UGPA2_SCHPO
ID UGPA2_SCHPO Reviewed; 499 AA.
AC O59819; Q9UTZ5;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
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 ORFNames=SPCC794.10;
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 GENOMIC DNA] OF 44-252, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
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).
CC -!- FUNCTION: Plays a central role as a glucosyl donor in cellular
CC metabolic pathways. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10759889}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329672; CAA19137.1; -; Genomic_DNA.
DR EMBL; AB027910; BAA87214.1; -; Genomic_DNA.
DR PIR; T41618; T41618.
DR RefSeq; NP_587758.1; NM_001022751.2.
DR AlphaFoldDB; O59819; -.
DR SMR; O59819; -.
DR BioGRID; 276144; 2.
DR STRING; 4896.SPCC794.10.1; -.
DR iPTMnet; O59819; -.
DR MaxQB; O59819; -.
DR PaxDb; O59819; -.
DR PRIDE; O59819; -.
DR EnsemblFungi; SPCC794.10.1; SPCC794.10.1:pep; SPCC794.10.
DR GeneID; 2539585; -.
DR KEGG; spo:SPCC794.10; -.
DR PomBase; SPCC794.10; -.
DR VEuPathDB; FungiDB:SPCC794.10; -.
DR eggNOG; KOG2638; Eukaryota.
DR HOGENOM; CLU_023632_3_0_1; -.
DR InParanoid; O59819; -.
DR OMA; YRRYLLH; -.
DR PhylomeDB; O59819; -.
DR PRO; PR:O59819; -.
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:0070569; F:uridylyltransferase activity; IEA:InterPro.
DR GO; GO:0005977; P:glycogen metabolic process; IBA:GO_Central.
DR GO; GO:0006011; P:UDP-glucose metabolic process; ISO: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 3: Inferred from homology;
KW Cytoplasm; Nucleotidyltransferase; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..499
FT /note="Probable UTP--glucose-1-phosphate
FT uridylyltransferase"
FT /id="PRO_0000185764"
FT BINDING 108..111
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 110..111
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 122
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 185
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 214
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 243..245
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 245
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 387
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
SQ SEQUENCE 499 AA; 56740 MW; 8DE4ABC3EC212A60 CRC64;
MLHRRIHFKS QSTLDFDSVA VSISASTMKN ELDKLVLNSR VSDKKTFGIQ MDNFFALYRR
YLLHTVKGYE CDWDSIRPLG PEDMIDYGDL PLCKNAGKYL NRLAVVKLNG GMGNALGVNY
PKAMIEVRDN QSFLDLSIRQ IEYLNRRYDV SVPFILMNSY DTNDETCKVL RKYAGCKIDI
STFEQSRYPR VFVDSQLPVP KAAPSPIEEW YPPGHGDIFD ALVHSGTIER LLAQGKDYLF
VSNIDNLGAS VDLNILSHVI DNQIEYSMEI TDKTKADIKV GILVNQDGLL RLLETNQVPE
QHREEFMSDK VFKYINTNNV WLYLPAVKRV VENRELNLDI MPNIETVYYN NEPARIIEFT
TAIGSAISQF KKTEGIRVSR PRFISVKNSS DLFLVRCDLY NVDHGSLKIE ESRLGFPPPV
VRMSNEFKDI AELFCRIPYM PSMKDLVSLS ISGNVYFGRN VILKGNIVIV ASENTILCIP
SNAVLENCVV TGNCKIMEC
