P49611 (METK1_BRAJU) Reviewed, UniProtKB/Swiss-Prot
Last modified
June 28, 2011.
Version 67.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: S-adenosylmethionine synthase 1 Short name=AdoMet synthase 1 EC=2.5.1.6 Alternative name(s): Methionine adenosyltransferase 1 Short name=MAT 1 | ||
| Gene names |
| ||
| Organism | Brassica juncea (Indian mustard) (Sinapis juncea) | ||
| Taxonomic identifier | 3707 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Brassiceae › Brassica |
Protein attributes
| Sequence length | 393 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme By similarity. |
| Catalytic activity | ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine. |
| Cofactor | Binds 2 divalent ions per subunit. Magnesium or cobalt By similarity. Binds 1 potassium ion per subunit By similarity. |
| Pathway | |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the AdoMet synthase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | One-carbon metabolism |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Cobalt Magnesium Metal-binding Nucleotide-binding Potassium |
| Molecular function | Transferase |
| Gene Ontology (GO) | |
| Biological process | S-adenosylmethionine biosynthetic process Inferred from electronic annotation. Source: InterPro one-carbon metabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW methionine adenosyltransferase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 393 | 393 | S-adenosylmethionine synthase 1 | PRO_0000174458 | |||||
Regions | |||||||||
| Nucleotide binding | 119 – 124 | 6 | ATP Potential | ||||||
| Nucleotide binding | 267 – 274 | 8 | ATP Potential | ||||||
Sites | |||||||||
| Metal binding | 17 | 1 | Magnesium By similarity | ||||||
| Metal binding | 43 | 1 | Potassium By similarity | ||||||
| Metal binding | 271 | 1 | Potassium By similarity | ||||||
| Metal binding | 279 | 1 | Magnesium By similarity | ||||||
| Binding site | 147 | 1 | ATP Potential | ||||||
Sequences
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References
| [1] | "Cloning and nucleotide sequence of a cDNA encoding S-adenosyl-L-methionine synthetase from mustard (Brassica juncea [L.] Czern & Coss)." Wen C.-M., Wu M., Goh C.-J., Pua E.-C. Plant Physiol. 107:1021-1022(1995) [PubMed: 7716233] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. India mustard. Tissue: Leaf. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X80362 mRNA. Translation: CAA56590.1. |
3D structure databases | |
| ProteinModelPortal | P49611. |
| SMR | P49611. Positions 3-388. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| 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. [Graphical view] |
| PANTHER | PTHR11964. S-AdoMet_synt. 1 hit. |
| Pfam | PF02773. S-AdoMet_synt_C. 1 hit. PF02772. S-AdoMet_synt_M. 1 hit. PF00438. S-AdoMet_synt_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000497. MAT. 1 hit. |
| SUPFAM | SSF55973. S-AdoMet_synt. 3 hits. |
| TIGRFAMs | TIGR01034. MetK. 1 hit. |
| PROSITE | PS00376. ADOMET_SYNTHASE_1. 1 hit. PS00377. ADOMET_SYNTHASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | METK1_BRAJU | ||||||||
| Accession | Primary (citable) accession number: P49611 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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