ID   UGPA1_DICDI             Reviewed;         511 AA.
AC   P08800; Q54GT7;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   24-JAN-2024, entry version 126.
DE   RecName: Full=UTP--glucose-1-phosphate uridylyltransferase 1;
DE            EC=2.7.7.9;
DE   AltName: Full=UDP-glucose pyrophosphorylase 1;
DE            Short=UDPGP 1;
DE            Short=UGPase 1;
GN   Name=uppA; ORFNames=DDB_G0289875;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=AX3;
RX   PubMed=3035502; DOI=10.1093/nar/15.9.3891;
RA   Ragheb J.A., Dottin R.P.;
RT   "Structure and sequence of a UDP glucose pyrophosphorylase gene of
RT   Dictyostelium discoideum.";
RL   Nucleic Acids Res. 15:3891-3906(1987).
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 1-30.
RX   PubMed=2854024; DOI=10.1002/dvg.1020090418;
RA   Pavlovic J., Haribabu B., Dottin R.P.;
RT   "Transmembrane signal transduction regulates gene expression in
RT   Dictyostelium discoideum.";
RL   Dev. Genet. 9:371-382(1988).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30, AND INDUCTION.
RX   PubMed=2557538; DOI=10.1128/mcb.9.11.4660-4669.1989;
RA   Pavlovic J., Haribabu B., Dottin R.P.;
RT   "Identification of a signal transduction response sequence element
RT   necessary for induction of a Dictyostelium discoideum gene by extracellular
RT   cyclic AMP.";
RL   Mol. Cell. Biol. 9:4660-4669(1989).
RN   [5]
RP   DEVELOPMENTAL STAGE.
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).
CC   -!- FUNCTION: Plays a central role as a glucosyl donor in cellular
CC       metabolic pathways. During development the lack of the enzyme activity
CC       leads to cell death and lysis. Strains which lack UDPG
CC       pyrophosphorylase accomplish early developmental events but are unable
CC       to culminate. The enzyme affects the growth rate of the cells but is
CC       not essential for growth. {ECO:0000269|PubMed:3035502}.
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   -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC   -!- SUBUNIT: Homooctamer. {ECO:0000250}.
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   -!- INDUCTION: By cAMP through transmembrane signal transduction.
CC       {ECO:0000269|PubMed:2557538}.
CC   -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR   EMBL; Y00145; CAA68340.1; -; Genomic_DNA.
DR   EMBL; AAFI02000149; EAL62450.1; -; Genomic_DNA.
DR   EMBL; M27639; AAA84450.1; -; Genomic_DNA.
DR   EMBL; M30467; AAA33271.1; -; Genomic_DNA.
DR   PIR; S07383; XNDOU.
DR   RefSeq; XP_635982.1; XM_630890.1.
DR   AlphaFoldDB; P08800; -.
DR   SMR; P08800; -.
DR   STRING; 44689.P08800; -.
DR   PaxDb; 44689-DDB0191527; -.
DR   EnsemblProtists; EAL62450; EAL62450; DDB_G0289875.
DR   GeneID; 8627397; -.
DR   KEGG; ddi:DDB_G0289875; -.
DR   dictyBase; DDB_G0289875; uppA.
DR   eggNOG; KOG2638; Eukaryota.
DR   HOGENOM; CLU_023632_0_0_1; -.
DR   InParanoid; P08800; -.
DR   OMA; WFGSSIT; -.
DR   PhylomeDB; P08800; -.
DR   UniPathway; UPA00214; -.
DR   PRO; PR:P08800; -.
DR   Proteomes; UP000002195; Chromosome 5.
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; IDA:dictyBase.
DR   GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR   GO; GO:0006012; P:galactose metabolic 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   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:SF3; UTP--GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE 1; 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   Magnesium; Metal-binding; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..511
FT                   /note="UTP--glucose-1-phosphate uridylyltransferase 1"
FT                   /id="PRO_0000185755"
FT   REGION          460..511
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        399
FT                   /evidence="ECO:0000250"
FT   BINDING         126..129
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         128..129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         140
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         203
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         233
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         262..264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         264
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         264
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         399
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   CONFLICT        28
FT                   /note="N -> D (in Ref. 1; CAA68340, 2; AAA84450 and 3;
FT                   AAA33271)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   511 AA;  57885 MW;  B6732C5C38218733 CRC64;
     MTDTATSKAT VERPKLQSTG SLHSLFKNVD LFSENDEELY PPLQHGARFA APIEDSTLLA
     LGMKPDELKA FQKQRHAYIN KDQIYTDEIK IPNKTEMVDY HQLHLVSPID QSNASRLLNK
     LVVIKLNGGL GNSMGCKTAK STMEIAPGVT FLDMAVAHIE QINQDYNVDV PLVIMNSYKT
     HNETNKVIEK YKTHKVSIKT FQQSMFPKMY KDTLNLVPKP NTPMNPKEWY PPGSGDIFRS
     LQRSGLIDEF LAAGKEYIFI SNVENLGSII DLQVLNHIHL QKIEFGLEVT NRINTDSTGG
     ILMSYKDKLH LLELSQVKPE KLKIFKDFKL WNTNNIWVNL KSVSNLIKED KLDLDWIVNY
     PLENHKAMVQ LETPAGMGIQ NFKNSVAIFV PRDRYRPIKS TSQLLVAQSN IFQFDHGQVK
     LNSKREGQDV PLVKLGEEFS TVSDYEKRFK SIPDLLELDH LTVSGDVYFG SRITLKGTVI
     IVANHGERVD IPDGVVLENK VLSGTLRILD H
//