ID C1G4T5_PARBD Unreviewed; 563 AA.
AC C1G4T5;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=guanosine-diphosphatase {ECO:0000256|ARBA:ARBA00038903};
DE EC=3.6.1.42 {ECO:0000256|ARBA:ARBA00038903};
GN ORFNames=PADG_01951 {ECO:0000313|EMBL:EEH45801.1};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH45801.1, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH45801.1, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH45801.1,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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:0000256|ARBA:ARBA00037742}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004323}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR EMBL; KN275958; EEH45801.1; -; Genomic_DNA.
DR RefSeq; XP_010757652.1; XM_010759350.1.
DR AlphaFoldDB; C1G4T5; -.
DR STRING; 502780.C1G4T5; -.
DR GeneID; 22581522; -.
DR KEGG; pbn:PADG_01951; -.
DR VEuPathDB; FungiDB:PADG_01951; -.
DR eggNOG; KOG1385; Eukaryota.
DR HOGENOM; CLU_010246_4_0_1; -.
DR InParanoid; C1G4T5; -.
DR OMA; WTCRIKE; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000001628; Unassembled WGS sequence.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IEA:UniProt.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR PANTHER; PTHR11782:SF83; NTPASE, ISOFORM F; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Hydrolase {ECO:0000256|RuleBase:RU003833};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001628};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 75..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 255
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 286..290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 563 AA; 62251 MW; C20BEEF9FE2686BB CRC64;
MPTGVNSRNR VGIWSYLPFG SSPRRRSVSI PLKSVRDPFE KADRHSRDPF RSTTTLTFRN
IFMVFTMTQS QRTRYFKTWG IIAILLLFLY VLLPSRSSVP ATINTPVSST KCTKPYDSSK
PLIQYALMID AGSTGSRIHV YRFNNCGPTP ELENEDFKMT EKKKGGAGLS AYANDPVAAA
KSLDPLMEVA LTSVPREYQA CSPVAVKATA GLRFLGQETS DKILEAVRDR LETVYPFPVV
SKERGGIEIM DGKYEGVYAW ITTNYLLGNI GTKERIPTAA VFDLGGGSTQ IVFEPTFKSV
NGAAPEQLAE GAHKFSLSFG GRDFALYQHS HLGYGLMKAR ETIHQAVVEA KHESNPNDQS
WLSKPLVNPC LSAGMNLKVN VTLGESHPLG KVVEVNMTGP KDIPSAAQCR GIADKILKKD
MECKLAPCSF NGVHQPPLQK TFAQEDLYIM SYFYDRTAPL GMPESFTLRD LQDLTSTVCS
GYGSWGVFES IKDALSELLD RPEHCLDLSF MLSLLHTGYD LPLSRQVKIA KQIKGNELGW
CLGASLPLLN KESGWQCRVK EVS
//
