GDA1_SCHPO
ID GDA1_SCHPO Reviewed; 556 AA.
AC Q9UT35;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Guanosine-diphosphatase;
DE Short=GDPase;
DE EC=3.6.1.42 {ECO:0000269|PubMed:14612233};
GN Name=gdp1; ORFNames=SPAC824.08;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP COFACTOR, AND SUBCELLULAR LOCATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=14612233; DOI=10.1016/s0378-1097(03)00698-0;
RA Sanchez R., Franco A., Gacto M., Notario V., Cansado J.;
RT "Characterization of gdp1+ as encoding a GDPase in the fission yeast
RT Schizosaccharomyces pombe.";
RL FEMS Microbiol. Lett. 228:33-38(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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:14612233}.
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:14612233};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22157;
CC Evidence={ECO:0000305|PubMed:14612233};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:14612233};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:14612233};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:14612233}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:14612233}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:14612233}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; AF465240; AAL69974.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB57338.1; -; Genomic_DNA.
DR PIR; T39109; T39109.
DR RefSeq; NP_593447.1; NM_001018880.2.
DR AlphaFoldDB; Q9UT35; -.
DR SMR; Q9UT35; -.
DR BioGRID; 278325; 23.
DR IntAct; Q9UT35; 1.
DR STRING; 4896.SPAC824.08.1; -.
DR MaxQB; Q9UT35; -.
DR PaxDb; Q9UT35; -.
DR DNASU; 2541834; -.
DR EnsemblFungi; SPAC824.08.1; SPAC824.08.1:pep; SPAC824.08.
DR GeneID; 2541834; -.
DR KEGG; spo:SPAC824.08; -.
DR PomBase; SPAC824.08; -.
DR VEuPathDB; FungiDB:SPAC824.08; -.
DR eggNOG; KOG1385; Eukaryota.
DR HOGENOM; CLU_010246_4_0_1; -.
DR InParanoid; Q9UT35; -.
DR OMA; DKPIVQY; -.
DR PhylomeDB; Q9UT35; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9UT35; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:PomBase.
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:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IDA:PomBase.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:PomBase.
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 Calcium; Glycoprotein; Golgi apparatus; Hydrolase; Manganese; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..556
FT /note="Guanosine-diphosphatase"
FT /id="PRO_0000209918"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..556
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 256
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 556 AA; 61589 MW; 1D811E3D6A6BBB85 CRC64;
MTPTMKSIAR RKALLIALSI FAVTFILWNG FPGSSNRPLP SSNDEFHYED IELPSGYRSE
GEVVDLLNPK DELEEPLFSE EPLFPVTTSI PTKTAVSKPK IAPTSAAKDV TFSSSIDSDD
CSVAYDNSKP VRQYVLMIDA GSTGSRVHVY QFNNCNPSPK LEEEFFKMIE PGLSSFAGDP
EGAAASLDPL LDYAMENVPE EYRRCSPIAV KATAGLRLTG ESEAKAILKS VRQHLENDYP
FPIVKDGVSI LEGSMEGIYA WITINYLLGT LGGKATHSTV AVMDLGGAST QLVFEPRFAS
DGESLVDGDH KYVLDYNGEQ YELYQHSHLG YGLKEARKLI HKFVLNNAEA LKESLELLGD
STSIIHPCLH LNASLTHPDS KSEASEVVFV GPSLAHLSLQ CRGIAEKALY KDKNCPVRPC
SFNGVHQPKF TETFTDSPIY LISYFYDRMI SLGMPSTFTI EDMKYLANSV CSGPTYWQDA
FSLTDALKEL KEEPEWCLDL NYMISLLSVG YEIPNNRQLH TAKKIDNKEL GWCLGASLSM
LSEQNNGWNC NVKEEI
