ID   UAP1_CAEEL              Reviewed;         484 AA.
AC   Q18493;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Probable UDP-N-acetylglucosamine pyrophosphorylase;
DE            EC=2.7.7.23;
GN   ORFNames=C36A4.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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   -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR   EMBL; Z66495; CAA91270.2; -; Genomic_DNA.
DR   PIR; T19764; T19764.
DR   RefSeq; NP_497777.1; NM_065376.3.
DR   AlphaFoldDB; Q18493; -.
DR   SMR; Q18493; -.
DR   BioGRID; 40735; 17.
DR   STRING; 6239.C36A4.4; -.
DR   EPD; Q18493; -.
DR   PaxDb; Q18493; -.
DR   PeptideAtlas; Q18493; -.
DR   EnsemblMetazoa; C36A4.4.1; C36A4.4.1; WBGene00007965.
DR   GeneID; 175497; -.
DR   KEGG; cel:CELE_C36A4.4; -.
DR   UCSC; C36A4.4.1; c. elegans.
DR   CTD; 175497; -.
DR   WormBase; C36A4.4; CE27831; WBGene00007965; -.
DR   eggNOG; KOG2388; Eukaryota.
DR   GeneTree; ENSGT00940000153464; -.
DR   HOGENOM; CLU_025603_1_1_1; -.
DR   InParanoid; Q18493; -.
DR   OMA; QPDVLKF; -.
DR   OrthoDB; 888726at2759; -.
DR   PhylomeDB; Q18493; -.
DR   Reactome; R-CEL-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR   UniPathway; UPA00113; UER00533.
DR   PRO; PR:Q18493; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00007965; Expressed in adult organism and 3 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070569; F:uridylyltransferase activity; IEA:InterPro.
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   3: Inferred from homology;
KW   Cytoplasm; Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..484
FT                   /note="Probable UDP-N-acetylglucosamine pyrophosphorylase"
FT                   /id="PRO_0000185769"
FT   MOTIF           107..110
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   MOTIF           304..305
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         107..110
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         121
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         200
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         226
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         227
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         377
FT                   /ligand="UTP"
FT                   /ligand_id="ChEBI:CHEBI:46398"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT   BINDING         407
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   484 AA;  53497 MW;  2E372500A052BECA CRC64;
     MTITAPPKDE IISKFPGSEP LLNFYNELSD AEKSKLFHQI STLNLSEAHQ WFIDSADQRA
     PSTAEDLKPV LDSQHFVQAE LHQVILDGLW NKGMDAIGRG EVCAIVLAGG QATRLGSSQP
     KGTIPLGINA SFGDSLLGIQ AAKIALLQAL AGEREHQNPG KIHWAVMTSP GTEEATREHV
     KKLAAHHGFD FDEQITIFSQ DEIAAYDEQG NFLLGTKGSV VAAPNGNGGL YSAISAHLPR
     LRAKGIKYFH VYCVDNILCK VADPHFIGFA ISNEADVATK CVPKQKGELV GSVCLDRGLP
     RVVEYSELGA ELAEQKTPDG KYLFGAGSIA NHFFTMDFMD RVCSPSSRLP YHRAHKKISY
     VNEQGTIVKP EKPNGIKLEQ FIFDVFELSK RFFIWEVARN EEFSPLKNAQ SVGTDCLSTC
     QRDLSNVNKL WLERVQAKVT ATEKPIYLKT IVSYNGENLQ ELRHREISDS ALESDHSINK
     FFVV