P04397 · GAL10_YEAST
- ProteinBifunctional protein GAL10
- GeneGAL10
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids699 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Mutarotase converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose (By similarity).
Catalytic activity
- UDP-alpha-D-glucose = UDP-alpha-D-galactose
Cofactor
Pathway
Carbohydrate metabolism; galactose metabolism.
Carbohydrate metabolism; hexose metabolism.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | aldose 1-epimerase activity | |
Molecular Function | carbohydrate binding | |
Molecular Function | UDP-glucose 4-epimerase activity | |
Biological Process | galactose catabolic process via UDP-galactose |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBifunctional protein GAL10
Including 2 domains:
- Recommended nameUDP-glucose 4-epimerase
- EC number
- Alternative names
- Recommended nameAldose 1-epimerase
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP04397
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000197442 | 1-699 | Bifunctional protein GAL10 | |||
Sequence: MTAQLQSESTSKIVLVTGGAGYIGSHTVVELIENGYDCVVADNLSNSTYDSVARLEVLTKHHIPFYEVDLCDRKGLEKVFKEYKIDSVIHFAGLKAVGESTQIPLRYYHNNILGTVVLLELMQQYNVSKFVFSSSATVYGDATRFPNMIPIPEECPLGPTNPYGHTKYAIENILNDLYNSDKKSWKFAILRYFNPIGAHPSGLIGEDPLGIPNNLLPYMAQVAVGRREKLYIFGDDYDSRDGTPIRDYIHVVDLAKGHIAALQYLEAYNENEGLCREWNLGSGKGSTVFEVYHAFCKASGIDLPYKVTGRRAGDVLNLTAKPDRAKRELKWQTELQVEDSCKDLWKWTTENPFGYQLRGVEARFSAEDMRYDARFVTIGAGTRFQATFANLGASIVDLKVNGQSVVLGYENEEGYLNPDSAYIGATIGRYANRISKGKFSLCNKDYQLTVNNGVNANHSSIGSFHRKRFLGPIIQNPSKDVFTAEYMLIDNEKDTEFPGDLLVTIQYTVNVAQKSLEMVYKGKLTAGEATPINLTNHSYFNLNKPYGDTIEGTEIMVRSKKSVDVDKNMIPTGNIVDREIATFNSTKPTVLGPKNPQFDCCFVVDENAKPSQINTLNNELTLIVKAFHPDSNITLEVLSTEPTYQFYTGDFLSAGYEARQGFAIEPGRYIDAINQENWKDCVTLKNGETYGSKIVYRFS | ||||||
Modified residue | 562 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
By galactose.
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-357 | Galactowaldenase | ||||
Sequence: MTAQLQSESTSKIVLVTGGAGYIGSHTVVELIENGYDCVVADNLSNSTYDSVARLEVLTKHHIPFYEVDLCDRKGLEKVFKEYKIDSVIHFAGLKAVGESTQIPLRYYHNNILGTVVLLELMQQYNVSKFVFSSSATVYGDATRFPNMIPIPEECPLGPTNPYGHTKYAIENILNDLYNSDKKSWKFAILRYFNPIGAHPSGLIGEDPLGIPNNLLPYMAQVAVGRREKLYIFGDDYDSRDGTPIRDYIHVVDLAKGHIAALQYLEAYNENEGLCREWNLGSGKGSTVFEVYHAFCKASGIDLPYKVTGRRAGDVLNLTAKPDRAKRELKWQTELQVEDSCKDLWKWTTENPFGYQL | ||||||
Region | 358-699 | Mutarotase | ||||
Sequence: RGVEARFSAEDMRYDARFVTIGAGTRFQATFANLGASIVDLKVNGQSVVLGYENEEGYLNPDSAYIGATIGRYANRISKGKFSLCNKDYQLTVNNGVNANHSSIGSFHRKRFLGPIIQNPSKDVFTAEYMLIDNEKDTEFPGDLLVTIQYTVNVAQKSLEMVYKGKLTAGEATPINLTNHSYFNLNKPYGDTIEGTEIMVRSKKSVDVDKNMIPTGNIVDREIATFNSTKPTVLGPKNPQFDCCFVVDENAKPSQINTLNNELTLIVKAFHPDSNITLEVLSTEPTYQFYTGDFLSAGYEARQGFAIEPGRYIDAINQENWKDCVTLKNGETYGSKIVYRFS |
Sequence similarities
In the N-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family.
In the C-terminal section; belongs to the aldose epimerase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length699
- Mass (Da)78,195
- Last updated1994-10-01 v2
- Checksum8354BAFF65D06934
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 302-306 | in Ref. 5; AAA34629 | ||||
Sequence: DLPYK → WSSVR | ||||||
Sequence conflict | 464 | in Ref. 5; AAA34629 | ||||
Sequence: F → L | ||||||
Sequence conflict | 479-480 | in Ref. 5; AAA34629 | ||||
Sequence: KD → NY | ||||||
Sequence conflict | 498 | in Ref. 5; AAA34629 | ||||
Sequence: P → Q | ||||||
Sequence conflict | 518 | in Ref. 5; AAA34629 | ||||
Sequence: M → I | ||||||
Sequence conflict | 667 | in Ref. 5; AAA34629 | ||||
Sequence: G → C | ||||||
Sequence conflict | 694-695 | in Ref. 5; AAA34629 | ||||
Sequence: IV → TL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z35888 EMBL· GenBank· DDBJ | CAA84961.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X81324 EMBL· GenBank· DDBJ | CAA57106.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
K02115 EMBL· GenBank· DDBJ | AAA34620.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M12348 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AH001375 EMBL· GenBank· DDBJ | AAA34629.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AH001375 EMBL· GenBank· DDBJ | AAA34630.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006936 EMBL· GenBank· DDBJ | DAA07141.1 EMBL· GenBank· DDBJ | Genomic DNA |