GAL7_YEAST
ID GAL7_YEAST Reviewed; 366 AA.
AC P08431; D6VQ20; P04398;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Galactose-1-phosphate uridylyltransferase;
DE Short=Gal-1-P uridylyltransferase;
DE EC=2.7.7.12 {ECO:0000250|UniProtKB:P09148};
DE AltName: Full=UDP-glucose--hexose-1-phosphate uridylyltransferase;
GN Name=GAL7; OrderedLocusNames=YBR018C; ORFNames=YBR0226;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [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 1-185.
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 1-21, AND PROTEIN SEQUENCE OF 2-8.
RX PubMed=6324089; DOI=10.1093/nar/11.24.8555;
RA Nogi Y., Fukasawa T.;
RT "Nucleotide sequence of the transcriptional initiation region of the yeast
RT GAL7 gene.";
RL Nucleic Acids Res. 11:8555-8568(1983).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, 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 1-phosphate + UDP-alpha-D-glucose = alpha-D-
CC glucose 1-phosphate + UDP-alpha-D-galactose; Xref=Rhea:RHEA:13989,
CC ChEBI:CHEBI:58336, ChEBI:CHEBI:58601, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:66914; EC=2.7.7.12;
CC Evidence={ECO:0000250|UniProtKB:P09148};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P09148};
CC Note=Binds 1 zinc ion per subunit. Zinc binding seems to play a
CC structural role. {ECO:0000250|UniProtKB:P09148};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P07902}.
CC -!- SIMILARITY: Belongs to the galactose-1-phosphate uridylyltransferase
CC type 1 family. {ECO:0000305}.
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DR EMBL; X81324; CAA57105.1; -; Genomic_DNA.
DR EMBL; M12348; AAA34627.1; -; Genomic_DNA.
DR EMBL; X00215; CAA25039.1; -; Genomic_DNA.
DR EMBL; Z35887; CAA84960.1; -; Genomic_DNA.
DR EMBL; K01752; AAA34628.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07140.1; -; Genomic_DNA.
DR PIR; S45873; XNBYUG.
DR RefSeq; NP_009574.1; NM_001178366.1.
DR AlphaFoldDB; P08431; -.
DR SMR; P08431; -.
DR BioGRID; 32721; 126.
DR DIP; DIP-5357N; -.
DR IntAct; P08431; 22.
DR MINT; P08431; -.
DR STRING; 4932.YBR018C; -.
DR iPTMnet; P08431; -.
DR MaxQB; P08431; -.
DR PaxDb; P08431; -.
DR PRIDE; P08431; -.
DR EnsemblFungi; YBR018C_mRNA; YBR018C; YBR018C.
DR GeneID; 852306; -.
DR KEGG; sce:YBR018C; -.
DR SGD; S000000222; GAL7.
DR VEuPathDB; FungiDB:YBR018C; -.
DR eggNOG; KOG2958; Eukaryota.
DR GeneTree; ENSGT00390000016188; -.
DR HOGENOM; CLU_029960_0_0_1; -.
DR InParanoid; P08431; -.
DR OMA; HAIYYPP; -.
DR BioCyc; YEAST:YBR018C-MON; -.
DR UniPathway; UPA00214; -.
DR PRO; PR:P08431; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P08431; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0008108; F:UDP-glucose:hexose-1-phosphate uridylyltransferase activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IDA:SGD.
DR CDD; cd00608; GalT; 1.
DR Gene3D; 3.30.428.10; -; 2.
DR InterPro; IPR001937; GalP_UDPtransf1.
DR InterPro; IPR019779; GalP_UDPtransf1_His-AS.
DR InterPro; IPR005850; GalP_Utransf_C.
DR InterPro; IPR005849; GalP_Utransf_N.
DR InterPro; IPR036265; HIT-like_sf.
DR PANTHER; PTHR11943; PTHR11943; 1.
DR Pfam; PF02744; GalP_UDP_tr_C; 1.
DR Pfam; PF01087; GalP_UDP_transf; 1.
DR PIRSF; PIRSF000808; GalT; 1.
DR SUPFAM; SSF54197; SSF54197; 2.
DR TIGRFAMs; TIGR00209; galT_1; 1.
DR PROSITE; PS00117; GAL_P_UDP_TRANSF_I; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Galactose metabolism;
KW Iron; Metal-binding; Nucleotidyltransferase; Phosphoprotein;
KW Reference proteome; Transferase; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6324089"
FT CHAIN 2..366
FT /note="Galactose-1-phosphate uridylyltransferase"
FT /id="PRO_0000169893"
FT ACT_SITE 182
FT /note="Tele-UMP-histidine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 63
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07902"
FT BINDING 79..80
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07902"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 169
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P07902"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10033"
FT BINDING 184
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07902"
FT BINDING 198
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 297
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 314
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 316
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P09148"
FT BINDING 329..332
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07902"
FT BINDING 334..335
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P07902"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 11
FT /note="H -> Y (in Ref. 5; AAA34628)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="P -> H (in Ref. 5; AAA34628)"
FT /evidence="ECO:0000305"
FT CONFLICT 85..86
FT /note="RL -> S (in Ref. 1; AAA34627)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="V -> A (in Ref. 1; AAA34627)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="T -> I (in Ref. 1; AAA34627)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 366 AA; 42385 MW; 960F75532D2621DC CRC64;
MTAEEFDFSS HSHRRYNPLT DSWILVSPHR AKRPWLGQQE AAYKPTAPLY DPKCYLCPGN
KRATGNLNPR YESTYIFPND YAAVRLDQPI LPQNDSNEDN LKNRLLKVQS VRGNCFVICF
SPNHNLTIPQ MKQSDLVHIV NSWQALTDDL SREARENHKP FKYVQIFENK GTAMGCSNLH
PHGQAWCLES IPSEVSQELK SFDKYKREHN TDLFADYVKL ESREKSRVVV ENESFIVVVP
YWAIWPFETL VISKKKLASI SQFNQMVKED LASILKQLTI KYDNLFETSF PYSMGIHQAP
LNATGDELSN SWFHMHFYPP LLRSATVRKF LVGFELLGEP QRDLTSEQAA EKLRNLDGQI
HYLQRL
