ID   GDPP1_XENLA             Reviewed;         399 AA.
AC   A8E5Y3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=GDP-D-glucose phosphorylase 1;
DE            EC=2.7.7.78;
GN   Name=gdpgp1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specific and highly efficient GDP-D-glucose phosphorylase
CC       regulating the levels of GDP-D-glucose in cells. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-alpha-D-glucose + phosphate = alpha-D-glucose 1-phosphate
CC         + GDP + H(+); Xref=Rhea:RHEA:30387, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189, ChEBI:CHEBI:58601,
CC         ChEBI:CHEBI:62230; EC=2.7.7.78;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GDPGP1 family. {ECO:0000305}.
CC   -!- CAUTION: The ortholog in A.thaliana catalyzes the first reaction of the
CC       Smirnoff-Wheeler pathway, the major route to ascorbate biosynthesis in
CC       plants. {ECO:0000305}.
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DR   EMBL; BC153762; AAI53763.1; -; mRNA.
DR   RefSeq; NP_001104198.1; NM_001110728.1.
DR   AlphaFoldDB; A8E5Y3; -.
DR   MaxQB; A8E5Y3; -.
DR   DNASU; 100126619; -.
DR   GeneID; 100126619; -.
DR   KEGG; xla:100126619; -.
DR   CTD; 100126619; -.
DR   Xenbase; XB-GENE-5867405; gdpgp1.S.
DR   OMA; GIRVILW; -.
DR   OrthoDB; 1178383at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 100126619; Expressed in testis and 16 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0080048; F:GDP-D-glucose phosphorylase activity; ISS:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; ISS:UniProtKB.
DR   InterPro; IPR026506; GDPGP.
DR   PANTHER; PTHR20884; PTHR20884; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Guanine-nucleotide releasing factor; Hydrolase;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..399
FT                   /note="GDP-D-glucose phosphorylase 1"
FT                   /id="PRO_0000336754"
FT   ACT_SITE        237
FT                   /note="Tele-GMP-histidine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   399 AA;  45093 MW;  81D5A4E085AF58CB CRC64;
     MEEEHINQRP SATVEEYSYS EADFVFSGLS WKERRQYAED TSFLSPFDKA LQSKWEQKMN
     EGLFRYPLRN LQTKILPGSL SYVAQLNIQR SINRRKPEDI WSIQQKFNPN QFNYNKIKPE
     EIVFQMIRSE TEHCVDSDKV HGSSVNGMGT SDCKSGSTHQ RCCILECKGG CTLVVINVSP
     LEFGHVLFMP DPSLCLPQIL TEDLMLFGLE SVLLSAHPGF RVGFNSLGGF ASVNHLHLHG
     FYLDHDLFIE SSSSKPLCPE MNFHLITHFP APSFLFYTDG RNLKSTAQNI CKVTDFLVAK
     NIAHNLFITR GSNPDTGNGS EGRNGIRVNI WARKPSFGAK EVSAFNVALC ELAGHLPVKN
     QEDFNSITED SVIDIIHNCL LADDEFTQLS LDLVEYLRK