UGPA1_DICDI
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 03-AUG-2022, entry version 121.
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 (Slime mold).
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.DDB0191527; -.
DR PaxDb; P08800; -.
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; MHFKSAT; -.
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; 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 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
