UGPA2_DICDI
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 03-AUG-2022, entry version 102.
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 (Slime mold).
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}.
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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.DDB0214911; -.
DR PaxDb; Q54YZ0; -.
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; TNNLWAK; -.
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; 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 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
