ID B6JYD5_SCHJY Unreviewed; 508 AA.
AC B6JYD5;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=guanosine-diphosphatase {ECO:0000256|ARBA:ARBA00038903};
DE EC=3.6.1.42 {ECO:0000256|ARBA:ARBA00038903};
GN Name=gda1 {ECO:0000313|JaponicusDB:SJAG_01595};
GN ORFNames=SJAG_01595 {ECO:0000313|EMBL:EEB06553.1};
OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB06553.1, ECO:0000313|Proteomes:UP000001744};
RN [1] {ECO:0000313|EMBL:EEB06553.1, ECO:0000313|Proteomes:UP000001744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(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; KE651168; EEB06553.1; -; Genomic_DNA.
DR RefSeq; XP_002172846.1; XM_002172810.2.
DR AlphaFoldDB; B6JYD5; -.
DR STRING; 402676.B6JYD5; -.
DR EnsemblFungi; EEB06553; EEB06553; SJAG_01595.
DR GeneID; 7052282; -.
DR JaponicusDB; SJAG_01595; gda1.
DR VEuPathDB; FungiDB:SJAG_01595; -.
DR eggNOG; KOG1385; Eukaryota.
DR HOGENOM; CLU_010246_4_0_1; -.
DR OMA; WTCRIKE; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000001744; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004382; F:GDP phosphatase activity; IBA:GO_Central.
DR GO; GO:0045134; F:UDP phosphatase activity; IBA:GO_Central.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
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:UP000001744};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..508
FT /note="guanosine-diphosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002847305"
FT REGION 48..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 211
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 242..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 508 AA; 56507 MW; 08D450A93D191AA1 CRC64;
MARPRALLFT VVAAALFLVL WFHVPQLNSS SNFASLDKTD LWTQQDLTST VDESTTESSQ
TDANEKSTSE LLTSCTVAYD ESKSVFQYVV MIDAGSTGSR VHVYKFNNCN PSPVLDDEFF
KMSEPGLSSY ADDPDAGARS LDELLDYAME HVPKEYQSCS PIAVKATAGL RLTGPAKAKA
ILDKVHQHLE RDYPFPVVEK GGVEIMDGSM EGVYAWITIN YLLGNLNVKP FHSTVAVMDL
GGASTQVVFE PKYSSPSETL AEGDHRYVLD YNGDRYTLYQ HSHLGYGLKE ARKAVHKEIV
DAYNVEPKPD SMLHPCLPVD TNITLSLPPA SDDTLAQDVV FHGPPFVPAA LQCRAYTEKI
LNKDEHCSLF PCSFNGVHQP RFRETFLNDK IFLISYFYDR MVDIGMPSTF TIEEMKDLAD
QVCRGPQAWS LFSNVVGAVD ALTDEPEWCL DLNYMITLLA TGYDIPNRRE LHTAKKINGM
ELGWCLGASL PLLSSETGHW TCKVSKEV
//
