ID   UGPA2_DICDI             Reviewed;         502 AA.
AC   Q54YZ0; Q27566; Q9XZN2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=UTP--glucose-1-phosphate uridylyltransferase 2;
DE            EC=2.7.7.9;
DE   AltName: Full=UDP-glucose pyrophosphorylase 2;
DE            Short=UDPGP 2;
DE            Short=UGPase 2;
GN   Name=ugpB; ORFNames=DDB_G0277879;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=AX4;
RX   PubMed=12060658; DOI=10.1074/jbc.m204245200;
RA   Bishop J.D., Moon B.C., Harrow F., Ratner D., Gomer R.H., Dottin R.P.,
RA   Brazill D.T.;
RT   "A second UDP-glucose pyrophosphorylase is required for differentiation and
RT   development in Dictyostelium discoideum.";
RL   J. Biol. Chem. 277:32430-32437(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 319-370.
RA   Moon B.C., Haribabu B., Dottin R.P.;
RT   "Null mutation of a UDPGP-glucose pyrophosphorylase gene by homologous
RT   recombination provides evidence for a second gene in Dictyostelium
RT   discoideum.";
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a central role as a glucosyl donor in cellular
CC       metabolic pathways. {ECO:0000269|PubMed:12060658}.
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   -!- DEVELOPMENTAL STAGE: Expressed in both prestalk and prespore cells.
CC       Expression becomes strong after 12 hours of development and peaks at 16
CC       hours. {ECO:0000269|PubMed:12060658}.
CC   -!- DISRUPTION PHENOTYPE: Cells undergo aberrant differentiation and
CC       development ending with small, gnarled fruiting bodies. They also have
CC       decreased spore viability and decreased levels of glycogen.
CC       {ECO:0000269|PubMed:12060658}.
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; AF150929; AAD34028.1; -; mRNA.
DR   EMBL; AAFI02000023; EAL68112.1; -; Genomic_DNA.
DR   EMBL; L28007; AAA91057.1; -; Genomic_DNA.
DR   RefSeq; XP_642062.1; XM_636970.1.
DR   AlphaFoldDB; Q54YZ0; -.
DR   SMR; Q54YZ0; -.
DR   STRING; 44689.Q54YZ0; -.
DR   PaxDb; 44689-DDB0214911; -.
DR   EnsemblProtists; EAL68112; EAL68112; DDB_G0277879.
DR   GeneID; 8621274; -.
DR   KEGG; ddi:DDB_G0277879; -.
DR   dictyBase; DDB_G0277879; ugpB.
DR   eggNOG; KOG2638; Eukaryota.
DR   HOGENOM; CLU_023632_3_0_1; -.
DR   InParanoid; Q54YZ0; -.
DR   OMA; KEYCFLS; -.
DR   PhylomeDB; Q54YZ0; -.
DR   Reactome; R-DDI-173599; Formation of the active cofactor, UDP-glucuronate.
DR   Reactome; R-DDI-3322077; Glycogen synthesis.
DR   PRO; PR:Q54YZ0; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR   GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IDA:dictyBase.
DR   GO; GO:0000045; P:autophagosome assembly; IMP:dictyBase.
DR   GO; GO:0030244; P:cellulose biosynthetic process; IMP:dictyBase.
DR   GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR   GO; GO:0005977; P:glycogen metabolic process; IMP:dictyBase.
DR   GO; GO:0006011; P:UDP-glucose metabolic process; IBA:GO_Central.
DR   CDD; cd00897; UGPase_euk; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR002618; UDPGP_fam.
DR   InterPro; IPR016267; UDPGP_trans.
DR   PANTHER; PTHR43511; -; 1.
DR   PANTHER; PTHR43511:SF4; UTP--GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; 1.
DR   Pfam; PF01704; UDPGP; 1.
DR   PIRSF; PIRSF000806; UDPGP; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   2: Evidence at transcript level;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..502
FT                   /note="UTP--glucose-1-phosphate uridylyltransferase 2"
FT                   /id="PRO_0000327942"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         114..117
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         116..117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         128
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         191
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         220
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         249..251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         251
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         390
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   CONFLICT        18
FT                   /note="A -> S (in Ref. 1; AAD34028)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        320
FT                   /note="I -> V (in Ref. 3; AAA91057)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        363..364
FT                   /note="EI -> RL (in Ref. 3; AAA91057)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   502 AA;  56268 MW;  3FC27BF59798F944 CRC64;
     MMKPDLNSPL PQSPQLQAFG SRSSDLATED LFLKKLEAIS QTAPNETVKN EFLNKEIPSI
     NKLFTRFLKN RKKVIDWDKI NPPPADMVLN YKDLPAITEQ RTSELASKLA VLKLNGGLGT
     TMGCTGPKSV IEVRSEKTFL DLSVQQIKEM NERYNIKVPL VLMNSFNTHQ ETGKIIQKYK
     YSDVKIHSFN QSRFPRILKD NLMPVPDKLF GSDSEWYPPG HGDVFFALQN SGLLETLINE
     GKEYLFISNV DNLGAVVDFN ILEAMDKNKV EYIMEVTNKT RADVKGGTLI QYEGKAKLLE
     IAQVPSSKVE EFKSIKKFKI FNTNNIWVNL KAMDRILKQN LLDDMDIIIN PKVADGKNII
     QLEIAAGAAI EFFNNARGVN VPRSRFLPVK STSDLFIVQS NLYSLEKGVL VMNKNRPFTT
     VPLVKLGDNF KKVSDYQARI KGIPDILELD QLTVSGDITF GPNMVLKGTV IIVANHGSRI
     DIPEGSEFEN KVVSGNLHCG AL
//