GDA1_CANAL
ID GDA1_CANAL Reviewed; 599 AA.
AC Q8TGH6; A0A1D8PKG9; Q5A4E0;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Guanosine-diphosphatase;
DE Short=GDPase;
DE EC=3.6.1.42 {ECO:0000269|PubMed:12455990};
GN Name=GDA1; OrderedLocusNames=CAALFM_C306120CA; ORFNames=CaO19.7394;
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=12455990; DOI=10.1128/ec.1.3.420-431.2002;
RA Herrero A.B., Uccelletti D., Hirschberg C.B., Dominguez A., Abeijon C.;
RT "The Golgi GDPase of the fungal pathogen Candida albicans affects
RT morphogenesis, glycosylation, and cell wall properties.";
RL Eukaryot. Cell 1:420-431(2002).
RN [2]
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 [3]
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 [4]
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).
CC -!- FUNCTION: After transfer of sugars to endogenous macromolecular
CC acceptors, the enzyme converts nucleoside diphosphates to nucleoside
CC monophosphates which in turn exit the Golgi lumen in a coupled
CC antiporter reaction, allowing entry of additional nucleotide sugar from
CC the cytosol. {ECO:0000269|PubMed:12455990}.
CC -!- FUNCTION: Has a role in cell wall morphogenesis during the transition
CC of budding growth into hyphal growth, a process known as dimorphism.
CC {ECO:0000269|PubMed:12455990}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP + H2O = GMP + H(+) + phosphate; Xref=Rhea:RHEA:22156,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58115, ChEBI:CHEBI:58189; EC=3.6.1.42;
CC Evidence={ECO:0000269|PubMed:12455990};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:12455990}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:12455990}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; AJ421721; CAD18870.1; -; Genomic_DNA.
DR EMBL; CP017625; AOW28620.1; -; Genomic_DNA.
DR RefSeq; XP_716635.1; XM_711542.1.
DR AlphaFoldDB; Q8TGH6; -.
DR SMR; Q8TGH6; -.
DR STRING; 237561.Q8TGH6; -.
DR GeneID; 3641762; -.
DR KEGG; cal:CAALFM_C306120CA; -.
DR CGD; CAL0000196532; GDA1.
DR VEuPathDB; FungiDB:C3_06120C_A; -.
DR eggNOG; KOG1385; Eukaryota.
DR HOGENOM; CLU_010246_4_1_1; -.
DR InParanoid; Q8TGH6; -.
DR OMA; DKPIVQY; -.
DR OrthoDB; 1337265at2759; -.
DR BRENDA; 3.6.1.42; 1096.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0005794; C:Golgi apparatus; IDA:CGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:CGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; IMP:CGD.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0036187; P:cell growth mode switching, budding to filamentous; IMP:CGD.
DR GO; GO:0036244; P:cellular response to neutral pH; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036178; P:filamentous growth of a population of unicellular organisms in response to neutral pH; IMP:CGD.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IMP:CGD.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IMP:CGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0006493; P:protein O-linked glycosylation; IMP:CGD.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; PTHR11782; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE 1: Evidence at protein level;
KW Golgi apparatus; Hydrolase; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..599
FT /note="Guanosine-diphosphatase"
FT /id="PRO_0000209916"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..599
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 41..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..64
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 599 AA; 65953 MW; D5BC3A4F6E1B646A CRC64;
MINPRNLRLI IAVIGLVGIF AFFASSQHSL VDRTALQVNK PAADSPHVPP PAAAAAPVSP
PPPSQQQKQQ EGSQKQLNDE NSDEKNTLQG TSYSGTKPPY EKVDGKSNKI LADKLDTTKN
SKPNQQQQQN TQKGASEEKS AQNKITTPEE VSMDNGKCND IDYVVMIDAG STGSRVHVYE
FNTCVKPPQL LSEEFEMLKP GLSSFDTDTV GAAKSLDPLL EVALKKVPKN KQSCTPVAVK
ATAGLRLLGE TKSKAILDEV RSHLEKDYPF AVVSEDGISI MDGKDEGVYA WVTANYLLGN
IGGKEKLPTA AVFDLGGGST QIVFEPDYKV DEVPVDGETK YHFTFGDNQY TLYQFSHLGY
GLMQGRNKVN QLVLKNKLSE LNLQKYTKKE VKGAKATVDV SNPCIPPGVV AKDVQVELGE
DEFYVVNMKG PSSKDSTVAG GSQCRYLAEK VLNKDAECTS KPCSFNGVHQ PSLTRTFNKN
SDMYVFSYFY DRTNPIGMPS SFSVEELKDL SKLVCQGETF WKDILLDDHV KNLNEEPQWC
LDLSFITAML HTGYDIPLHR ELKTAKTIDN NELGWCLGAS LPLLDKNNAK WTCRIDKTD
