A0A1W6CR15 · A0A1W6CR15_9PROT
- ProteinGlutamine--fructose-6-phosphate aminotransferase [isomerizing]
- GeneglmS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids607 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Catalytic activity
- D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 2 | Nucleophile; for GATase activity | ||||
Sequence: C | ||||||
Active site | 602 | For Fru-6P isomerization activity | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | carbohydrate derivative binding | |
Molecular Function | glutamine-fructose-6-phosphate transaminase (isomerizing) activity | |
Biological Process | carbohydrate metabolic process | |
Biological Process | fructose 6-phosphate metabolic process | |
Biological Process | glutamine metabolic process | |
Biological Process | protein N-linked glycosylation | |
Biological Process | UDP-N-acetylglucosamine metabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlutamine--fructose-6-phosphate aminotransferase [isomerizing]
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Rhodospirillaceae > Magnetospirillum
Accessions
- Primary accessionA0A1W6CR15
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M |
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-217 | Glutamine amidotransferase type-2 | ||||
Sequence: CGIVGIIGKQEVPSLLVEGLRRLEYRGYDSAGIATLVDGRIERRRAEGKLANLEALLQTKPVGGLIGIGHTRWATHGVPNERNAHPHATRRVAVVHNGIIENFHELKAELTAKGHAFESDTDTEAVAQLIDHHLGLGMSPEDATAKALERLQGAFALGIIFAGRPDMMIAARQGSPLAIGYGAGEMYLGSDALALAPLTQKISYLNDGDWAVLTAE | ||||||
Domain | 283-422 | SIS | ||||
Sequence: LPFDLSAVKRVRIIACGTSYYAASVAKYWIEKLARLPVEVDIASEFRYRCPPMEADGLAIFISQSGETADTLAALRYCREHGQKTLALVNVPESTIARESEAALLTMAGPEIGVASTKAFTTQLTVLACLAIGMGRATGA | ||||||
Domain | 455-597 | SIS | ||||
Sequence: IAQGIAEARDVLYLGRGTGYPIALEGALKLKEISYIHAEGYAAGELKHGPIALIDDSVPVIVICPTDELYEKTASNVQEVVARGGRVVFFSDREGIDRLSAKAFSSMALPAVDPIVAPILYAIPVQLLAYHVAVAKGTDVDQP |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length607
- Mass (Da)65,223
- Last updated2017-07-05 v1
- ChecksumC436BE6866F58432
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP015848 EMBL· GenBank· DDBJ | ARJ67291.1 EMBL· GenBank· DDBJ | Genomic DNA |