P04397 · GAL10_YEAST

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

Cofactor

NAD+ (UniProtKB | Rhea| CHEBI:57540 )

Pathway

Carbohydrate metabolism; galactose metabolism.
Carbohydrate metabolism; hexose metabolism.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site13-44NAD+ (UniProtKB | ChEBI)
Active site537For mutarotase activity

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionaldose 1-epimerase activity
Molecular Functioncarbohydrate binding
Molecular FunctionUDP-glucose 4-epimerase activity
Biological Processgalactose catabolic process via UDP-galactose

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Bifunctional protein GAL10

Including 2 domains:

  • Recommended name
    UDP-glucose 4-epimerase
  • EC number
  • Alternative names
    • Galactowaldenase
  • Recommended name
    Aldose 1-epimerase
  • EC number
  • Alternative names
    • Galactose mutarotase

Gene names

    • Name
      GAL10
    • ORF names
      YBR0301
    • Ordered locus names
      YBR019C

Organism names

Accessions

  • Primary accession
    P04397
  • Secondary accessions
    • D6VQ21
    • Q05765

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001974421-699Bifunctional protein GAL10
Modified residue562Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Induction

By galactose.

Interaction

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-357Galactowaldenase
Region358-699Mutarotase

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 status
    Complete
  • Length
    699
  • Mass (Da)
    78,195
  • Last updated
    1994-10-01 v2
  • Checksum
    8354BAFF65D06934
MTAQLQSESTSKIVLVTGGAGYIGSHTVVELIENGYDCVVADNLSNSTYDSVARLEVLTKHHIPFYEVDLCDRKGLEKVFKEYKIDSVIHFAGLKAVGESTQIPLRYYHNNILGTVVLLELMQQYNVSKFVFSSSATVYGDATRFPNMIPIPEECPLGPTNPYGHTKYAIENILNDLYNSDKKSWKFAILRYFNPIGAHPSGLIGEDPLGIPNNLLPYMAQVAVGRREKLYIFGDDYDSRDGTPIRDYIHVVDLAKGHIAALQYLEAYNENEGLCREWNLGSGKGSTVFEVYHAFCKASGIDLPYKVTGRRAGDVLNLTAKPDRAKRELKWQTELQVEDSCKDLWKWTTENPFGYQLRGVEARFSAEDMRYDARFVTIGAGTRFQATFANLGASIVDLKVNGQSVVLGYENEEGYLNPDSAYIGATIGRYANRISKGKFSLCNKDYQLTVNNGVNANHSSIGSFHRKRFLGPIIQNPSKDVFTAEYMLIDNEKDTEFPGDLLVTIQYTVNVAQKSLEMVYKGKLTAGEATPINLTNHSYFNLNKPYGDTIEGTEIMVRSKKSVDVDKNMIPTGNIVDREIATFNSTKPTVLGPKNPQFDCCFVVDENAKPSQINTLNNELTLIVKAFHPDSNITLEVLSTEPTYQFYTGDFLSAGYEARQGFAIEPGRYIDAINQENWKDCVTLKNGETYGSKIVYRFS

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict302-306in Ref. 5; AAA34629
Sequence conflict464in Ref. 5; AAA34629
Sequence conflict479-480in Ref. 5; AAA34629
Sequence conflict498in Ref. 5; AAA34629
Sequence conflict518in Ref. 5; AAA34629
Sequence conflict667in Ref. 5; AAA34629
Sequence conflict694-695in Ref. 5; AAA34629

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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