Reviewed,
UniProtKB/Swiss-Prot Q6KNA9 (METE_BACAN)
Last modified
November 3, 2009.
Version 42.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase EC=2.1.1.14 Alternative name(s): Methionine synthase, vitamin-B12 independent isozyme Cobalamin-independent methionine synthase | ||||
| Gene names |
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| Organism | Bacillus anthracis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1392 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 762 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| 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. |
| 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: HAMAP |
| Molecular function | 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity Inferred from electronic annotation. Source: HAMAP zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| 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_0000098609 | |||||
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 genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. Fraser C.M.Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton. |
| [2] | "Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor. |
| [3] | "Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne. |
Cross-references
Sequence databases | |
|---|---|
| AE016879 Genomic DNA. Translation: AAP27939.1. AE017334 Genomic DNA. Translation: AAT33335.1. AE017225 Genomic DNA. Translation: AAT56213.1. | |
| RefSeq | NP_846453.1. YP_020860.1. YP_030162.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1088935. 2818200. 2850686. |
| GenomeReviews | Gene locus BA_4218 in contig AE016879_GR. Gene locus BAS3912 in contig AE017225_GR. Gene locus GBAA_4218 in contig AE017334_GR. |
| KEGG | ban:BA4218. bar:GBAA4218. bat:BAS3912. |
| TIGR | BA_4218. GBAA_4218. |
Phylogenomic databases | |
| HOGENOM | Q6KNA9. |
| OMA | CSLLHTP. |
Enzyme and pathway databases | |
| BioCyc | BANT260799:BAS3912-MON. BANT261594:GBAA4218-MON. |
| BRENDA | 2.1.1.14. 267517. |
Family and domain databases | |
| HAMAP | MF_00172. [Tree] |
| InterPro | IPR013215. Cbl-indep_Met_Synth_N. IPR002629. Methionine_synth. IPR006276. MeTrfase_B12_ind. [Graphical view] |
| Pfam | PF08267. Meth_synt_1. 1 hit. PF01717. Meth_synt_2. 1 hit. [Graphical view] |
| PIRSF | PIRSF000382. MeTrfase_B12_ind. 1 hit. |
| ProDom | PD004692. Methionine_synth. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR01371. met_syn_B12ind. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | METE_BACAN | ||||||||
| Accession | Primary (citable) accession number: Q6KNA9 Secondary accession number(s): Q6HU26, Q81MM9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


