GAL1_YEAST
ID GAL1_YEAST Reviewed; 528 AA.
AC P04385; D6VQ22;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Galactokinase;
DE EC=2.7.1.6;
DE AltName: Full=Galactose kinase;
GN Name=GAL1; OrderedLocusNames=YBR020W; ORFNames=YBR0302;
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 [GENOMIC DNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
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 [6]
RP PROTEIN SEQUENCE OF 2-12.
RX PubMed=200486; DOI=10.1016/0014-5793(77)80638-8;
RA Schlesinger D.H., Schell M.A., Wilson D.B.;
RT "The NH2-terminal sequences of galactokinase from Escherichia coli and
RT Saccharomyces cerevisiae.";
RL FEBS Lett. 83:45-47(1977).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, 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).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-galactose + ATP = ADP + alpha-D-galactose 1-phosphate
CC + H(+); Xref=Rhea:RHEA:13553, ChEBI:CHEBI:15378, ChEBI:CHEBI:28061,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58336, ChEBI:CHEBI:456216; EC=2.7.1.6;
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC -!- INTERACTION:
CC P04385; P04387: GAL80; NbExp=2; IntAct=EBI-7272, EBI-2061197;
CC -!- SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily.
CC {ECO:0000305}.
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DR EMBL; K01609; AAA34631.1; -; Genomic_DNA.
DR EMBL; X76078; CAA53677.1; -; Genomic_DNA.
DR EMBL; Z35889; CAA84962.1; -; Genomic_DNA.
DR EMBL; K02115; AAA34621.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07142.1; -; Genomic_DNA.
DR PIR; S45876; KIBYGG.
DR RefSeq; NP_009576.1; NM_001178368.1.
DR PDB; 2AJ4; X-ray; 2.40 A; A/B=2-528.
DR PDBsum; 2AJ4; -.
DR AlphaFoldDB; P04385; -.
DR SMR; P04385; -.
DR BioGRID; 32723; 90.
DR ComplexPortal; CPX-1043; GAL1-GAL80 transcription regulation complex.
DR DIP; DIP-2333N; -.
DR IntAct; P04385; 99.
DR STRING; 4932.YBR020W; -.
DR iPTMnet; P04385; -.
DR PaxDb; P04385; -.
DR PRIDE; P04385; -.
DR EnsemblFungi; YBR020W_mRNA; YBR020W; YBR020W.
DR GeneID; 852308; -.
DR KEGG; sce:YBR020W; -.
DR SGD; S000000224; GAL1.
DR VEuPathDB; FungiDB:YBR020W; -.
DR eggNOG; KOG0631; Eukaryota.
DR GeneTree; ENSGT00950000183187; -.
DR HOGENOM; CLU_017814_6_2_1; -.
DR InParanoid; P04385; -.
DR OMA; PVCYNLR; -.
DR BioCyc; YEAST:YBR020W-MON; -.
DR UniPathway; UPA00214; -.
DR EvolutionaryTrace; P04385; -.
DR PRO; PR:P04385; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P04385; protein.
DR GO; GO:0005737; C:cytoplasm; IGI:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004335; F:galactokinase activity; IDA:SGD.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IDA:SGD.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IDA:SGD.
DR GO; GO:0006012; P:galactose metabolic process; IBA:GO_Central.
DR GO; GO:0000411; P:positive regulation of transcription by galactose; IGI:SGD.
DR GO; GO:0000435; P:positive regulation of transcription from RNA polymerase II promoter by galactose; IC:ComplexPortal.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR000705; Galactokinase.
DR InterPro; IPR019741; Galactokinase_CS.
DR InterPro; IPR019539; GalKase_N.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR InterPro; IPR006206; Mevalonate/galactokinase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR Pfam; PF10509; GalKase_gal_bdg; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF000530; Galactokinase; 1.
DR PRINTS; PR00473; GALCTOKINASE.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR00131; gal_kin; 1.
DR PROSITE; PS00106; GALACTOKINASE; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism;
KW Direct protein sequencing; Galactose metabolism; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:200486"
FT CHAIN 2..528
FT /note="Galactokinase"
FT /id="PRO_0000184657"
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 163..173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT SITE 53
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 6
FT /note="S -> R (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="V -> I (in Ref. 1; AAA34631)"
FT /evidence="ECO:0000305"
FT CONFLICT 206..239
FT /note="EHYVGVNNGGMDQAASVCGEEDHALYVEFKPQLK -> DIMLVLTMAVWIRL
FT PLFAVRKIMLYTLSSNAVE (in Ref. 1; AAA34631)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="L -> P (in Ref. 1; AAA34631)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="A -> V (in Ref. 1; AAA34631)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="N -> NN (in Ref. 1; AAA34631)"
FT /evidence="ECO:0000305"
FT HELIX 23..40
FT /evidence="ECO:0007829|PDB:2AJ4"
FT STRAND 45..57
FT /evidence="ECO:0007829|PDB:2AJ4"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:2AJ4"
FT STRAND 68..84
FT /evidence="ECO:0007829|PDB:2AJ4"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:2AJ4"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:2AJ4"
FT HELIX 123..141
FT /evidence="ECO:0007829|PDB:2AJ4"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:2AJ4"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:2AJ4"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:2AJ4"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:2AJ4"
FT HELIX 170..187
FT /evidence="ECO:0007829|PDB:2AJ4"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:2AJ4"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:2AJ4"
FT HELIX 216..223
FT /evidence="ECO:0007829|PDB:2AJ4"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:2AJ4"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:2AJ4"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:2AJ4"
FT STRAND 252..259
FT /evidence="ECO:0007829|PDB:2AJ4"
FT TURN 266..273
FT /evidence="ECO:0007829|PDB:2AJ4"
FT HELIX 274..291
FT /evidence="ECO:0007829|PDB:2AJ4"
FT HELIX 310..322
FT /evidence="ECO:0007829|PDB:2AJ4"
FT HELIX 332..350
FT /evidence="ECO:0007829|PDB:2AJ4"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:2AJ4"
FT HELIX 359..366
FT /evidence="ECO:0007829|PDB:2AJ4"
FT HELIX 370..378
FT /evidence="ECO:0007829|PDB:2AJ4"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:2AJ4"
FT HELIX 390..412
FT /evidence="ECO:0007829|PDB:2AJ4"
FT HELIX 419..439
FT /evidence="ECO:0007829|PDB:2AJ4"
FT HELIX 446..457
FT /evidence="ECO:0007829|PDB:2AJ4"
FT STRAND 461..465
FT /evidence="ECO:0007829|PDB:2AJ4"
FT STRAND 470..481
FT /evidence="ECO:0007829|PDB:2AJ4"
FT HELIX 486..496
FT /evidence="ECO:0007829|PDB:2AJ4"
FT HELIX 498..501
FT /evidence="ECO:0007829|PDB:2AJ4"
FT HELIX 507..513
FT /evidence="ECO:0007829|PDB:2AJ4"
FT STRAND 514..517
FT /evidence="ECO:0007829|PDB:2AJ4"
FT STRAND 523..527
FT /evidence="ECO:0007829|PDB:2AJ4"
SQ SEQUENCE 528 AA; 57944 MW; 1DA31A1915C19107 CRC64;
MTKSHSEEVI VPEFNSSAKE LPRPLAEKCP SIIKKFISAY DAKPDFVARS PGRVNLIGEH
IDYCDFSVLP LAIDFDMLCA VKVLNEKNPS ITLINADPKF AQRKFDLPLD GSYVTIDPSV
SDWSNYFKCG LHVAHSFLKK LAPERFASAP LAGLQVFCEG DVPTGSGLSS SAAFICAVAL
AVVKANMGPG YHMSKQNLMR ITVVAEHYVG VNNGGMDQAA SVCGEEDHAL YVEFKPQLKA
TPFKFPQLKN HEISFVIANT LVVSNKFETA PTNYNLRVVE VTTAANVLAA TYGVVLLSGK
EGSSTNKGNL RDFMNVYYAR YHNISTPWNG DIESGIERLT KMLVLVEESL ANKKQGFSVD
DVAQSLNCSR EEFTRDYLTT SPVRFQVLKL YQRAKHVYSE SLRVLKAVKL MTTASFTADE
DFFKQFGALM NESQASCDKL YECSCPEIDK ICSIALSNGS YGSRLTGAGW GGCTVHLVPG
GPNGNIEKVK EALANEFYKV KYPKITDAEL ENAIIVSKPA LGSCLYEL
