UGPA_PIG
ID UGPA_PIG Reviewed; 508 AA.
AC P79303;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=UTP--glucose-1-phosphate uridylyltransferase;
DE EC=2.7.7.9 {ECO:0000250|UniProtKB:Q16851};
DE AltName: Full=UDP-glucose pyrophosphorylase;
DE Short=UDPGP;
DE Short=UGPase;
GN Name=UGP2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RA Looft C., Paul S.;
RT "cDNA sequencing of the porcine UDP glucose pyrophosphorylase gene.";
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: UTP--glucose-1-phosphate uridylyltransferase catalyzing the
CC conversion of glucose-1-phosphate into UDP-glucose, a crucial precursor
CC for the production of glycogen. {ECO:0000250|UniProtKB:Q16851}.
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:0000250|UniProtKB:Q16851};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19890;
CC Evidence={ECO:0000250|UniProtKB:Q16851};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000250|UniProtKB:Q16851}.
CC -!- SUBUNIT: Homooctamer. {ECO:0000250|UniProtKB:Q16851}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16851}.
CC -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR EMBL; X99312; CAA67690.1; -; mRNA.
DR RefSeq; NP_999145.1; NM_213980.1.
DR STRING; 9823.ENSSSCP00000008931; -.
DR PaxDb; P79303; -.
DR PeptideAtlas; P79303; -.
DR PRIDE; P79303; -.
DR GeneID; 397040; -.
DR KEGG; ssc:397040; -.
DR CTD; 7360; -.
DR eggNOG; KOG2638; Eukaryota.
DR InParanoid; P79303; -.
DR OrthoDB; 503037at2759; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IBA:GO_Central.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0005977; P:glycogen metabolic process; IBA:GO_Central.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IBA:GO_Central.
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 Acetylation; Cytoplasm; Magnesium; Metal-binding; Nucleotidyltransferase;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..508
FT /note="UTP--glucose-1-phosphate uridylyltransferase"
FT /id="PRO_0000185754"
FT REGION 457..508
FT /note="Oligomerization"
FT /evidence="ECO:0000250"
FT REGION 502..503
FT /note="Critical for end-to-end subunit interaction"
FT /evidence="ECO:0000250"
FT ACT_SITE 396
FT /evidence="ECO:0000250"
FT BINDING 113..116
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 115..116
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 190
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 222
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 251..253
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 396
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT MOD_RES 426
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT MOD_RES 438
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
SQ SEQUENCE 508 AA; 56953 MW; 327F66CD91783965 CRC64;
MSRFVQDLSK AMSQDGASQF QEVIRQELEL SVKKELEKIL TTAPSHEFEH TKKDLDGFRK
LFHRFLQEKG PSVDWGKIQR PPEDSIQPYE KIKARGLPDN ISSVLNKLVV VKLNGGLGTS
MGCKGPKSLI GVRNENTFLD LTVQQIEHLN KTYNTDVPLV LMNSFNTDED TKKILQKYNH
CRVKIYTFNQ SRYPRINKES LLPVAKDVSY SGENTEAWYP PGHGDIYASF YNSGLLDTFI
GEGKEYIFVS NIDNLGATVD LYILNHLMNP PNGRPCEFVM EATNKARADV KGGTLTQYEG
KLRLVEIAQV PKPHVDEFKS VSKFKIFNTN NLWISLAAVK RLQEQNAIDM EIIVNPKTLD
GGLNVIQLET AVGAAIKSFE NSLGINVPRS RFLPVKTTSD LLLVMSNLYS LNAGSLTMSE
KREFPTVPLV KLGSSFTKVQ DYLRRFESIP DMLELDHLTV SGDVTFGKNV SLKGTVIIIX
NHGDRIDIPP GAVLENKIVS GNLRILDH
