GDPP1_CAEEL
ID GDPP1_CAEEL Reviewed; 482 AA.
AC Q5ZR76; O16879;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=GDP-D-glucose phosphorylase 1 {ECO:0000250|UniProtKB:Q6ZNW5};
DE EC=2.7.7.78 {ECO:0000269|PubMed:21507950};
DE AltName: Full=Metabolite control phosphorylase 1 {ECO:0000312|WormBase:C10F3.4b};
GN Name=mcp-1 {ECO:0000312|WormBase:C10F3.4b};
GN ORFNames=C10F3.4 {ECO:0000312|WormBase:C10F3.4b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=21507950; DOI=10.1074/jbc.m111.238774;
RA Adler L.N., Gomez T.A., Clarke S.G., Linster C.L.;
RT "A novel GDP-D-glucose phosphorylase involved in quality control of the
RT nucleoside diphosphate sugar pool in Caenorhabditis elegans and mammals.";
RL J. Biol. Chem. 286:21511-21523(2011).
CC -!- FUNCTION: Specific and highly efficient GDP-D-glucose phosphorylase
CC regulating the levels of GDP-D-glucose in cells.
CC {ECO:0000269|PubMed:21507950}.
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:0000269|PubMed:21507950};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for GDP-D-glucose (at 26 degrees Celsius)
CC {ECO:0000269|PubMed:21507950};
CC KM=11 uM for GDP-L-galactose (at 26 degrees Celsius)
CC {ECO:0000269|PubMed:21507950};
CC KM=330 uM for GDP-D-mannose (at 26 degrees Celsius)
CC {ECO:0000269|PubMed:21507950};
CC KM=1.2 mM for inorganic phosphate (at 26 degrees Celsius)
CC {ECO:0000269|PubMed:21507950};
CC Note=kcat is 265 sec(-1). The catalytic efficiency for GDP-D-glucose
CC is 750-fold higher than for GDP-L-galactose.;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21507950}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:C10F3.4b};
CC IsoId=Q5ZR76-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:C10F3.4a};
CC IsoId=Q5ZR76-2; Sequence=VSP_041658;
CC -!- TISSUE SPECIFICITY: Expressed throughout the neuronal system, in the
CC spermatheca and anterior hypodermal cells.
CC {ECO:0000269|PubMed:21507950}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all the normal larval stages
CC observed. {ECO:0000269|PubMed:21507950}.
CC -!- MISCELLANEOUS: The orthologs in A.thaliana are GDP-L-galactose
CC phosphorylases catalyzing the first reaction of the Smirnoff-Wheeler
CC pathway, the major route to ascorbate biosynthesis in plants.
CC -!- SIMILARITY: Belongs to the GDPGP1 family. {ECO:0000305}.
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DR EMBL; FO080493; CCD64123.1; -; Genomic_DNA.
DR EMBL; FO080493; CCD64124.1; -; Genomic_DNA.
DR PIR; T32151; T32151.
DR RefSeq; NP_001023638.1; NM_001028467.3.
DR RefSeq; NP_001023639.1; NM_001028468.2. [Q5ZR76-1]
DR AlphaFoldDB; Q5ZR76; -.
DR STRING; 6239.C10F3.4b; -.
DR EPD; Q5ZR76; -.
DR PaxDb; Q5ZR76; -.
DR PeptideAtlas; Q5ZR76; -.
DR EnsemblMetazoa; C10F3.4a.1; C10F3.4a.1; WBGene00015678. [Q5ZR76-2]
DR EnsemblMetazoa; C10F3.4a.2; C10F3.4a.2; WBGene00015678. [Q5ZR76-2]
DR EnsemblMetazoa; C10F3.4b.1; C10F3.4b.1; WBGene00015678. [Q5ZR76-1]
DR GeneID; 178982; -.
DR KEGG; cel:CELE_C10F3.4; -.
DR UCSC; C10F3.4b; c. elegans.
DR CTD; 178982; -.
DR WormBase; C10F3.4a; CE30723; WBGene00015678; mcp-1. [Q5ZR76-1]
DR WormBase; C10F3.4b; CE37609; WBGene00015678; mcp-1. [Q5ZR76-2]
DR eggNOG; KOG2720; Eukaryota.
DR GeneTree; ENSGT00390000016718; -.
DR InParanoid; Q5ZR76; -.
DR OMA; FNYGLNC; -.
DR OrthoDB; 691047at2759; -.
DR PhylomeDB; Q5ZR76; -.
DR BRENDA; 2.7.7.78; 1045.
DR PRO; PR:Q5ZR76; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00015678; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0080048; F:GDP-D-glucose phosphorylase activity; IDA: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; IDA:WormBase.
DR InterPro; IPR026506; GDPGP.
DR PANTHER; PTHR20884; PTHR20884; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Guanine-nucleotide releasing factor;
KW Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..482
FT /note="GDP-D-glucose phosphorylase 1"
FT /id="PRO_0000412198"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 255
FT /note="Tele-GMP-histidine intermediate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..24
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_041658"
SQ SEQUENCE 482 AA; 55683 MW; E8E1D35BB4340B14 CRC64;
MEPFPRILDD RLPRNMRRPR PIDKMPMRKI VMLGANARTQ RSVSSIQLPA EYSPSASSAP
YFNYSPDDFI LDLRSHQSDE IYENGNSNHE KDEKKALKEL LHERWENAKQ YNAFNYPLNC
MYRCLDGKYD LSMQLNIERG ELRRKPMHFK NIKEPFNHLR FNFAKLHDHE ILFYLKCDTD
PISNDLLDRH LVAVNASPLE RDHSLIVPSV NKCSPQVLTL QAVRIAVDLM LLVDDDMFHI
LFNSLLGQAS VNHLHLHAMY WPYDSDLINR KCEPLHDVPN VYVIRPPVWI CPAIVFQLDS
LDNYEQFKMN IYKCVEHLTE SNQAHNLFLA RAQPIRTTGA EKEEDRRGER PQLVTCYVFP
RMNMIGAKPP SNFNPAANEL AGNLTSYTIR FFESANEQSV IRIIEEEASL DDDTFRSLCF
DLADVLIGRS VGTSRPQDLD TLAGLTSPEI DELRDSFQSF MPRSPSIRHR SSTRAQSDEG
SK
