenosylmethionine synthase isoform type-1 (MAT1A)
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

UniPathwayiUPA00315; UER00080.

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine synthase isoform type-1 (EC:2.5.1.6By similarity)
Short name:
AdoMet synthase 1
Alternative name(s):
Methionine adenosyltransferase 1
Short name:
MAT 1
Gene namesi
Name:MAT1A
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002875271 – 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

PaxDbiQ2KJC6.
PeptideAtlasiQ2KJC6.
PRIDEiQ2KJC6.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000031255.

Structurei

3D structure databases

ProteinModelPortaliQ2KJC6.
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.
HOGENOMiHOG000245710.
HOVERGENiHBG001562.
InParanoidiQ2KJC6.
KOiK00789.

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.

Q2KJC6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGPVDGLCD HSLSEEGAFM FTSESVGEGH PDKICDQISD AVLDAHLKQD
60 70 80 90 100
PNAKVACETV CKTGMVLLCG EITSMAMVDY QRVVRETIQH IGYDDSAKGF
110 120 130 140 150
DFKTCNVLVA LEQQSPDIAQ CVHLDRNEED VGAGDQGLMF GYATDETEEC
160 170 180 190 200
MPLTIMLAHR LNARMAELRR SGQLPWLQPD SKTQVTVQYT QDNGAVIPMR
210 220 230 240 250
VHTVVISVQH NEDITLEDMR RALKEQVIRA VVPARYLDED TIYHLQPSGR
260 270 280 290 300
FVIGGPQGDA GVTGRKIIVD TYGGWGAHGG GAFSGKDYTK VDRSAAYAAR
310 320 330 340 350
WVAKSLVKAG LCRRVLVQVS YAIGVAEPLS ISIFTYGTSQ KTERELLDVV
360 370 380 390
NKNFDLRPGV IVRDLDLKKP IYQKTACYGH FGRSEFPWEV PKKLVF
Length:396
Mass (Da):43,761
Last modified:March 7, 2006 - v1
Checksum:i2188750981D65CDB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC105410 mRNA. Translation: AAI05411.1.
RefSeqiNP_001039962.1. NM_001046497.1.
UniGeneiBt.55380.

Genome annotation databases

GeneIDi541078.
KEGGibta:541078.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC105410 mRNA. Translation: AAI05411.1.
RefSeqiNP_001039962.1. NM_001046497.1.
UniGeneiBt.55380.

3D structure databases

ProteinModelPortaliQ2KJC6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000031255.

Proteomic databases

PaxDbiQ2KJC6.
PeptideAtlasiQ2KJC6.
PRIDEiQ2KJC6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi541078.
KEGGibta:541078.

Organism-specific databases

CTDi4143.

Phylogenomic databases

eggNOGiKOG1506. Eukaryota.
COG0192. LUCA.
HOGENOMiHOG000245710.
HOVERGENiHBG001562.
InParanoidiQ2KJC6.
KOiK00789.

Enzyme and pathway databases

UniPathwayiUPA00315; UER00080.

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_BOVIN
AccessioniPrimary (citable) accession number: Q2KJC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: March 7, 2006
Last modified: November 2, 2016
This is version 81 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.