UAP1_YEAST
ID UAP1_YEAST Reviewed; 477 AA.
AC P43123; D6VRP7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase {ECO:0000303|PubMed:9603950};
DE EC=2.7.7.23 {ECO:0000269|PubMed:9603950};
GN Name=QRI1; Synonyms=UAP1 {ECO:0000303|PubMed:9603950};
GN OrderedLocusNames=YDL103C; ORFNames=D2362;
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], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-111; GLY-112; GLY-114;
RP THR-115; ARG-116; LEU-117; PRO-122 AND LYS-123, AND PATHWAY.
RC STRAIN=ATCC 200589 / A451;
RX PubMed=9603950; DOI=10.1074/jbc.273.23.14392;
RA Mio T., Yabe T., Arisawa M., Yamada-Okabe H.;
RT "The eukaryotic UDP-N-acetylglucosamine pyrophosphorylases: gene cloning,
RT protein expression, and catalytic mechanism.";
RL J. Biol. Chem. 273:14392-14397(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7725801; DOI=10.1002/yea.320101215;
RA Simon M., Benit P., Vassal A., Dubois C., Faye G.;
RT "Sequence of the PHO2-POL3 (CDC2) region of chromosome IV of Saccharomyces
RT cerevisiae.";
RL Yeast 10:1653-1656(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896274;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1077::aid-yea8>3.0.co;2-z;
RA Saiz J.E., Buitrago M.J., Garcia R., Revuelta J.L., del Rey F.;
RT "The sequence of a 20.3 kb DNA fragment from the left arm of Saccharomyces
RT cerevisiae chromosome IV contains the KIN28, MSS2, PHO2, POL3 and DUN1
RT genes, and six new open reading frames.";
RL Yeast 12:1077-1084(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [5]
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 [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, 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: UDP-N-acetylglucosamine pyrophosphorylase that utilizes N-
CC acetylglucosamine-1-phosphate as substrate (PubMed:9603950). Together
CC with AGM1, is involved in the production of UDP-N-acetylglucosamine
CC from N-acetylglucosamine-6-phosphate (PubMed:9603950).
CC {ECO:0000269|PubMed:9603950}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP =
CC diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23;
CC Evidence={ECO:0000269|PubMed:9603950};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.51 uM for N-acetyl-alpha-D-glucosamine 1-phosphate
CC {ECO:0000269|PubMed:9603950};
CC KM=20.58 uM for UTP {ECO:0000269|PubMed:9603950};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-
CC acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
CC {ECO:0000269|PubMed:9603950}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 5480 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR EMBL; AB011272; BAA31203.1; -; Genomic_DNA.
DR EMBL; X79380; CAA55927.1; -; Genomic_DNA.
DR EMBL; X95644; CAA64910.1; -; Genomic_DNA.
DR EMBL; Z74151; CAA98670.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11757.1; -; Genomic_DNA.
DR PIR; S50738; S50738.
DR RefSeq; NP_010180.1; NM_001180162.1.
DR AlphaFoldDB; P43123; -.
DR SMR; P43123; -.
DR BioGRID; 31959; 423.
DR DIP; DIP-2837N; -.
DR IntAct; P43123; 1.
DR MINT; P43123; -.
DR STRING; 4932.YDL103C; -.
DR iPTMnet; P43123; -.
DR MaxQB; P43123; -.
DR PaxDb; P43123; -.
DR PRIDE; P43123; -.
DR EnsemblFungi; YDL103C_mRNA; YDL103C; YDL103C.
DR GeneID; 851455; -.
DR KEGG; sce:YDL103C; -.
DR SGD; S000002261; QRI1.
DR VEuPathDB; FungiDB:YDL103C; -.
DR eggNOG; KOG2388; Eukaryota.
DR GeneTree; ENSGT00940000153464; -.
DR HOGENOM; CLU_025603_1_1_1; -.
DR InParanoid; P43123; -.
DR OMA; QPDVLKF; -.
DR BioCyc; MetaCyc:YDL103C-MON; -.
DR BioCyc; YEAST:YDL103C-MON; -.
DR BRENDA; 2.7.7.23; 984.
DR Reactome; R-SCE-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR SABIO-RK; P43123; -.
DR UniPathway; UPA00113; UER00533.
DR PRO; PR:P43123; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P43123; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IDA:SGD.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IDA:SGD.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR039741; UDP-sugar_pyrophosphorylase.
DR InterPro; IPR002618; UDPGP_fam.
DR PANTHER; PTHR11952; PTHR11952; 1.
DR Pfam; PF01704; UDPGP; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleotidyltransferase; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..477
FT /note="UDP-N-acetylglucosamine pyrophosphorylase"
FT /id="PRO_0000185773"
FT MOTIF 109..112
FT /note="Substrate binding"
FT /evidence="ECO:0000250|UniProtKB:Q16222"
FT MOTIF 302..303
FT /note="Substrate binding"
FT /evidence="ECO:0000250|UniProtKB:Q16222"
FT BINDING 109..112
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 123
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 194
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 221
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16222"
FT BINDING 252
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 377
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 409
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16222"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 111
FT /note="G->A: Decrease of activity."
FT /evidence="ECO:0000269|PubMed:9603950"
FT MUTAGEN 112
FT /note="G->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9603950"
FT MUTAGEN 114
FT /note="G->A: Decrease of activity."
FT /evidence="ECO:0000269|PubMed:9603950"
FT MUTAGEN 115
FT /note="T->A: Decrease of activity."
FT /evidence="ECO:0000269|PubMed:9603950"
FT MUTAGEN 116
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9603950"
FT MUTAGEN 117
FT /note="L->A: Decrease of activity."
FT /evidence="ECO:0000269|PubMed:9603950"
FT MUTAGEN 122
FT /note="P->A: Decrease of activity."
FT /evidence="ECO:0000269|PubMed:9603950"
FT MUTAGEN 123
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9603950"
SQ SEQUENCE 477 AA; 53476 MW; 2D656E31C17805FD CRC64;
MTDTKQLFIE AGQSQLFHNW ESLSRKDQEE LLSNLEQISS KRSPAKLLED CQNAIKFSLA
NSSKDTGVEI SPLPPTSYES LIGNSKKENE YWRLGLEAIG KGEVAVILMA GGQGTRLGSS
QPKGCYDIGL PSKKSLFQIQ AEKLIRLQDM VKDKKVEIPW YIMTSGPTRA ATEAYFQEHN
YFGLNKEQIT FFNQGTLPAF DLTGKHFLMK DPVNLSQSPD GNGGLYRAIK ENKLNEDFDR
RGIKHVYMYC VDNVLSKIAD PVFIGFAIKH GFELATKAVR KRDAHESVGL IATKNEKPCV
IEYSEISNEL AEAKDKDGLL KLRAGNIVNH YYLVDLLKRD LDQWCENMPY HIAKKKIPAY
DSVTGKYTKP TEPNGIKLEQ FIFDVFDTVP LNKFGCLEVD RCKEFSPLKN GPGSKNDNPE
TSRLAYLKLG TSWLEDAGAI VKDGVLVEVS SKLSYAGENL SQFKGKVFDR SGIVLEK
