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P04397

- GAL10_YEAST

UniProt

P04397 - GAL10_YEAST

Protein

Bifunctional protein GAL10

Gene

GAL10

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    UDP-alpha-D-glucose = UDP-alpha-D-galactose.
    Alpha-D-glucose = beta-D-glucose.PROSITE-ProRule annotation

    Cofactori

    NAD.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei537 – 5371For mutarotase activitySequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi13 – 4432NADSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. aldose 1-epimerase activity Source: SGD
    2. carbohydrate binding Source: InterPro
    3. coenzyme binding Source: InterPro
    4. UDP-glucose 4-epimerase activity Source: SGD

    GO - Biological processi

    1. cellular metabolic process Source: InterPro
    2. galactose catabolic process via UDP-galactose Source: SGD

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Carbohydrate metabolism, Galactose metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciYEAST:YBR019C-MONOMER.
    UniPathwayiUPA00214.
    UPA00242.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional protein GAL10
    Including the following 2 domains:
    UDP-glucose 4-epimerase (EC:5.1.3.2)
    Alternative name(s):
    Galactowaldenase
    Aldose 1-epimerase (EC:5.1.3.3)
    Alternative name(s):
    Galactose mutarotase
    Gene namesi
    Name:GAL10
    Ordered Locus Names:YBR019C
    ORF Names:YBR0301
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBR019c.
    SGDiS000000223. GAL10.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: SGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 699699Bifunctional protein GAL10PRO_0000197442Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei562 – 5621Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP04397.
    PeptideAtlasiP04397.
    PRIDEiP04397.

    Expressioni

    Inductioni

    By galactose.

    Gene expression databases

    GenevestigatoriP04397.

    Interactioni

    Protein-protein interaction databases

    BioGridi32722. 53 interactions.
    DIPiDIP-4891N.
    MINTiMINT-526001.
    STRINGi4932.YBR019C.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 175
    Turni18 – 203
    Helixi22 – 3312
    Beta strandi37 – 426
    Helixi50 – 5910
    Beta strandi65 – 673
    Helixi73 – 8210
    Beta strandi87 – 904
    Helixi97 – 1026
    Helixi104 – 12522
    Beta strandi129 – 1357
    Helixi136 – 1394
    Helixi142 – 1443
    Helixi162 – 18019
    Beta strandi186 – 1927
    Beta strandi194 – 1963
    Beta strandi209 – 2113
    Helixi215 – 2239
    Beta strandi226 – 2283
    Beta strandi248 – 2503
    Helixi251 – 26717
    Beta strandi274 – 2818
    Helixi288 – 29912
    Helixi323 – 3286
    Helixi337 – 35014
    Beta strandi360 – 3678
    Beta strandi373 – 3797
    Beta strandi382 – 39110
    Beta strandi395 – 4006
    Helixi412 – 4154
    Beta strandi432 – 4343
    Helixi435 – 4373
    Beta strandi438 – 4414
    Beta strandi444 – 4474
    Beta strandi455 – 4573
    Helixi460 – 4623
    Helixi464 – 4663
    Beta strandi470 – 4789
    Beta strandi481 – 49010
    Helixi492 – 4943
    Beta strandi495 – 51016
    Turni511 – 5144
    Beta strandi515 – 53117
    Turni542 – 5454
    Beta strandi548 – 5503
    Beta strandi553 – 5586
    Beta strandi561 – 5655
    Beta strandi571 – 5777
    Beta strandi585 – 5873
    Beta strandi589 – 5913
    Beta strandi599 – 6046
    Beta strandi621 – 6277
    Turni629 – 6313
    Beta strandi634 – 64714
    Beta strandi662 – 6687
    Helixi672 – 6743
    Turni676 – 6783
    Helixi679 – 6824
    Beta strandi683 – 6853
    Beta strandi689 – 69911

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Z45X-ray1.85A1-699[»]
    ProteinModelPortaliP04397.
    SMRiP04397. Positions 11-699.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04397.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 357357GalactowaldenaseAdd
    BLAST
    Regioni358 – 699342MutarotaseAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family.Curated
    In the C-terminal section; belongs to the aldose epimerase family.Curated

    Phylogenomic databases

    eggNOGiCOG2017.
    GeneTreeiENSGT00530000063128.
    HOGENOMiHOG000247896.
    KOiK01784.
    K01785.
    OMAiDLWKWTT.
    OrthoDBiEOG77T1F2.

    Family and domain databases

    Gene3Di2.70.98.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR018052. Ald1_epimerase_CS.
    IPR008183. Aldose_1/G6P_1-epimerase.
    IPR025308. Epimerase_C.
    IPR001509. Epimerase_deHydtase.
    IPR011013. Gal_mutarotase_SF_dom.
    IPR005886. GalE.
    IPR014718. Glyco_hydro-type_carb-bd_sub.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR10366:SF39. PTHR10366:SF39. 1 hit.
    PfamiPF01263. Aldose_epim. 1 hit.
    PF01370. Epimerase. 1 hit.
    PF13950. Epimerase_Csub. 1 hit.
    [Graphical view]
    SUPFAMiSSF74650. SSF74650. 1 hit.
    TIGRFAMsiTIGR01179. galE. 1 hit.
    PROSITEiPS00545. ALDOSE_1_EPIMERASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P04397-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTAQLQSEST SKIVLVTGGA GYIGSHTVVE LIENGYDCVV ADNLSNSTYD    50
    SVARLEVLTK HHIPFYEVDL CDRKGLEKVF KEYKIDSVIH FAGLKAVGES 100
    TQIPLRYYHN NILGTVVLLE LMQQYNVSKF VFSSSATVYG DATRFPNMIP 150
    IPEECPLGPT NPYGHTKYAI ENILNDLYNS DKKSWKFAIL RYFNPIGAHP 200
    SGLIGEDPLG IPNNLLPYMA QVAVGRREKL YIFGDDYDSR DGTPIRDYIH 250
    VVDLAKGHIA ALQYLEAYNE NEGLCREWNL GSGKGSTVFE VYHAFCKASG 300
    IDLPYKVTGR RAGDVLNLTA KPDRAKRELK WQTELQVEDS CKDLWKWTTE 350
    NPFGYQLRGV EARFSAEDMR YDARFVTIGA GTRFQATFAN LGASIVDLKV 400
    NGQSVVLGYE NEEGYLNPDS AYIGATIGRY ANRISKGKFS LCNKDYQLTV 450
    NNGVNANHSS IGSFHRKRFL GPIIQNPSKD VFTAEYMLID NEKDTEFPGD 500
    LLVTIQYTVN VAQKSLEMVY KGKLTAGEAT PINLTNHSYF NLNKPYGDTI 550
    EGTEIMVRSK KSVDVDKNMI PTGNIVDREI ATFNSTKPTV LGPKNPQFDC 600
    CFVVDENAKP SQINTLNNEL TLIVKAFHPD SNITLEVLST EPTYQFYTGD 650
    FLSAGYEARQ GFAIEPGRYI DAINQENWKD CVTLKNGETY GSKIVYRFS 699
    Length:699
    Mass (Da):78,195
    Last modified:October 1, 1994 - v2
    Checksum:i8354BAFF65D06934
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti302 – 3065DLPYK → WSSVR no nucleotide entry (PubMed:6715281)Curated
    Sequence conflicti464 – 4641F → L no nucleotide entry (PubMed:6715281)Curated
    Sequence conflicti479 – 4802KD → NY no nucleotide entry (PubMed:6715281)Curated
    Sequence conflicti498 – 4981P → Q no nucleotide entry (PubMed:6715281)Curated
    Sequence conflicti518 – 5181M → I no nucleotide entry (PubMed:6715281)Curated
    Sequence conflicti667 – 6671G → C no nucleotide entry (PubMed:6715281)Curated
    Sequence conflicti694 – 6952IV → TL no nucleotide entry (PubMed:6715281)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z35888 Genomic DNA. Translation: CAA84961.1.
    X81324 Genomic DNA. Translation: CAA57106.1.
    K02115 Genomic DNA. Translation: AAA34620.1.
    M12348 Genomic DNA. No translation available.
    K01609 Genomic DNA. Translation: AAA34630.1.
    BK006936 Genomic DNA. Translation: DAA07141.1.
    PIRiS45875. XEBYUG.
    RefSeqiNP_009575.1. NM_001178367.1.

    Genome annotation databases

    EnsemblFungiiYBR019C; YBR019C; YBR019C.
    GeneIDi852307.
    KEGGisce:YBR019C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z35888 Genomic DNA. Translation: CAA84961.1 .
    X81324 Genomic DNA. Translation: CAA57106.1 .
    K02115 Genomic DNA. Translation: AAA34620.1 .
    M12348 Genomic DNA. No translation available.
    K01609 Genomic DNA. Translation: AAA34630.1 .
    BK006936 Genomic DNA. Translation: DAA07141.1 .
    PIRi S45875. XEBYUG.
    RefSeqi NP_009575.1. NM_001178367.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Z45 X-ray 1.85 A 1-699 [» ]
    ProteinModelPortali P04397.
    SMRi P04397. Positions 11-699.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32722. 53 interactions.
    DIPi DIP-4891N.
    MINTi MINT-526001.
    STRINGi 4932.YBR019C.

    Proteomic databases

    PaxDbi P04397.
    PeptideAtlasi P04397.
    PRIDEi P04397.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR019C ; YBR019C ; YBR019C .
    GeneIDi 852307.
    KEGGi sce:YBR019C.

    Organism-specific databases

    CYGDi YBR019c.
    SGDi S000000223. GAL10.

    Phylogenomic databases

    eggNOGi COG2017.
    GeneTreei ENSGT00530000063128.
    HOGENOMi HOG000247896.
    KOi K01784.
    K01785.
    OMAi DLWKWTT.
    OrthoDBi EOG77T1F2.

    Enzyme and pathway databases

    UniPathwayi UPA00214 .
    UPA00242 .
    BioCyci YEAST:YBR019C-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P04397.
    NextBioi 970981.
    PROi P04397.

    Gene expression databases

    Genevestigatori P04397.

    Family and domain databases

    Gene3Di 2.70.98.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProi IPR018052. Ald1_epimerase_CS.
    IPR008183. Aldose_1/G6P_1-epimerase.
    IPR025308. Epimerase_C.
    IPR001509. Epimerase_deHydtase.
    IPR011013. Gal_mutarotase_SF_dom.
    IPR005886. GalE.
    IPR014718. Glyco_hydro-type_carb-bd_sub.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR10366:SF39. PTHR10366:SF39. 1 hit.
    Pfami PF01263. Aldose_epim. 1 hit.
    PF01370. Epimerase. 1 hit.
    PF13950. Epimerase_Csub. 1 hit.
    [Graphical view ]
    SUPFAMi SSF74650. SSF74650. 1 hit.
    TIGRFAMsi TIGR01179. galE. 1 hit.
    PROSITEi PS00545. ALDOSE_1_EPIMERASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "The complete sequence of a 33 kb fragment on the right arm of chromosome II from Saccharomyces cerevisiae reveals 16 open reading frames, including ten new open reading frames, five previously identified genes and a homologue of the SCO1 gene."
      Smits P.H.M., de Haan M., Maat C., Grivell L.A.
      Yeast 10:S75-S80(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-500.
      Strain: ATCC 204508 / S288c.
    4. "Sequence and functional analysis of a 7.2 kb fragment of Saccharomyces cerevisiae chromosome II including GAL7 and GAL10 and a new essential open reading frame."
      Schaaff-Gerstenschlaeger I., Schindwolf T., Lehnert W., Rose M., Zimmermann F.K.
      Yeast 11:79-83(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-699.
      Strain: ATCC 204508 / S288c.
    5. "Sequence of the Saccharomyces GAL region and its transcription in vivo."
      Citron B.A., Donelson J.E.
      J. Bacteriol. 158:269-278(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47 AND 302-699.
      Strain: Carlsbergensis.
    6. "Sequences that regulate the divergent GAL1-GAL10 promoter in Saccharomyces cerevisiae."
      Johnston M., Davis R.W.
      Mol. Cell. Biol. 4:1440-1448(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46.
    7. "Primary structure of the Saccharomyces cerevisiae GAL7 gene."
      Tajima M., Nogi Y., Fukasawa T.
      Yeast 1:67-77(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 630-699.
    8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGAL10_YEAST
    AccessioniPrimary (citable) accession number: P04397
    Secondary accession number(s): D6VQ21
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3