UGPA1_ENCCU
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 03-AUG-2022, entry version 94.
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; TNNLWAK; -.
DR OrthoDB; 503037at2759; -.
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; 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 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
