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Database: UniProt
Entry: D8QQH0_SELML
LinkDB: D8QQH0_SELML
Original site: D8QQH0_SELML 
ID   D8QQH0_SELML            Unreviewed;       389 AA.
AC   D8QQH0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=GDP-D-glucose phosphorylase 1 {ECO:0000256|ARBA:ARBA00018857};
DE            EC=2.7.7.78 {ECO:0000256|ARBA:ARBA00012507};
GN   ORFNames=SELMODRAFT_139516 {ECO:0000313|EMBL:EFJ38457.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ38457.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA   Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA   Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA   Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA   Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA   Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA   Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA   Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA   Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA   Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA   Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA   Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA   Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(2011).
CC   -!- FUNCTION: Specific and highly efficient GDP-D-glucose phosphorylase
CC       regulating the levels of GDP-D-glucose in cells.
CC       {ECO:0000256|ARBA:ARBA00003049}.
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         Evidence={ECO:0000256|ARBA:ARBA00000063};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the GDPGP1 family.
CC       {ECO:0000256|ARBA:ARBA00006451}.
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DR   EMBL; GL377565; EFJ38457.1; -; Genomic_DNA.
DR   RefSeq; XP_002960918.1; XM_002960872.1.
DR   AlphaFoldDB; D8QQH0; -.
DR   STRING; 88036.D8QQH0; -.
DR   EnsemblPlants; EFJ38457; EFJ38457; SELMODRAFT_139516.
DR   GeneID; 9641747; -.
DR   Gramene; EFJ38457; EFJ38457; SELMODRAFT_139516.
DR   KEGG; smo:SELMODRAFT_139516; -.
DR   eggNOG; KOG2720; Eukaryota.
DR   HOGENOM; CLU_041964_1_0_1; -.
DR   InParanoid; D8QQH0; -.
DR   OMA; SKEMMIT; -.
DR   OrthoDB; 463544at2759; -.
DR   Proteomes; UP000001514; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0080048; F:GDP-D-glucose phosphorylase activity; IBA:GO_Central.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR   InterPro; IPR026506; GDPGP.
DR   PANTHER; PTHR20884; GDP-D-GLUCOSE PHOSPHORYLASE 1; 1.
DR   PANTHER; PTHR20884:SF8; GDP-D-GLUCOSE PHOSPHORYLASE 1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   389 AA;  44112 MW;  949940634CB3C04A CRC64;
     MLAIKRVPTV VSVNQDCGSV SRDCLQSCFL TGFDLPLFKY TKKMKTTELQ LLGDEEVPSS
     PPTIERSFLG TLLLSKWEER ASQGLFRYDV TACESRVLSG NYGFIAQLNE GRHLKKRLTE
     FRVDQVLQEF DPKKFNFSKV NRNEVLFQFG EGEEAGYYDI TPILSSPDFV LINVSPIEYG
     HVLLVPRLFD FVPQRLCAND LLLALYFTAE VDCPYFRVGY NSLGAFATIN HLHFQAYYLA
     YPFPVECASI TRINKGSLKS SLRISELVDY PVKGVVYESM DLNEIAISVA STCQELELRN
     IPFNLLICDC GTRVFLFPQC FARKQALHQV SQKVLDTQVN PAAWEIGGHI VLKRKEDYEH
     ATEEFVTALL AEVSLSDPDF QDVKNIICK
//
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