GAL10_YEAST
ID GAL10_YEAST Reviewed; 699 AA.
AC P04397; D6VQ21;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Bifunctional protein GAL10;
DE Includes:
DE RecName: Full=UDP-glucose 4-epimerase;
DE EC=5.1.3.2;
DE AltName: Full=Galactowaldenase;
DE Includes:
DE RecName: Full=Aldose 1-epimerase;
DE EC=5.1.3.3;
DE AltName: Full=Galactose mutarotase;
GN Name=GAL10; OrderedLocusNames=YBR019C; ORFNames=YBR0301;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-500.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091864; DOI=10.1002/yea.320100010;
RA Smits P.H.M., de Haan M., Maat C., Grivell L.A.;
RT "The complete sequence of a 33 kb fragment on the right arm of chromosome
RT II from Saccharomyces cerevisiae reveals 16 open reading frames, including
RT ten new open reading frames, five previously identified genes and a
RT homologue of the SCO1 gene.";
RL Yeast 10:S75-S80(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-699.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7762304; DOI=10.1002/yea.320110110;
RA Schaaff-Gerstenschlaeger I., Schindwolf T., Lehnert W., Rose M.,
RA Zimmermann F.K.;
RT "Sequence and functional analysis of a 7.2 kb fragment of Saccharomyces
RT cerevisiae chromosome II including GAL7 and GAL10 and a new essential open
RT reading frame.";
RL Yeast 11:79-83(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47 AND 302-699.
RC STRAIN=Carlsbergensis;
RX PubMed=6715281; DOI=10.1128/jb.158.1.269-278.1984;
RA Citron B.A., Donelson J.E.;
RT "Sequence of the Saccharomyces GAL region and its transcription in vivo.";
RL J. Bacteriol. 158:269-278(1984).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46.
RX PubMed=6092912; DOI=10.1128/mcb.4.8.1440-1448.1984;
RA Johnston M., Davis R.W.;
RT "Sequences that regulate the divergent GAL1-GAL10 promoter in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 4:1440-1448(1984).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 630-699.
RX PubMed=2851900; DOI=10.1002/yea.320010108;
RA Tajima M., Nogi Y., Fukasawa T.;
RT "Primary structure of the Saccharomyces cerevisiae GAL7 gene.";
RL Yeast 1:67-77(1985).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Mutarotase converts alpha-aldose to the beta-anomer. It is
CC active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and
CC lactose (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-alpha-D-glucose = UDP-alpha-D-galactose;
CC Xref=Rhea:RHEA:22168, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914;
CC EC=5.1.3.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose = beta-D-glucose; Xref=Rhea:RHEA:10264,
CC ChEBI:CHEBI:15903, ChEBI:CHEBI:17925; EC=5.1.3.3;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10126};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC -!- INDUCTION: By galactose.
CC -!- SIMILARITY: In the N-terminal section; belongs to the NAD(P)-dependent
CC epimerase/dehydratase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the aldose epimerase
CC family. {ECO:0000305}.
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DR EMBL; Z35888; CAA84961.1; -; Genomic_DNA.
DR EMBL; X81324; CAA57106.1; -; Genomic_DNA.
DR EMBL; K02115; AAA34620.1; -; Genomic_DNA.
DR EMBL; M12348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; K01609; AAA34630.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07141.1; -; Genomic_DNA.
DR PIR; S45875; XEBYUG.
DR RefSeq; NP_009575.1; NM_001178367.1.
DR PDB; 1Z45; X-ray; 1.85 A; A=1-699.
DR PDBsum; 1Z45; -.
DR AlphaFoldDB; P04397; -.
DR SMR; P04397; -.
DR BioGRID; 32722; 114.
DR DIP; DIP-4891N; -.
DR IntAct; P04397; 44.
DR MINT; P04397; -.
DR STRING; 4932.YBR019C; -.
DR iPTMnet; P04397; -.
DR PaxDb; P04397; -.
DR PRIDE; P04397; -.
DR TopDownProteomics; P04397; -.
DR EnsemblFungi; YBR019C_mRNA; YBR019C; YBR019C.
DR GeneID; 852307; -.
DR KEGG; sce:YBR019C; -.
DR SGD; S000000223; GAL10.
DR VEuPathDB; FungiDB:YBR019C; -.
DR eggNOG; KOG1371; Eukaryota.
DR eggNOG; KOG1604; Eukaryota.
DR GeneTree; ENSGT00940000158000; -.
DR HOGENOM; CLU_007383_22_0_1; -.
DR InParanoid; P04397; -.
DR OMA; KGLYREW; -.
DR BioCyc; YEAST:YBR019C-MON; -.
DR BRENDA; 5.1.3.2; 984.
DR Reactome; R-SCE-70370; Galactose catabolism.
DR UniPathway; UPA00214; -.
DR UniPathway; UPA00242; -.
DR EvolutionaryTrace; P04397; -.
DR PRO; PR:P04397; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P04397; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0004034; F:aldose 1-epimerase activity; IDA:SGD.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IDA:SGD.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IDA:SGD.
DR CDD; cd05247; UDP_G4E_1_SDR_e; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR018052; Ald1_epimerase_CS.
DR InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005886; UDP_G4E.
DR Pfam; PF01263; Aldose_epim; 1.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR TIGRFAMs; TIGR01179; galE; 1.
DR PROSITE; PS00545; ALDOSE_1_EPIMERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Galactose metabolism; Isomerase;
KW Multifunctional enzyme; NAD; Phosphoprotein; Reference proteome.
FT CHAIN 1..699
FT /note="Bifunctional protein GAL10"
FT /id="PRO_0000197442"
FT REGION 1..357
FT /note="Galactowaldenase"
FT REGION 358..699
FT /note="Mutarotase"
FT ACT_SITE 537
FT /note="For mutarotase activity"
FT /evidence="ECO:0000255"
FT BINDING 13..44
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 302..306
FT /note="DLPYK -> WSSVR (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="F -> L (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 479..480
FT /note="KD -> NY (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="P -> Q (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="M -> I (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 667
FT /note="G -> C (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 694..695
FT /note="IV -> TL (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:1Z45"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:1Z45"
FT HELIX 22..33
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:1Z45"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1Z45"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1Z45"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:1Z45"
FT HELIX 104..125
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:1Z45"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:1Z45"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:1Z45"
FT HELIX 162..180
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:1Z45"
FT HELIX 215..223
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:1Z45"
FT HELIX 251..267
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 274..281
FT /evidence="ECO:0007829|PDB:1Z45"
FT HELIX 288..299
FT /evidence="ECO:0007829|PDB:1Z45"
FT HELIX 323..328
FT /evidence="ECO:0007829|PDB:1Z45"
FT HELIX 337..350
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 360..367
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 382..391
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:1Z45"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:1Z45"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 438..441
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:1Z45"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:1Z45"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 470..478
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 481..490
FT /evidence="ECO:0007829|PDB:1Z45"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 495..510
FT /evidence="ECO:0007829|PDB:1Z45"
FT TURN 511..514
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 515..531
FT /evidence="ECO:0007829|PDB:1Z45"
FT TURN 542..545
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 553..558
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 561..565
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 571..577
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 599..604
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 621..627
FT /evidence="ECO:0007829|PDB:1Z45"
FT TURN 629..631
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 634..647
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 662..668
FT /evidence="ECO:0007829|PDB:1Z45"
FT HELIX 672..674
FT /evidence="ECO:0007829|PDB:1Z45"
FT TURN 676..678
FT /evidence="ECO:0007829|PDB:1Z45"
FT HELIX 679..682
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 683..685
FT /evidence="ECO:0007829|PDB:1Z45"
FT STRAND 689..699
FT /evidence="ECO:0007829|PDB:1Z45"
SQ SEQUENCE 699 AA; 78195 MW; 8354BAFF65D06934 CRC64;
MTAQLQSEST SKIVLVTGGA GYIGSHTVVE LIENGYDCVV ADNLSNSTYD SVARLEVLTK
HHIPFYEVDL CDRKGLEKVF KEYKIDSVIH FAGLKAVGES TQIPLRYYHN NILGTVVLLE
LMQQYNVSKF VFSSSATVYG DATRFPNMIP IPEECPLGPT NPYGHTKYAI ENILNDLYNS
DKKSWKFAIL RYFNPIGAHP SGLIGEDPLG IPNNLLPYMA QVAVGRREKL YIFGDDYDSR
DGTPIRDYIH VVDLAKGHIA ALQYLEAYNE NEGLCREWNL GSGKGSTVFE VYHAFCKASG
IDLPYKVTGR RAGDVLNLTA KPDRAKRELK WQTELQVEDS CKDLWKWTTE NPFGYQLRGV
EARFSAEDMR YDARFVTIGA GTRFQATFAN LGASIVDLKV NGQSVVLGYE NEEGYLNPDS
AYIGATIGRY ANRISKGKFS LCNKDYQLTV NNGVNANHSS IGSFHRKRFL GPIIQNPSKD
VFTAEYMLID NEKDTEFPGD LLVTIQYTVN VAQKSLEMVY KGKLTAGEAT PINLTNHSYF
NLNKPYGDTI EGTEIMVRSK KSVDVDKNMI PTGNIVDREI ATFNSTKPTV LGPKNPQFDC
CFVVDENAKP SQINTLNNEL TLIVKAFHPD SNITLEVLST EPTYQFYTGD FLSAGYEARQ
GFAIEPGRYI DAINQENWKD CVTLKNGETY GSKIVYRFS
