P14742 · GFA1_YEAST
- ProteinGlutamine--fructose-6-phosphate aminotransferase [isomerizing]
- GeneGFA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids717 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in amino sugar synthesis (formation of chitin, supplies the amino sugars of asparagine-linked oligosaccharides of glycoproteins).
Miscellaneous
Present with 14300 molecules/cell in log phase SD medium.
Catalytic activity
- D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate
Pathway
Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 2 | For GATase activity | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | carbohydrate derivative binding | |
Molecular Function | glutamine-fructose-6-phosphate transaminase (isomerizing) activity | |
Biological Process | chitin biosynthetic process | |
Biological Process | fructose 6-phosphate metabolic process | |
Biological Process | glutamine metabolic process | |
Biological Process | protein N-linked glycosylation | |
Biological Process | UDP-N-acetylglucosamine biosynthetic process | |
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
- Short namesGFAT
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP14742
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000135289 | 2-717 | Glutamine--fructose-6-phosphate aminotransferase [isomerizing] | |||
Sequence: CGIFGYCNYLVERSRGEIIDTLVDGLQRLEYRGYDSTGIAIDGDEADSTFIYKQIGKVSALKEEITKQNPNRDVTFVSHCGIAHTRWATHGRPEQVNCHPQRSDPEDQFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIAKLYLHLYNTNLQNGHDLDFHELTKLVLLELEGSYGLLCKSCHYPNEVIATRKGSPLLIGVKSEKKLKVDFVDVEFPEENAGQPEIPLKSNNKSFGLGPKKAREFEAGSQNANLLPIAANEFNLRHSQSRAFLSEDGSPTPVEFFVSSDAASVVKHTKKVLFLEDDDLAHIYDGELHIHRSRREVGASMTRSIQTLEMELAQIMKGPYDHFMQKEIYEQPESTFNTMRGRIDYENNKVILGGLKAWLPVVRRARRLIMIACGTSYHSCLATRAIFEELSDIPVSVELASDFLDRKCPVFRDDVCVFVSQSGETADTMLALNYCLERGALTVGIVNSVGSSISRVTHCGVHINAGPEIGVASTKAYTSQYIALVMFALSLSDDRVSKIDRRIEIIQGLKLIPGQIKQVLKLEPRIKKLCATELKDQKSLLLLGRGYQFAAALEGALKIKEISYMHSEGVLAGELKHGVLALVDENLPIIAFGTRDSLFPKVVSSIEQVTARKGHPIIICNENDEVWAQKSKSIDLQTLEVPQTVDCLQGLINIIPLQLMSYWLAVNKGIDVDFPRNLAKSVTVE | ||||||
Modified residue | 253 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 334 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 336 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
The activity of this enzyme increases in presence of mating pheromone (transcriptional regulation).
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-318 | Glutamine amidotransferase type-2 | ||||
Sequence: CGIFGYCNYLVERSRGEIIDTLVDGLQRLEYRGYDSTGIAIDGDEADSTFIYKQIGKVSALKEEITKQNPNRDVTFVSHCGIAHTRWATHGRPEQVNCHPQRSDPEDQFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIAKLYLHLYNTNLQNGHDLDFHELTKLVLLELEGSYGLLCKSCHYPNEVIATRKGSPLLIGVKSEKKLKVDFVDVEFPEENAGQPEIPLKSNNKSFGLGPKKAREFEAGSQNANLLPIAANEFNLRHSQSRAFLSEDGSPTPVEFFVSSDAASVVKHTKKVLFLEDDDLAHIYDG | ||||||
Domain | 390-529 | SIS 1 | ||||
Sequence: WLPVVRRARRLIMIACGTSYHSCLATRAIFEELSDIPVSVELASDFLDRKCPVFRDDVCVFVSQSGETADTMLALNYCLERGALTVGIVNSVGSSISRVTHCGVHINAGPEIGVASTKAYTSQYIALVMFALSLSDDRVS | ||||||
Domain | 562-707 | SIS 2 | ||||
Sequence: CATELKDQKSLLLLGRGYQFAAALEGALKIKEISYMHSEGVLAGELKHGVLALVDENLPIIAFGTRDSLFPKVVSSIEQVTARKGHPIIICNENDEVWAQKSKSIDLQTLEVPQTVDCLQGLINIIPLQLMSYWLAVNKGIDVDFP |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length717
- Mass (Da)80,047
- Last updated2007-01-23 v4
- Checksum27E5F0D24BDC451A
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 453-454 | in Ref. 1; AAA34643 | ||||
Sequence: QS → HC | ||||||
Sequence conflict | 534 | in Ref. 1; AAA34643 | ||||
Sequence: Missing |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J04719 EMBL· GenBank· DDBJ | AAA34643.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X71133 EMBL· GenBank· DDBJ | CAA50453.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z28104 EMBL· GenBank· DDBJ | CAA81944.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006944 EMBL· GenBank· DDBJ | DAA09054.1 EMBL· GenBank· DDBJ | Genomic DNA |