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UGPA_PYRPY
ID   UGPA_PYRPY              Reviewed;         471 AA.
AC   O64459;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=UTP--glucose-1-phosphate uridylyltransferase;
DE            EC=2.7.7.9;
DE   AltName: Full=UDP-glucose pyrophosphorylase;
DE            Short=UDPGP;
DE            Short=UGPase;
OS   Pyrus pyrifolia (Chinese pear) (Pyrus serotina).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Pyrus.
OX   NCBI_TaxID=3767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Nijisseiki; TISSUE=Pollen;
RA   Kiyozumi D., Ishimizu T., Nakanishi T., Sakiyama F., Norioka S.;
RT   "Molecular cloning and nucleotide sequencing of a cDNA encoding UDP-glucose
RT   pyrophosphorylase of Japanese pear (Pyrus pyrifolia Nakai).";
RL   (er) Plant Gene Register PGR99-006(1999).
CC   -!- FUNCTION: Plays a central role as a glucosyl donor in cellular
CC       metabolic pathways.
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.
CC   -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR   EMBL; AB013353; BAA25917.1; -; mRNA.
DR   AlphaFoldDB; O64459; -.
DR   SMR; O64459; -.
DR   PRIDE; O64459; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cytoplasm; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..471
FT                   /note="UTP--glucose-1-phosphate uridylyltransferase"
FT                   /id="PRO_0000185761"
FT   BINDING         87..90
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         89..90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         101
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         164
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         193
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         222..224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         224
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         362
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
SQ   SEQUENCE   471 AA;  51845 MW;  CE5523CE35E13B40 CRC64;
     MAAVATGNVD KLKSDVASLS QISENEKNGF INLVSRYVSG EEAQHVEWSK IQTPTDEVVV
     PYDGLAPTPE DPEEIKKLLD KLVVLKLNGG LGTTMGCTGP KSVIEVRNGL TFLDLIVIQI
     ENLNNKYGSC VPLLLMNSFN THDDTQKIVE KYSKSNVQIH TFNQSQYPRL VVEDFSPLPS
     KGQTGKDGWY PPGHGDVFPS LKNSGKLDLL LSQGKEYVFI ANSDNLGAVV DLKILHHLIQ
     KKNEYCMEVT PKTLADVKGG TLISYEGRVQ LLEIAQVPDQ HVNEFKSIEK FKIFNTNNLW
     VNLNAIKRLV EADALKMEII PNPKEVDGVK VLQLETAAGA AIRFFNHAIG INVPRSRFLP
     VKATSDLLLV QSDLYTLQDG FVTRNSARKN PENPTIELGP EFKKVGSYLS RFKSIPSILE
     LESLKVSGDV WFGAGVVLKG KVTITAKSGV KLEIPDNAVI ANKDINGPED L
 
 
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