GDA1_KLULA
ID GDA1_KLULA Reviewed; 522 AA.
AC Q9HEM6;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Guanosine-diphosphatase;
DE Short=GDPase;
DE EC=3.6.1.42;
GN Name=GDA1; OrderedLocusNames=KLLA0F16863g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 201343 / MG1/2;
RX PubMed=11425802; DOI=10.1093/glycob/11.5.413;
RA Lopez-Avalos M.D., Uccelletti D., Abeijon C., Hirschberg C.B.;
RT "The UDPase activity of the Kluyveromyces lactis Golgi GDPase has a role in
RT uridine nucleotide sugar transport into Golgi vesicles.";
RL Glycobiology 11:413-422(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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:11425802}.
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 -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:11425802}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:11425802}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ401304; CAC21576.1; -; Genomic_DNA.
DR EMBL; CR382126; CAG98545.1; -; Genomic_DNA.
DR RefSeq; XP_455837.1; XM_455837.1.
DR AlphaFoldDB; Q9HEM6; -.
DR SMR; Q9HEM6; -.
DR STRING; 28985.XP_455837.1; -.
DR EnsemblFungi; CAG98545; CAG98545; KLLA0_F16863g.
DR GeneID; 2895656; -.
DR KEGG; kla:KLLA0_F16863g; -.
DR eggNOG; KOG1385; Eukaryota.
DR HOGENOM; CLU_010246_4_1_1; -.
DR InParanoid; Q9HEM6; -.
DR OMA; DKPIVQY; -.
DR BRENDA; 3.6.1.42; 2825.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IEA:EnsemblFungi.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW Golgi apparatus; Hydrolase; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..522
FT /note="Guanosine-diphosphatase"
FT /id="PRO_0000209917"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..522
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 35..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 220
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 522 AA; 56863 MW; A7A27902607A6732 CRC64;
MHINSVVRNY RFLIGALTAL MLLLLLRSSA SPQVGSLANS NKVDTPDGLK VPGASSPISQ
NINEDSQKQT AKDHTSQNLE SGSNSLSKSQ CTEGHKYVVM IDAGSTGSRV HVYEFDVCTQ
PPTLINETFE MLKPGLSSFD IDAVGAAKSL DPLLKIAMDA VPKDKRNCTP VAVKATAGLR
MLGDEKSSKI LAQVRKHLEQ DYPFPVVDGD GVSIMDGEEE GVYAWVTANY LLGNIGAGSK
LPTAAVFDLG GGSTQIVFEP SFPPNEKMVD GEHKYELSFG GHDYTLYQFS HLGYGLMQGR
NKINTELVNV AISSGTITKG QTARTYELSS PCLPPGTTAE GEKVKISDDE IYTVNFKGPK
VPAGPQCRYL ADKILNKDAK CNTPPCSFNG IHQPSLVHTF KETSDLYVFS YFYDRTQPLG
LPLSFTLQEL QDLARTVCNG EEVWESVFSG IEGSLSELSK EPQWCLDLNF QVSLLHTGYD
IPLQRELRTA KTIANNELGW CLGASLPLLE SANWSCKVSK VE
