UGPA1_SCHPO
ID UGPA1_SCHPO Reviewed; 506 AA.
AC P78811;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable UTP--glucose-1-phosphate uridylyltransferase;
DE EC=2.7.7.9;
DE AltName: Full=UDP-glucose pyrophosphorylase;
DE Short=UDPGP;
DE Short=UGPase;
GN Name=fyu1; ORFNames=SPCC1322.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 203-506.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-17, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [5]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=21862693; DOI=10.1124/dmd.111.041640;
RA Buchheit D., Dragan C.A., Schmitt E.I., Bureik M.;
RT "Production of ibuprofen acyl glucosides by human UGT2B7.";
RL Drug Metab. Dispos. 39:2174-2181(2011).
CC -!- FUNCTION: Plays a central role as a glucosyl donor in cellular
CC metabolic pathways. {ECO:0000269|PubMed:21862693}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-
CC alpha-D-glucose; Xref=Rhea:RHEA:19889, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:58601,
CC ChEBI:CHEBI:58885; EC=2.7.7.9;
CC Evidence={ECO:0000269|PubMed:21862693};
CC -!- SUBUNIT: Homooctamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR EMBL; CU329672; CAA22857.1; -; Genomic_DNA.
DR EMBL; D89160; BAA13822.1; -; mRNA.
DR PIR; T40935; T40935.
DR PIR; T42521; T42521.
DR RefSeq; NP_588132.1; NM_001023122.2.
DR AlphaFoldDB; P78811; -.
DR SMR; P78811; -.
DR BioGRID; 275456; 6.
DR STRING; 4896.SPCC1322.04.1; -.
DR iPTMnet; P78811; -.
DR MaxQB; P78811; -.
DR PaxDb; P78811; -.
DR PRIDE; P78811; -.
DR EnsemblFungi; SPCC1322.04.1; SPCC1322.04.1:pep; SPCC1322.04.
DR GeneID; 2538877; -.
DR KEGG; spo:SPCC1322.04; -.
DR PomBase; SPCC1322.04; fyu1.
DR VEuPathDB; FungiDB:SPCC1322.04; -.
DR eggNOG; KOG2638; Eukaryota.
DR HOGENOM; CLU_023632_3_0_1; -.
DR InParanoid; P78811; -.
DR OMA; TNNLWAK; -.
DR PhylomeDB; P78811; -.
DR Reactome; R-SPO-173599; Formation of the active cofactor, UDP-glucuronate.
DR Reactome; R-SPO-3322077; Glycogen synthesis.
DR PRO; PR:P78811; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IMP:PomBase.
DR GO; GO:0005977; P:glycogen metabolic process; IBA:GO_Central.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IMP:PomBase.
DR CDD; cd00897; UGPase_euk; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR002618; UDPGP_fam.
DR InterPro; IPR016267; UDPGP_trans.
DR PANTHER; PTHR43511; PTHR43511; 1.
DR Pfam; PF01704; UDPGP; 1.
DR PIRSF; PIRSF000806; UDPGP; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..506
FT /note="Probable UTP--glucose-1-phosphate
FT uridylyltransferase"
FT /id="PRO_0000185763"
FT REGION 455..506
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT ACT_SITE 394
FT /evidence="ECO:0000250"
FT BINDING 115..118
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 117..118
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 192
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:Q16851"
FT BINDING 250..252
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 394
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 506 AA; 56430 MW; CC4B7EF856D25630 CRC64;
MDLAPRPLGR QHSKSQSAFA FDNTATSIAA STMKNELNHL ASTVKDPLAK KAFQKEMDNF
FSLFSRYLQE DARGSEINWD LVESPKPEQV VEYDTITEAG GLSRDYLNKL AVLKLNGGLG
TTMGCVGPKS IIEVRDGNSF LDLSVRQIEH LNRKYNVNVP FVLMNSFNTD EATAKVIKKY
EAHKIDILTF NQSRYPRVHK ETLLPVPHTA DSAIDEWYPP GHGDVFEALT NSGIIDTLIA
QGKEYLFVSN IDNLGAVVDL NILNHMVETN AEYLMELTNK TKADVKGGTL IDYDGNVRLL
EIAQVPPQHV EEFKSIKKFK YFNTNNLWFH LPSVKRVVNN HELSMEIIPN KKTIKHKGEN
INIIQLETAA GAAIRHFKNA HGVNVPRRRF LPVKTCSDLL LVKSDLYSIN HGQVEMNPRR
FGGTAPLVKL GAHFKKVADF SAHIPSIPKI LELDHLTITG DVNIGRNVTL KGTVIIVASD
ANRIDIPNGS VLENCVITGN LNILEH
