ID A0A0P1BK65_9BASI Unreviewed; 554 AA.
AC A0A0P1BK65;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=guanosine-diphosphatase {ECO:0000256|ARBA:ARBA00038903};
DE EC=3.6.1.42 {ECO:0000256|ARBA:ARBA00038903};
OS Ceraceosorus bombacis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH16815.1, ECO:0000313|Proteomes:UP000054845};
RN [1] {ECO:0000313|EMBL:CEH16815.1, ECO:0000313|Proteomes:UP000054845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA Brescovit A.D., Santos A.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CCYA01000391; CEH16815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1BK65; -.
DR STRING; 401625.A0A0P1BK65; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000054845; 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 Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000054845}.
FT ACT_SITE 240
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 274..278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 554 AA; 59405 MW; EADCED8D6F27F8F7 CRC64;
MARSRLALSP RKFIFLAVSL TFLGIVLLSP SRRYVAERGK AAWASAGERL EEVDLSGLHF
DWPQNPWMGG DVLGNIRTPP EKHADPLRTR RCESNGGRIV DAKGHLRPTV QYGIMIDAGS
TGSRVHVYKF NYCSSSPELE SEVFEMIRGG LSSYGSNAQG AADSLRPLLQ TAYKSVPPSL
RRCTPISVKA TAGLRLLGAK QSKDILNAVR YMLEHEYPFP IADGPDGRGK GVEIMEGRDE
GVFAWITVNY LLNRIGVQGT NVAPKTAAVM DLGGASTQIV FEPTPGSGPM PPGAHVYTLE
GFGGRNYTLY QNSYLGYGLM QARKSINALA TFSHALSHPS AVKFGPSTGT AVIGVTAGAD
AARIPSPCFA PGTEKKAKVV LPGRDGEVEV MLTGAPGGFA GCKRLVEVMM NKDAACATSP
CSFAGVYQPS LMNSFADSPI VALSYFYDRL EPLGVNGTFS ISLLESLAKD VCAGPARWSV
RFPPSKYPEA LKELRDRPET CLDLTFQHAL LSLGYDLGAN RQVTVAKKLA GSELGWCAGA
QLMTLDEEGV LCKA
//
