UAP1_CANAX
ID UAP1_CANAX Reviewed; 486 AA.
AC O74933;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase;
DE EC=2.7.7.23;
GN Name=UAP1;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9603950; DOI=10.1074/jbc.273.23.14392;
RA Mio T., Yabe T., Arisawa M., Yamada-Okabe H.;
RT "The eukaryotic UDP-N-acetylglucosamine pyrophosphorylases: gene cloning,
RT protein expression, and catalytic mechanism.";
RL J. Biol. Chem. 273:14392-14397(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; AB011003; BAA32334.1; -; Genomic_DNA.
DR PDB; 2YQC; X-ray; 1.90 A; A=1-486.
DR PDB; 2YQH; X-ray; 2.30 A; A/B=1-486.
DR PDB; 2YQJ; X-ray; 2.31 A; A/B=1-486.
DR PDB; 2YQS; X-ray; 2.30 A; A=1-486.
DR PDBsum; 2YQC; -.
DR PDBsum; 2YQH; -.
DR PDBsum; 2YQJ; -.
DR PDBsum; 2YQS; -.
DR AlphaFoldDB; O74933; -.
DR SMR; O74933; -.
DR VEuPathDB; FungiDB:C5_02530W_A; -.
DR VEuPathDB; FungiDB:CAWG_04635; -.
DR BRENDA; 2.7.7.23; 1096.
DR UniPathway; UPA00113; UER00533.
DR EvolutionaryTrace; O74933; -.
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 3D-structure; Cytoplasm; Nucleotidyltransferase; Transferase.
FT CHAIN 1..486
FT /note="UDP-N-acetylglucosamine pyrophosphorylase"
FT /id="PRO_0000185771"
FT MOTIF 109..112
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT MOTIF 309..310
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT BINDING 109..112
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 123
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 199
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 257
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 389
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 421
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 30..41
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 46..59
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:2YQC"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 85..100
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 104..113
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 136..155
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 278..285
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:2YQC"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 315..319
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 333..342
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 343..353
FT /evidence="ECO:0007829|PDB:2YQC"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:2YQC"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 394..400
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 406..411
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 413..416
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 431..448
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:2YQS"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:2YQC"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:2YQC"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:2YQC"
SQ SEQUENCE 486 AA; 54644 MW; 6C488939A16870F9 CRC64;
MTVKSQQQII DSFKQANQDQ LFQYYDSLTI DQQQEFIDQL STIEEPAKLI STVEQAIQFS
QTNSTSRNFT QLPNEQTAST LDLSKDILQN WTELGLKAIG NGEVAVLLMA GGQGTRLGSS
APKGCFNIEL PSQKSLFQIQ AEKILKIEQL AQQYLKSTKK PIINWYIMTS GPTRNATESF
FIENNYFGLN SHQVIFFNQG TLPCFNLQGN KILLESKNSI CQSPDGNGGL YKALKDNGIL
DDLNSKGIKH IHMYCVDNCL VKVADPIFIG FAIAKKFDLA TKVVRKRDAN ESVGLIVLDQ
DNQKPCVIEY SEISQELANK KDPQDSSKLF LRAANIVNHY YSVEFLNKMI PKWISSQKYL
PFHIAKKKIP SLNLENGEFY KPTEPNGIKL EQFIFDVFPS VELNKFGCLE VDRLDEFSPL
KNADGAKNDT PTTCRNHYLE RSSKWVIQNG GVIDNQGLVE VDSKTSYGGE GLEFVNGKHF
KNGDII
