P65340 (METE_MYCTU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 53.
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 | Mycobacterium tuberculosis | ||||||
| Taxonomic identifier | 1773 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 759 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 | growth Inferred from mutant phenotype. Source: MTBBASE methionine biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cell wall Inferred from direct assay. Source: MTBBASE cytosolInferred from direct assay. Source: MTBBASE plasma membraneInferred from direct assay. Source: MTBBASE |
| 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 – 759 | 759 | 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase HAMAP MF_00172 | PRO_0000098641 | |||||
Sites | |||||||||
| Metal binding | 647 | 1 | Zinc By similarity | ||||||
| Metal binding | 649 | 1 | Zinc By similarity | ||||||
| Metal binding | 732 | 1 | Zinc By similarity | ||||||
Sequences
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References
| [1] | "Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G.Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv. |
| [2] | "Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M.J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX842575 Genomic DNA. Translation: CAB09044.1. AE000516 Genomic DNA. Translation: AAK45422.1. |
| PIR | F70539. |
| RefSeq | NP_215649.1. NC_000962.2. NP_335608.1. NC_002755.2. |
3D structure databases | |
| ProteinModelPortal | P65340. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000001734; EBMYCP00000001734; EBMYCG00000001733. EBMYCT00000072486; EBMYCP00000070545; EBMYCG00000072481. |
| GeneID | 888947. 924927. |
| GenomeReviews | Gene locus MT1165 in contig AE000516_GR. Gene locus Rv1133c in contig AL123456_GR. |
| KEGG | mtc:MT1165. mtu:Rv1133c. |
| PATRIC | 18124325. VBIMycTub22151_1282. |
| TIGR | MT1165. |
Organism-specific databases | |
| TubercuList | Rv1133c. |
Phylogenomic databases | |
| GeneTree | EBGT00050000017657. |
| HOGENOM | HBG287495. |
| OMA | RNIWRAN. |
| PhylomeDB | P65340. |
| ProtClustDB | PRK05222. |
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_MYCTU | ||||||||
| Accession | Primary (citable) accession number: P65340 Secondary accession number(s): O06584 | ||||||||
| 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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