Q6KNA9 (METE_BACAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 62.
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 anthracis | ||||
| Taxonomic identifier | 1392 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
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 Reference 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_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 | |
|---|---|
| EMBL GenBank DDBJ | AE016879 Genomic DNA. Translation: AAP27939.1. AE017334 Genomic DNA. Translation: AAT33335.1. AE017225 Genomic DNA. Translation: AAT56213.1. |
| RefSeq | NP_846453.1. NC_003997.3. YP_020860.1. NC_007530.2. YP_030162.1. NC_005945.1. |
3D structure databases | |
| ProteinModelPortal | Q6KNA9. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q6KNA9. 21 interactions. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000008091; EBBACP00000007847; EBBACG00000008083. EBBACT00000014632; EBBACP00000014253; EBBACG00000014624. EBBACT00000019817; EBBACP00000019302; EBBACG00000019808. |
| 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:BA_4218. bar:GBAA_4218. bat:BAS3912. |
| TIGR | BA_4218. GBAA_4218. |
Phylogenomic databases | |
| GeneTree | EBGT00050000001686. |
| HOGENOM | HBG287495. |
| OMA | RNIWRAN. |
| ProtClustDB | PRK05222. |
Enzyme and pathway databases | |
| BioCyc | BANT260799:BAS3912-MONOMER. BANT261594:GBAA4218-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_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 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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