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Entry version 156 (18 Sep 2019)
Sequence version 2 (01 Nov 1990)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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), Methionine adenosyltransferase 2 subunit beta (Mat2b), 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
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi24MagnesiumCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi180 – 182ATPCombined sources1 Publication3
Nucleotide bindingi248 – 251ATPCombined sources2 Publications4
Nucleotide bindingi265 – 266ATPCombined sources1 Publication2

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTransferase
Biological processOne-carbon metabolism
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-8568

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.5.1.6 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-156581 Methylation
R-RNO-1614635 Sulfur amino acid metabolism
R-RNO-2408508 Metabolism of ingested SeMet, Sec, MeSec into H2Se

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00315;UER00080

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Mat1a
Synonyms:Ams1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
3050 Mat1a

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2195

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001744341 – 397S-adenosylmethionine synthase isoform type-1Add BLAST397

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi35 ↔ 611 Publication1 Publication
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei121S-nitrosocysteine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P13444

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P13444

PRoteomics IDEntifications database

More...
PRIDEi
P13444

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P13444

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P13444

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
247370, 2 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-58 Methionine adenosyltransferase complex variant 1
CPX-59 Methionine adenosyltransferase complex variant 3

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000015190

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P13444

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1397
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P13444

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P13444

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni114 – 126Flexible loopBy similarityAdd BLAST13

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the AdoMet synthase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1506 Eukaryota
COG0192 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P13444

KEGG Orthology (KO)

More...
KOi
K00789

Database of Orthologous Groups

More...
OrthoDBi
685006at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P13444

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_00086 S_AdoMet_synth1, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR022631 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

The PANTHER Classification System

More...
PANTHERi
PTHR11964 PTHR11964, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02773 S-AdoMet_synt_C, 1 hit
PF02772 S-AdoMet_synt_M, 1 hit
PF00438 S-AdoMet_synt_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000497 MAT, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF55973 SSF55973, 3 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01034 metK, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00376 ADOMET_SYNTHASE_1, 1 hit
PS00377 ADOMET_SYNTHASE_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA847A8CCBB2007BA
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2K248A0A0G2K248_RAT
S-adenosylmethionine synthase
Mat1a
396Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F1LZ34F1LZ34_RAT
S-adenosylmethionine synthase
Mat1a
395Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti345Missing in AAH89770 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X15734 mRNA Translation: CAA33754.1
X60822 mRNA No translation available.
BC089770 mRNA Translation: AAH89770.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S06114

NCBI Reference Sequences

More...
RefSeqi
NP_036992.2, NM_012860.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
25331

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:25331

UCSC genome browser

More...
UCSCi
RGD:3050 rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]
SMRiP13444
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi247370, 2 interactors
ComplexPortaliCPX-58 Methionine adenosyltransferase complex variant 1
CPX-59 Methionine adenosyltransferase complex variant 3
STRINGi10116.ENSRNOP00000015190

Chemistry databases

BindingDBiP13444
ChEMBLiCHEMBL2195

PTM databases

iPTMnetiP13444
PhosphoSitePlusiP13444

Proteomic databases

jPOSTiP13444
PaxDbiP13444
PRIDEiP13444

Genome annotation databases

GeneIDi25331
KEGGirno:25331
UCSCiRGD:3050 rat

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
4143
RGDi3050 Mat1a

Phylogenomic databases

eggNOGiKOG1506 Eukaryota
COG0192 LUCA
InParanoidiP13444
KOiK00789
OrthoDBi685006at2759
PhylomeDBiP13444

Enzyme and pathway databases

UniPathwayiUPA00315;UER00080
BioCyciMetaCyc:MONOMER-8568
BRENDAi2.5.1.6 5301
ReactomeiR-RNO-156581 Methylation
R-RNO-1614635 Sulfur amino acid metabolism
R-RNO-2408508 Metabolism of ingested SeMet, Sec, MeSec into H2Se

Miscellaneous databases

EvolutionaryTraceiP13444

Protein Ontology

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PROi
PR:P13444

Family and domain databases

HAMAPiMF_00086 S_AdoMet_synth1, 1 hit
InterProiView protein in InterPro
IPR022631 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
PANTHERiPTHR11964 PTHR11964, 1 hit
PfamiView protein in Pfam
PF02773 S-AdoMet_synt_C, 1 hit
PF02772 S-AdoMet_synt_M, 1 hit
PF00438 S-AdoMet_synt_N, 1 hit
PIRSFiPIRSF000497 MAT, 1 hit
SUPFAMiSSF55973 SSF55973, 3 hits
TIGRFAMsiTIGR01034 metK, 1 hit
PROSITEiView protein in PROSITE
PS00376 ADOMET_SYNTHASE_1, 1 hit
PS00377 ADOMET_SYNTHASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMETK1_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P13444
Secondary accession number(s): Q5FVU2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 1, 1990
Last modified: September 18, 2019
This is version 156 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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