UGP1_CANAL
ID UGP1_CANAL Reviewed; 500 AA.
AC Q59KI0; A0A1D8PST7;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 99.
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=CAALFM_CR04660CA;
GN ORFNames=CaO19.1738, CaO19.9305;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=12782322; DOI=10.1016/s0014-5793(03)00455-1;
RA Urban C., Sohn K., Lottspeich F., Brunner H., Rupp S.;
RT "Identification of cell surface determinants in Candida albicans reveals
RT Tsa1p, a protein differentially localized in the cell.";
RL FEBS Lett. 544:228-235(2003).
RN [5]
RP INDUCTION.
RX PubMed=17285563; DOI=10.1002/pmic.200600575;
RA Kusch H., Engelmann S., Albrecht D., Morschhauser J., Hecker M.;
RT "Proteomic analysis of the oxidative stress response in Candida albicans.";
RL Proteomics 7:686-697(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RX PubMed=17588813; DOI=10.1016/j.ijmm.2007.03.020;
RA Kusch H., Engelmann S., Bode R., Albrecht D., Morschhauser J., Hecker M.;
RT "A proteomic view of Candida albicans yeast cell metabolism in exponential
RT and stationary growth phases.";
RL Int. J. Med. Microbiol. 298:291-318(2008).
RN [7]
RP INDUCTION.
RX PubMed=22544909; DOI=10.1128/ec.00103-12;
RA Fanning S., Xu W., Solis N., Woolford C.A., Filler S.G., Mitchell A.P.;
RT "Divergent targets of Candida albicans biofilm regulator Bcr1 in vitro and
RT in vivo.";
RL Eukaryot. Cell 11:896-904(2012).
RN [8]
RP INDUCTION.
RX PubMed=23563485; DOI=10.1128/ec.00071-13;
RA Srikantha T., Daniels K.J., Pujol C., Kim E., Soll D.R.;
RT "Identification of genes upregulated by the transcription factor Bcr1 that
RT are involved in impermeability, impenetrability, and drug resistance of
RT Candida albicans a/alpha biofilms.";
RL Eukaryot. Cell 12:875-888(2013).
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 -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:12782322}. Note=Localizes to yeast but not hyphal
CC cell surface.
CC -!- INDUCTION: Expression is up-regulated during oropharyngeal candidiasis
CC (OPC) infection and during stationary phase. Repressed by HOG1, BCR1
CC and hydrogen peroxide. {ECO:0000269|PubMed:17285563,
CC ECO:0000269|PubMed:17588813, ECO:0000269|PubMed:22544909,
CC ECO:0000269|PubMed:23563485}.
CC -!- MISCELLANEOUS: Present with 17200 molecules/cell in log phase SD
CC medium.
CC -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
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DR EMBL; CP017630; AOW31202.1; -; Genomic_DNA.
DR RefSeq; XP_019331084.1; XM_019475539.1.
DR AlphaFoldDB; Q59KI0; -.
DR SMR; Q59KI0; -.
DR STRING; 237561.Q59KI0; -.
DR PRIDE; Q59KI0; -.
DR GeneID; 3648144; -.
DR KEGG; cal:CAALFM_CR04660CA; -.
DR CGD; CAL0000175518; UGP1.
DR VEuPathDB; FungiDB:CR_04660C_A; -.
DR eggNOG; KOG2638; Eukaryota.
DR HOGENOM; CLU_023632_3_0_1; -.
DR InParanoid; Q59KI0; -.
DR OMA; TNNLWAK; -.
DR OrthoDB; 503037at2759; -.
DR PRO; PR:Q59KI0; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IBA:GO_Central.
DR GO; GO:0006078; P:(1->6)-beta-D-glucan biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0005977; P:glycogen metabolic process; IBA:GO_Central.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0005992; P:trehalose biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IBA:GO_Central.
DR CDD; cd00897; UGPase_euk; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR006141; Intein_N.
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.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 1: Evidence at protein level;
KW Cell wall; Magnesium; Metal-binding; Nucleotidyltransferase;
KW Reference proteome; Secreted; Transferase.
FT CHAIN 1..500
FT /note="UTP--glucose-1-phosphate uridylyltransferase"
FT /id="PRO_0000424335"
FT REGION 449..500
FT /note="Oligomerization"
FT /evidence="ECO:0000250|UniProtKB:P32861"
FT ACT_SITE 388
FT /evidence="ECO:0000250|UniProtKB:P32861"
FT BINDING 109..112
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 111..112
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P32861"
FT BINDING 123
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 186
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 215
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 244..246
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16851"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P32861"
FT BINDING 246
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
FT BINDING 388
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000250|UniProtKB:Q9M9P3"
SQ SEQUENCE 500 AA; 55552 MW; 476B07B548695192 CRC64;
MATTGKRHAK SQSTYAFDNT ATNVTASQMR NALNNLADTV ENPEQTTRFE NEMDNFFTLF
RRYLTEKASG STLDWDKIRS PSSDEVVEYG DLNSANNSAN LSKLAVLKLN GGLGTSMGCV
GPKSVIEVRD GNNFLDLAVR QIEHLNRKYD ADVPLLLMNS FNTDADTEKI IKKYQSHRIR
VKTFNQSRFP RIYKDSLLPV PESFDDSLEA WYPPGHGDLF EALVQSGELD ALLAQGREIL
FVSNGDNLGA TVDSKILDHM IETGAEYIME LTPKTRADVK GGTLINYQGE VRLLEIAQVP
KEHVEEFKSI KKFKYFNTNN LWINLRAIKK LVEANAIEVE IIPNQKTISH GKSDINVLQL
ETAVGAAIRH FKGAHGVVVP RSRFLPVKTC SDLLLVKSDL FYLEHGALVL DPTRDGFSNP
LIKLGSHFKK VSGFQSRIPY IPKILELDHL TITGNVTIGK GVQLKGTVII VCNDGDKIDI
PNGAILENVV VTGNLTILEH
