UAP1_DICDI
ID UAP1_DICDI Reviewed; 487 AA.
AC Q54GN5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable UDP-N-acetylglucosamine pyrophosphorylase;
DE EC=2.7.7.23;
GN Name=uap1; ORFNames=DDB_G0290055;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
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).
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; AAFI02000151; EAL62433.1; -; Genomic_DNA.
DR RefSeq; XP_635927.1; XM_630835.1.
DR AlphaFoldDB; Q54GN5; -.
DR SMR; Q54GN5; -.
DR STRING; 44689.DDB0266385; -.
DR PaxDb; Q54GN5; -.
DR EnsemblProtists; EAL62433; EAL62433; DDB_G0290055.
DR GeneID; 8627448; -.
DR KEGG; ddi:DDB_G0290055; -.
DR dictyBase; DDB_G0290055; uap1.
DR eggNOG; KOG2388; Eukaryota.
DR HOGENOM; CLU_025603_1_2_1; -.
DR InParanoid; Q54GN5; -.
DR OMA; QPDVLKF; -.
DR PhylomeDB; Q54GN5; -.
DR Reactome; R-DDI-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR UniPathway; UPA00113; UER00533.
DR PRO; PR:Q54GN5; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IBA:GO_Central.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
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..487
FT /note="Probable UDP-N-acetylglucosamine pyrophosphorylase"
FT /id="PRO_0000328000"
FT MOTIF 105..108
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT MOTIF 307..308
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT BINDING 105..108
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 119
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 198
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 225
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 382
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 412
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 487 AA; 55431 MW; 0E12B99059A0E87C CRC64;
MDTTNFEDIR NEWIEQGQGH VFNWFDKLSN EEKLNFENDI RKINVKEVNK DYKNVLLNKD
EQKIMKYEHF ENVMTLNKIK EQDKKKWEDI GYELISKGEV AVLLLAGGQA TRLGTTFPKG
FYDVGLPSKK SLFQLQAERI YRLQQLVSER YNGSYDQDSK PIQWYIMTSE ATHSETIKFF
ENKNYFGLKK SAFFFFSQAM IPCITPEDGK IISESGSKLS LSPNGNGGLF KALSTSGAID
DMRKKGIKYV TQYCVDNILI NMADPVFVGY MHDQSADCGA KVVSKSDPKE PVGVMALNGD
GKPFVLEYSE IDEQSKFKKD QNGQLVFNYA HICINAFSFD FLDRIAKNHL DHLKYHVAFK
KIPSAHPISG ERQSPSSPNG WKLEKFIFDV FPFSKKMVCL EIERSKEFSP LKNCGGMNLP
DSPETCLRDI SNLHKSFIEN SGGKIDSSNS TICEVSPLVS LNGENLKNFV NDKTFILPIE
INQNLNN
