Q9MBC2 (MMT1_HORVU) Reviewed, UniProtKB/Swiss-Prot
Last modified
July 27, 2011.
Version 50.
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: Methionine S-methyltransferase EC=2.1.1.12 Alternative name(s): AdoMet:Met S-methyltransferase Hv-MMT1 | ||||
| Gene names |
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| Organism | Hordeum vulgare (Barley) | ||||
| Taxonomic identifier | 4513 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum |
Protein attributes
| Sequence length | 1088 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the S-methylmethionine (SMM) biosynthesis from adenosyl-L-homocysteine (AdoMet) and methionine. SMM biosynthesis (by MMT1) and degradation (by HMT-1, HMT-2 and HMT-3) constitute the SMM cycle in plants, which is probably required to achieve short term control of AdoMet level. Also able to catalyze the selenium-methylmethionine (SeMM) from AdoMet and selenium-methionine (SeMet). May play a role in phoem sulfur transport; such function is however not essential. |
| Catalytic activity | S-adenosyl-L-methionine + L-methionine = S-adenosyl-L-homocysteine + S-methyl-L-methionine. Ref.2 |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Tissue specificity | Expressed in the shoot, scutellum, and aleurone cells but not in the root or endosperm. Ref.2 |
| Developmental stage | Increases during germination. |
| Sequence similarities | Belongs to the methyltransferase superfamily. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Transferase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | biosynthetic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | methionine S-methyltransferase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro transferase activity, transferring nitrogenous groupsInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 1088 | 1088 | Methionine S-methyltransferase | PRO_0000204461 | |||
Sequences
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References
| [1] | "Cloning and expression studies of S-adenosyl-L-methionine:L-methionine S-methyltransferase (MMT) in germinating barley." Pimenta M., Kaneta T., Kamiya Y. Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Haruna Nijo. |
| [2] | "S-adenosyl-L-methionine:L-methionine S-methyltransferase from germinating barley. Purification and localization." Pimenta M.J., Kaneta T., Larondelle Y., Dohmae N., Kamiya Y. Plant Physiol. 118:431-438(1998) [PubMed: 9765528] [Abstract] Cited for: PROTEIN SEQUENCE OF 159-183, ENZYME ACTIVITY, TISSUE SPECIFICITY. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB028870 mRNA. Translation: BAA94795.1. |
3D structure databases | |
| ProteinModelPortal | Q9MBC2. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Organism-specific databases | |
| Gramene | Q9MBC2. |
Gene expression databases | |
| Genevestigator | Q9MBC2. |
Family and domain databases | |
| InterPro | IPR004839. Aminotransferase_I/II. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view] |
| Gene3D | G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 2 hits. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit. |
| Pfam | PF00155. Aminotran_1_2. 1 hit. [Graphical view] |
| SUPFAM | SSF53383. PyrdxlP-dep_Trfase_major. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | MMT1_HORVU | ||||||||
| Accession | Primary (citable) accession number: Q9MBC2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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