| General Information |
| MoonProt ID | 4050 |
| First appeared in release | 4.0 |
| Name(s) | Methionine Synthase; 5-methyltetrahydropteroyltriglutamate-homocysteine methyltransferase |
| UniProt ID | P82610 |
| GO terms | "GO:0003871 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity
GO:0008168 methyltransferase activity
GO:0008270 zinc ion binding
GO:0016740 transferase activity
GO:0046872 metal ion binding
GO:0006555 methionine metabolic process
GO:0008652 amino acid biosynthetic process
GO:0009086 methionine biosynthetic process
GO:0019280 L-methionine biosynthetic process from L-homoserine via O-acetyl-L-homoserine
GO:0032259 methylation
GO:0034605 cellular response to heat
GO:0052553 symbiont-mediated perturbation of host immune response
GO:0071266 'de novo' L-methionine biosynthetic process
GO:0098609 cell-cell adhesion
GO:1901605 alpha-amino acid metabolic process
GO:0005634 nucleus
GO:0009277 fungal-type cell wall
GO:0009986 cell surface
GO:0030446 hyphal cell wall
GO:0062040 fungal biofilm matrix" |
| Organisms for which functions have been demonstrated | Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
| Sequence length | 767.0 |
| FASTA sequence | ">sp|P82610|METE_CANAL 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=MET6 PE=1 SV=2
MVQSSVLGFPRIGGQRELKKITEAYWSGKATVEELLAKGKELREHNWKLQQKAGVDIIPSNDFSYYDQVLDLSLLFNAIPERYTKFDLAPIDVLFAMGRGLQKKATETQAAVDVTALEMVKWFDSNYHYVRPTFSHSTEFKLNTAAGIKPVDEFNEAKALGVQTRPVILGPVSYLYLGKADKDSLDLEPISLLPKILPVYKELLQKLKEAGAEQVQIDEPVLVLDLPEAVQSKFKEAYDALVGADVPELILTTYFGDVRPNLKAIENLPVAGFHFDFVRVPEQLDEVASILKDGQTLSAGVVDGRNIWKTDFAKASAVVQKAIEKVGKDKVVVATSSSLLHTPVDLESETKLDAVIKDWFSFATQKLDEVVVIAKNVSGEDVSKQLEANAASIKARSESSITNDPKVQERLTTINEALATRKAAFPERLTEQKAKYNLPLFPTTTIGSFPQTKDIRINRNKFAKGQITAEEYEAFINKEIETVVRFQEEIGLDVLVHGEPERNDMVQYFGEQLNGFAFTTNGWVQSYGSRYVRPPIIVGDVSRPKAMTVKESVYAQSITSKPMKGMLTGPVTILRWSFPRDDVSGKIQALQLGLALRDEVNDLEGAGITVIQVDEPAIREGLPLRAGKERSDYLNWAAQSFRVATSGVENSTQIHSHFCYSDLDPNHIKALDADVVSIEFSKKDDPNYIQEFSEYPNHIGLGLFDIHSPRIPSKQEFVSRIEEILKVYPASKFWVNPDCGLKTRGWPEVKESLTNMVEAAKEFRAKY" |
| Structure Information |
| PDB ID | NA |
| Quaternary structure | NA |
| SCOP | |
| CATH | |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | |
| Predicted Disorder Regions | |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | enzyme, methionine synthase, Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation |
| References for function | Ordiales H, Olano C, Martín C, Blanco-Agudín N, Alcalde I, Merayo-Lloves J, Quirós LM. Phosphoglycerate mutase and methionine synthase act as adhesins of Candida albicans to the corneal epithelium, altering their expression during the tissue adhesion process. Exp Eye Res. 2025 May;254:110322. doi: 10.1016/j.exer.2025.110322. Epub 2025 Mar 6. PMID: 40057112. |
| E.C. number | 2.1.1.14 |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |
| Function 2 |
| Function description | adhesin, binds to heparin sulfate |
| References for function | Ordiales H, Olano C, Martín C, Blanco-Agudín N, Alcalde I, Merayo-Lloves J, Quirós LM. Phosphoglycerate mutase and methionine synthase act as adhesins of Candida albicans to the corneal epithelium, altering their expression during the tissue adhesion process. Exp Eye Res. 2025 May;254:110322. doi: 10.1016/j.exer.2025.110322. Epub 2025 Mar 6. PMID: 40057112. |
| E.C. number | |
| Location of functional site(s) | |
| Cellular location of function | cell surface |
| Comments | |