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}.
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; 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