ID   UAP1_ENCCU              Reviewed;         335 AA.
AC   Q8SQS1;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Probable UDP-N-acetylglucosamine pyrophosphorylase;
DE            EC=2.7.7.23;
GN   Name=UAP1; OrderedLocusNames=ECU11_1780;
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP =
CC         diphosphate + UDP-N-acetyl-alpha-D-glucosamine; Xref=Rhea:RHEA:13509,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:57776; EC=2.7.7.23;
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC       glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-
CC       acetyl-alpha-D-glucosamine 1-phosphate: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {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; AL590450; CAD26088.1; -; Genomic_DNA.
DR   RefSeq; NP_586484.1; NM_001042317.1.
DR   AlphaFoldDB; Q8SQS1; -.
DR   SMR; Q8SQS1; -.
DR   STRING; 284813.Q8SQS1; -.
DR   GeneID; 860138; -.
DR   KEGG; ecu:ECU11_1780; -.
DR   VEuPathDB; MicrosporidiaDB:ECU11_1780; -.
DR   HOGENOM; CLU_025603_1_2_1; -.
DR   InParanoid; Q8SQS1; -.
DR   OMA; ANICHHY; -.
DR   OrthoDB; 888726at2759; -.
DR   UniPathway; UPA00113; UER00533.
DR   Proteomes; UP000000819; Chromosome XI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR039741; UDP-sugar_pyrophosphorylase.
DR   InterPro; IPR002618; UDPGP_fam.
DR   PANTHER; PTHR11952; PTHR11952; 1.
DR   Pfam; PF01704; UDPGP; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..335
FT                   /note="Probable UDP-N-acetylglucosamine pyrophosphorylase"
FT                   /id="PRO_0000381748"
FT   MOTIF           45..48
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   MOTIF           218..219
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         45..48
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         59
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         120
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         145
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         278
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         308
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   335 AA;  37953 MW;  FDADE0691BC0289A CRC64;
     MGYISMNSTN LIRPYEGTEL NDAGRKYKKI GERLLREKKL GVVILSGGQG TRLGSDEPKG
     LFKIKGKTLF EWHMETIKEL ISKYNADIAV FIMTSSFTDE AVRKYFQSTD FGLKIQFFKQ
     RNSLCVGTDG KPLEWYDGHA ESPYGNGDIF NAIQQVNLEG IEALNVICID NVLAKILDPV
     FVGAFYSDDY DILSKSVTKE EKESVGAFLM DERLKIKEYS ENDAKGEGIQ GNICNHIFKT
     SFIKKMKNIN LPEHKAFKKI PYTISGKLIK PVKPNGFKKE TFIFDSFEYT QKNGVMNVPR
     EKEFSPLKNG MDSSVDNPVT CTIAVERHRI KTTIQ