Q65KT8 (METE_BACLD) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 64.
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: 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase EC=2.1.1.14 Alternative name(s): Cobalamin-independent methionine synthase Methionine synthase, vitamin-B12 independent isozyme | ||||
| Gene names |
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| Organism | Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 279010 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 762 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation By similarity. HAMAP MF_00172 |
| Catalytic activity | 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine. HAMAP MF_00172 |
| Cofactor | Binds 1 zinc ion per subunit By similarity. HAMAP MF_00172 |
| Pathway | Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1. HAMAP MF_00172 |
| Sequence similarities | Belongs to the vitamin-B12 independent methionine synthase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Methionine biosynthesis |
| Domain | Repeat |
| Ligand | Metal-binding Zinc |
| Molecular function | Methyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity Inferred from electronic annotation. Source: EC zinc ion bindingInferred 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 – 762 | 762 | 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase HAMAP MF_00172 | PRO_1000017223 | |||||
Sites | |||||||||
| Metal binding | 645 | 1 | Zinc By similarity | ||||||
| Metal binding | 647 | 1 | Zinc By similarity | ||||||
| Metal binding | 730 | 1 | Zinc By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580. |
| [2] | "Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. Berka R.M.Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000002 Genomic DNA. Translation: AAU22973.1. AE017333 Genomic DNA. Translation: AAU40326.1. |
| RefSeq | YP_078611.1. NC_006270.3. YP_091019.1. NC_006322.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1XDJ based on UniProtKB Q9X112. |
| ProteinModelPortal | Q65KT8. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q65KT8. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000056208; EBBACP00000054739; EBBACG00000056199. EBBACT00000058876; EBBACP00000057309; EBBACG00000058867. |
| GeneID | 3030479. 3098755. |
| GenomeReviews | Gene locus BLi01422 in contig AE017333_GR. Gene locus BL03738 in contig CP000002_GR. |
| KEGG | bld:BLi01422. bli:BL03738. |
| NMPDR | fig|279010.5.peg.876. |
| PATRIC | 18948425. VBIBacLic203714_1416. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0620. |
| GeneTree | EBGT00050000001686. |
| HOGENOM | HBG287495. |
| OMA | RNIWRAN. |
| PhylomeDB | Q65KT8. |
| ProtClustDB | PRK05222. |
Enzyme and pathway databases | |
| BioCyc | BLIC279010-1:BLI01422-MONOMER. BLIC279010:BL03738-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00172. Meth_synth. [Tree] |
| InterPro | IPR013215. Cbl-indep_Met_Synth_N. IPR006276. Cobalamin-indep_Met_synthase. IPR002629. Methionine_synth. [Graphical view] |
| KO | K00549. |
| Pfam | PF08267. Meth_synt_1. 1 hit. PF01717. Meth_synt_2. 1 hit. [Graphical view] |
| PIRSF | PIRSF000382. MeTrfase_B12_ind. 1 hit. |
| TIGRFAMs | TIGR01371. Met_syn_B12ind. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | METE_BACLD | ||||||||
| Accession | Primary (citable) accession number: Q65KT8 Secondary accession number(s): Q62W85 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic 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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