ID   UGPA1_ENCCU             Reviewed;         492 AA.
AC   Q8SSC5;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=UTP--glucose-1-phosphate uridylyltransferase;
DE            EC=2.7.7.9;
DE   AltName: Full=UDP-glucose pyrophosphorylase;
DE            Short=UDPGP;
DE            Short=UGPase;
GN   Name=UGP1; OrderedLocusNames=ECU03_0280;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
CC   -!- FUNCTION: Plays a central role as a glucosyl donor in cellular
CC       metabolic pathways. {ECO:0000250}.
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   -!- SUBUNIT: Homooctamer. {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR   EMBL; AL590443; CAD26174.1; -; Genomic_DNA.
DR   RefSeq; NP_597539.1; NM_001040903.1.
DR   AlphaFoldDB; Q8SSC5; -.
DR   SMR; Q8SSC5; -.
DR   STRING; 284813.Q8SSC5; -.
DR   GeneID; 858701; -.
DR   KEGG; ecu:ECU03_0280; -.
DR   VEuPathDB; MicrosporidiaDB:ECU03_0280; -.
DR   HOGENOM; CLU_023632_3_0_1; -.
DR   InParanoid; Q8SSC5; -.
DR   OMA; KEYCFLS; -.
DR   OrthoDB; 45684at2759; -.
DR   Proteomes; UP000000819; Chromosome III.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro.
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   1: Evidence at protein level;
KW   Magnesium; Metal-binding; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..492
FT                   /note="UTP--glucose-1-phosphate uridylyltransferase"
FT                   /id="PRO_0000381754"
FT   REGION          441..492
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        379
FT                   /evidence="ECO:0000250"
FT   BINDING         110..113
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         112..113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         124
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         183
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         210
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         239..241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16851"
FT   BINDING         241
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         241
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         379
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
SQ   SEQUENCE   492 AA;  55910 MW;  22754F479329775D CRC64;
     MQESRSKEST LSGDEDKDVH RFLDEFDDKC TCKLLKEMKE TLEGLKKSHP NPTNLDEFYR
     LFERYLRTRH EKIVWEKIRS PKDRIVQYNE IPEPTEKSKE LLRKLAILKL NGGLGTTMGC
     VGPKSAITIK DGKNFIDLVV KQIRYLNSKY KIDVPLILMN SFNTEGMTDK IIFRYDGIKK
     FSQSKFPRIS SETLLPVSPS HGDKGMYPPG HGDLFYSMKN SGMLEELLEG GYEYLFVSNI
     DNLASTVDLK LLEYFATNEL GFLMEVTDKT RADVKGGTLI EYKGALRLLE IAQVPSNKKS
     EFTSFKKFTI FNTNNLWINL KEMKKKLEEG FFDLDIIENK KALDDETVIQ LETAIGSAIK
     YFPNSCGVVV PRSRFLPVKT CSDLFLVESN LFVEKNGTLQ LHPSRVPETC PTVKLIGENF
     SKIEKYEKCF KGIPDILELE VLTVSGNVLF GKNVVLKGTV IILADEKSKI CVPDGSVLED
     NIIYGNLPII DH
//