A0A158JZV0 · A0A158JZV0_9BURK
- ProteinDihydrofolate synthase/folylpolyglutamate synthase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids436 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes successive additions of L-glutamate to tetrahydrofolate or 10-formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, leading to folylpolyglutamate derivatives.
Catalytic activity
- (6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-glutamate = (6R)-5,10-methylenetetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + H+ + phosphate
(6R)-5,10-methylenetetrahydrofolyl-(γ-L-Glu)(n) RHEA-COMP:13257 + CHEBI:30616 + CHEBI:29985 = (6R)-5,10-methylenetetrahydrofolyl-(γ-L-Glu)(n+1) RHEA-COMP:13258 + CHEBI:456216 + CHEBI:15378 + CHEBI:43474
Pathway
Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2.
Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | dihydrofolate synthase activity | |
Molecular Function | metal ion binding | |
Molecular Function | tetrahydrofolylpolyglutamate synthase activity | |
Biological Process | folic acid biosynthetic process | |
Biological Process | tetrahydrofolate biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDihydrofolate synthase/folylpolyglutamate synthase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Caballeronia
Accessions
- Primary accessionA0A158JZV0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 47-269 | Mur ligase central | ||||
Sequence: VGGTNGKGSTCAILETILLRAGYRVGCHTSPHLLAFNERARIDGADATDAELLEHFEAVEAARASLSEPVSLTYFEFTTLAILRLFASRKLDAVILEVGLGGRLDAVNIVDTDCAIVTSIDIDHTDYLGDTREKIGFEKAGIFRAGKPAVCGDPSPPQTLIDHAEAVGADLWLVGRDFRYEAQPGNERQQWSYIGRSQRRSALAYPALRGANQLINTSAALAA | ||||||
Domain | 295-421 | Mur ligase C-terminal | ||||
Sequence: GRFQVLPGKPQIILDVAHNPHAAAVLAQNLGNMGFFPYTYAVFGAMGDKDVEGIVKQLKGEIDHWNVTSLPTPRAASTEALEAALREAGVEDGPDSSVTRFETPVEAFQDAIKRASENDRILVFGSF |
Sequence similarities
Belongs to the folylpolyglutamate synthase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length436
- Mass (Da)47,103
- Last updated2017-09-27 v1
- Checksum16BB7C392D7700DB
Keywords
- Technical term