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Protein

GDP-D-glucose phosphorylase 1

Gene

GDPGP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Specific and highly efficient GDP-D-glucose phosphorylase regulating the levels of GDP-D-glucose in cells.1 Publication

Catalytic activityi

GDP-alpha-D-glucose + phosphate = alpha-D-glucose 1-phosphate + GDP.1 Publication

Kineticsi

kcat is 26 s(-1) at 31 degrees Celsius. The catalytic efficiency for GDP-D-glucose is 35-fold higher than for GDP-L-galactose.

  1. KM=2 µM for GDP-D-glucose (at 31 degrees Celsius)1 Publication
  2. KM=12 µM for GDP-L-galactose (at 31 degrees Celsius)1 Publication
  3. KM=42 µM for GDP-D-mannose (at 31 degrees Celsius)1 Publication
  4. KM=2.9 mM for inorganic phosphate (at 31 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei218 – 2181Tele-GMP-histidine intermediateBy similarity

    GO - Molecular functioni

    GO - Biological processi

    • glucose metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Guanine-nucleotide releasing factor, Hydrolase, Nucleotidyltransferase, Transferase

    Keywords - Ligandi

    Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:G66-31756-MONOMER.
    BRENDAi2.7.7.78. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GDP-D-glucose phosphorylase 1 (EC:2.7.7.78)
    Gene namesi
    Name:GDPGP1
    Synonyms:C15orf58
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:34360. GDPGP1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162378247.

    Polymorphism and mutation databases

    BioMutaiGDPGP1.
    DMDMi296434456.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 385385GDP-D-glucose phosphorylase 1PRO_0000336750Add
    BLAST

    Proteomic databases

    MaxQBiQ6ZNW5.
    PaxDbiQ6ZNW5.
    PRIDEiQ6ZNW5.

    Expressioni

    Gene expression databases

    BgeeiQ6ZNW5.
    CleanExiHS_C15orf58.
    ExpressionAtlasiQ6ZNW5. baseline and differential.
    GenevestigatoriQ6ZNW5.

    Organism-specific databases

    HPAiHPA048189.
    HPA059841.

    Interactioni

    Protein-protein interaction databases

    BioGridi133642. 2 interactions.
    STRINGi9606.ENSP00000368405.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6ZNW5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GDPGP1 family.Curated

    Phylogenomic databases

    eggNOGiNOG307761.
    GeneTreeiENSGT00390000016718.
    HOVERGENiHBG106673.
    InParanoidiQ6ZNW5.
    KOiK15630.
    OMAiASEEKAW.
    OrthoDBiEOG7M98H0.
    PhylomeDBiQ6ZNW5.
    TreeFamiTF313615.

    Family and domain databases

    InterProiIPR026506. GDPGP.
    [Graphical view]
    PANTHERiPTHR20884. PTHR20884. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q6ZNW5-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MALPHDSNET SYLLPPNNED WGRQTIPDFV YGQKDLMAEG IQWPRNAPGI
    60 70 80 90 100
    PDALPQSPFD AALCSAWKQR VELGLFRYRL RELQTQILPG AVGFVAQLNV
    110 120 130 140 150
    ERGVQRRPPQ TIKSVRQAFD PVQFNFNKIR PGEVLFRLHR EPDLPGTLLQ
    160 170 180 190 200
    EDILVVINVS PLEWGHVLLV PEPARQLPQR LLPGALRAGI EAVLLSLHPG
    210 220 230 240 250
    FRVGFNSLGG LASVNHLHLH GYYLAHRLPV EQAPSEPLDP GGHLHLLQDL
    260 270 280 290 300
    PAPGFLFYTR GPGPDLESLI SRVCRATDYL TDHEIAHNLF VTRGAPPGKT
    310 320 330 340 350
    SPSSALTGVR VILWARKSSF GIKDGEAFNV ALCELAGHLP VKTSQDFSSL
    360 370 380
    TEAAAVALIQ DCRLPPSQAE DVQAALVALM SQEEQ
    Length:385
    Mass (Da):42,362
    Last modified:May 18, 2010 - v2
    Checksum:i921A656C721876EC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231R → G in BAC85370 (PubMed:14702039).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti37 – 371M → T.1 Publication
    Corresponds to variant rs7171194 [ dbSNP | Ensembl ].
    VAR_043555
    Natural varianti264 – 2641P → T.1 Publication
    Corresponds to variant rs10152994 [ dbSNP | Ensembl ].
    VAR_043556
    Natural varianti307 – 3071T → I.1 Publication
    Corresponds to variant rs10153004 [ dbSNP | Ensembl ].
    VAR_043557

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK130527 mRNA. Translation: BAC85370.1.
    AC091167 Genomic DNA. No translation available.
    CCDSiCCDS32327.1.
    RefSeqiNP_001013679.2. NM_001013657.2.
    UniGeneiHs.304673.

    Genome annotation databases

    EnsembliENST00000329600; ENSP00000368405; ENSG00000183208.
    ENST00000558017; ENSP00000452793; ENSG00000183208.
    GeneIDi390637.
    KEGGihsa:390637.
    UCSCiuc002bpc.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK130527 mRNA. Translation: BAC85370.1.
    AC091167 Genomic DNA. No translation available.
    CCDSiCCDS32327.1.
    RefSeqiNP_001013679.2. NM_001013657.2.
    UniGeneiHs.304673.

    3D structure databases

    ProteinModelPortaliQ6ZNW5.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi133642. 2 interactions.
    STRINGi9606.ENSP00000368405.

    Polymorphism and mutation databases

    BioMutaiGDPGP1.
    DMDMi296434456.

    Proteomic databases

    MaxQBiQ6ZNW5.
    PaxDbiQ6ZNW5.
    PRIDEiQ6ZNW5.

    Protocols and materials databases

    DNASUi390637.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000329600; ENSP00000368405; ENSG00000183208.
    ENST00000558017; ENSP00000452793; ENSG00000183208.
    GeneIDi390637.
    KEGGihsa:390637.
    UCSCiuc002bpc.3. human.

    Organism-specific databases

    CTDi390637.
    GeneCardsiGC15P090778.
    HGNCiHGNC:34360. GDPGP1.
    HPAiHPA048189.
    HPA059841.
    neXtProtiNX_Q6ZNW5.
    PharmGKBiPA162378247.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG307761.
    GeneTreeiENSGT00390000016718.
    HOVERGENiHBG106673.
    InParanoidiQ6ZNW5.
    KOiK15630.
    OMAiASEEKAW.
    OrthoDBiEOG7M98H0.
    PhylomeDBiQ6ZNW5.
    TreeFamiTF313615.

    Enzyme and pathway databases

    BioCyciMetaCyc:G66-31756-MONOMER.
    BRENDAi2.7.7.78. 2681.

    Miscellaneous databases

    GenomeRNAii390637.
    NextBioi103948.
    PROiQ6ZNW5.

    Gene expression databases

    BgeeiQ6ZNW5.
    CleanExiHS_C15orf58.
    ExpressionAtlasiQ6ZNW5. baseline and differential.
    GenevestigatoriQ6ZNW5.

    Family and domain databases

    InterProiIPR026506. GDPGP.
    [Graphical view]
    PANTHERiPTHR20884. PTHR20884. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS THR-37; THR-264 AND ILE-307.
      Tissue: Salivary gland.
    2. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "A novel GDP-D-glucose phosphorylase involved in quality control of the nucleoside diphosphate sugar pool in Caenorhabditis elegans and mammals."
      Adler L.N., Gomez T.A., Clarke S.G., Linster C.L.
      J. Biol. Chem. 286:21511-21523(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS.

    Entry informationi

    Entry nameiGDPP1_HUMAN
    AccessioniPrimary (citable) accession number: Q6ZNW5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: May 18, 2010
    Last modified: April 29, 2015
    This is version 73 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    The orthologs in A.thaliana are GDP-L-galactose phosphorylases catalyzing the first reaction of the Smirnoff-Wheeler pathway, the major route to ascorbate biosynthesis in plants.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. SIMILARITY comments
      Index of protein domains and families
    5. Uncharacterized protein families (UPF)
      List of uncharacterized protein family (UPF) entries

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.