GDE1_CANAL
ID GDE1_CANAL Reviewed; 1162 AA.
AC A0A1D8PNZ7;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Glycerophosphocholine phosphodiesterase GDE1 {ECO:0000303|PubMed:24114876};
DE EC=3.1.4.2 {ECO:0000305|PubMed:24114876};
DE AltName: Full=Glycerophosphodiester phosphodiesterase GDE1;
GN Name=GDE1 {ECO:0000303|PubMed:24114876};
GN OrderedLocusNames=CAALFM_C504510WA;
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 INDUCTION.
RX PubMed=16151249; DOI=10.1128/ec.4.9.1562-1573.2005;
RA Murillo L.A., Newport G., Lan C.Y., Habelitz S., Dungan J., Agabian N.M.;
RT "Genome-wide transcription profiling of the early phase of biofilm
RT formation by Candida albicans.";
RL Eukaryot. Cell 4:1562-1573(2005).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=17604452; DOI=10.1371/journal.ppat.0030092;
RA Xu D., Jiang B., Ketela T., Lemieux S., Veillette K., Martel N.,
RA Davison J., Sillaots S., Trosok S., Bachewich C., Bussey H., Youngman P.,
RA Roemer T.;
RT "Genome-wide fitness test and mechanism-of-action studies of inhibitory
RT compounds in Candida albicans.";
RL PLoS Pathog. 3:E92-E92(2007).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=24114876; DOI=10.1074/jbc.m113.505735;
RA Bishop A.C., Ganguly S., Solis N.V., Cooley B.M., Jensen-Seaman M.I.,
RA Filler S.G., Mitchell A.P., Patton-Vogt J.;
RT "Glycerophosphocholine utilization by Candida albicans: role of the Git3
RT transporter in virulence.";
RL J. Biol. Chem. 288:33939-33952(2013).
CC -!- FUNCTION: Glycerophosphocholine glycerophosphodiesterase responsible
CC for the hydrolysis of intracellular glycerophosphocholine into
CC glycerol-phosphate and choline (PubMed:24114876). The choline is used
CC for phosphatidyl-choline synthesis (PubMed:24114876). Required for
CC utilization of glycerophosphocholine as phosphate source
CC (PubMed:24114876). C.albicans can utilize GroPCho through transport and
CC intracellular hydrolysis or through extracellular hydrolysis
CC (PubMed:24114876). {ECO:0000269|PubMed:24114876}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sn-glycerol 3-phosphocholine = choline + H(+) + sn-
CC glycerol 3-phosphate; Xref=Rhea:RHEA:16061, ChEBI:CHEBI:15354,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:57597; EC=3.1.4.2;
CC Evidence={ECO:0000305|PubMed:24114876};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16062;
CC Evidence={ECO:0000305|PubMed:24114876};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:24114876}.
CC -!- INDUCTION: Expression is positively regulated by the transcription
CC factor PHO4 (PubMed:24114876). Induced during early phase of biofilm
CC formation (PubMed:16151249). {ECO:0000269|PubMed:16151249,
CC ECO:0000269|PubMed:24114876}.
CC -!- DISRUPTION PHENOTYPE: Results in altered glycerophosphocholine
CC catabolism (PubMed:24114876). Leads to hypersensitivity to 5-
CC fluorouracil (5-FU) (PubMed:17604452). {ECO:0000269|PubMed:17604452,
CC ECO:0000269|PubMed:24114876}.
CC -!- SIMILARITY: Belongs to the GDE1 family. {ECO:0000305}.
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DR EMBL; CP017627; AOW29857.1; -; Genomic_DNA.
DR RefSeq; XP_721845.1; XM_716752.2.
DR AlphaFoldDB; A0A1D8PNZ7; -.
DR SMR; A0A1D8PNZ7; -.
DR STRING; 237561.A0A1D8PNZ7; -.
DR GeneID; 3636505; -.
DR KEGG; cal:CAALFM_C504510WA; -.
DR CGD; CAL0000191313; GDE1.
DR VEuPathDB; FungiDB:C5_04510W_A; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG1162; Eukaryota.
DR eggNOG; KOG2421; Eukaryota.
DR OMA; HSTQLDT; -.
DR OrthoDB; 687958at2759; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047389; F:glycerophosphocholine phosphodiesterase activity; IMP:CGD.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IMP:CGD.
DR Gene3D; 1.25.40.20; -; 2.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR033506; Gde1.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR004331; SPX_dom.
DR PANTHER; PTHR22958:SF1; PTHR22958:SF1; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF03009; GDPD; 1.
DR Pfam; PF03105; SPX; 1.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS51704; GP_PDE; 1.
DR PROSITE; PS51382; SPX; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Cytoplasm; Hydrolase; Reference proteome; Repeat.
FT CHAIN 1..1162
FT /note="Glycerophosphocholine phosphodiesterase GDE1"
FT /id="PRO_0000439802"
FT DOMAIN 1..155
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT REPEAT 346..375
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 392..421
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 423..452
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 458..487
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 492..521
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 525..554
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT DOMAIN 817..1146
FT /note="GP-PDE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01041"
SQ SEQUENCE 1162 AA; 130854 MW; CFB280D9215A1F0C CRC64;
MKFGKTYVTH QIPEWSIYYM NYKQLKKIIK SIDSAANTNV DESKYPEVIS DTLGSFFYDL
DRDIEKVDSF YNTKFKEYNR RLNKIFQVLG YQDGQITHNI ESSEELDEII NILIELKSLF
RNLKWFAELN HKGFIKILKK LDKKLTSILS QHSGVSVGGV SNHNQEAYMG SRINALPFAN
GTEASNCLDS IHHILSRIET RNDVVQETIP VENNETSISA LIKNDDFEGL KKHITIKSSQ
KFLISTLNKA ALANSTKCID VIWNQLDMLY DDSDFNGRNF FHQHIISLGK AQFIREEQIV
PGEVTNRLIG GDNGPDNSNK NDNPIGLLYI LNKLKHKRLI LAEDHYHRTP LHYASQYGLV
EVTRYLVEFG VKWGLINTSI SIDDVSIWGD QEGLTPLHLS IIGKHPKTTE TLLGFNKAQT
LTCPNLLLLA VRLNSPQILN SLIVEGNIDV NYTDIDHRNE TALYIASKLN HPDLVEFLLE
SNANTEIGEN VFGWTPIFIA ASEGFMTIVK LLKEYGASYD IVDDSGWLPM EHACLRGHLD
VTDLLLPKNE KLLLYDMYHP ENNLPRIPSL AASPVLTGSD DGTVSTSSID KLPEPQKNTV
NQFYKQLKNN SSNNVSRSTS PKRNKRYKPV KSFGHRYLNE DESLILLTLG TTDLRDTNVP
VELNKVSLAK SFATELDTAL SLSITCRHKL TNNPVEPPVV VDLPLEDFHG SATDPISFKL
SNDLTVNDVI ITFDIIPTYQ VNKKVIGRAI ALLKDAYTKV GPNLRSLNNS IAIPIIESTN
LDILGTIRFE YLQVLPFKHK AMSIARSDTY WKQLVSTRVI GHRGLGKNLS GKKSLQLGEN
TVESFIAAAS LGASYVEFDV QLTKDHVPVV YHDFTVAESG VDIPMHLLTL EQFMGFNTPT
EKPTHTVDDE VLTRGKQRAQ SSYQLSNNHN DDIEKEFANQ RDERMKFTKT WKNQGYKGNL
RGSSVASNFV TLRELFRKLP NNVGFNIEVK YPMLDEAQLE DMGEIGVDLN FFVDTILKVI
YDENTTGRDI VFSSFHPDIC LLLSLKQPTM PVLFLTEAGT APMYDIRASS LQNAVRFSKK
WNLLGIVSNA LALIKTPRLA QVVKSMGLVC VTYGTENNEP ELAKIQMRAG VDAVIVDSVL
AVREGLREHN ETMNEFEDSP TE
