ADPGK_CAEEL
ID ADPGK_CAEEL Reviewed; 502 AA.
AC Q86S40;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable ADP-dependent glucokinase;
DE Short=ADP-GK;
DE Short=ADPGK;
DE EC=2.7.1.147;
DE Flags: Precursor;
GN ORFNames=C50D2.7;
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-89, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-glucose to D-glucose 6-
CC phosphate using ADP as the phosphate donor. GDP and CDP can replace
CC ADP, but with reduced efficiency (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + D-glucose = AMP + D-glucose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:11460, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:61548, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=2.7.1.147;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00584};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00584};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis. {ECO:0000255|PROSITE-
CC ProRule:PRU00584}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ADP-dependent glucokinase family.
CC {ECO:0000305}.
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DR EMBL; FO080633; CCD65339.1; -; Genomic_DNA.
DR RefSeq; NP_493657.2; NM_061256.4.
DR AlphaFoldDB; Q86S40; -.
DR SMR; Q86S40; -.
DR STRING; 6239.C50D2.7; -.
DR iPTMnet; Q86S40; -.
DR EPD; Q86S40; -.
DR PaxDb; Q86S40; -.
DR PeptideAtlas; Q86S40; -.
DR EnsemblMetazoa; C50D2.7.1; C50D2.7.1; WBGene00016810.
DR GeneID; 173393; -.
DR KEGG; cel:CELE_C50D2.7; -.
DR UCSC; C50D2.7.1; c. elegans.
DR CTD; 173393; -.
DR WormBase; C50D2.7; CE33040; WBGene00016810; -.
DR eggNOG; KOG4184; Eukaryota.
DR GeneTree; ENSGT00390000017953; -.
DR HOGENOM; CLU_032362_0_0_1; -.
DR InParanoid; Q86S40; -.
DR OMA; MWRKASA; -.
DR OrthoDB; 1036373at2759; -.
DR PhylomeDB; Q86S40; -.
DR Reactome; R-CEL-70171; Glycolysis.
DR UniPathway; UPA00109; -.
DR PRO; PR:Q86S40; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00016810; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043843; F:ADP-specific glucokinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR007666; ADP_PFK/GK.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR21208; PTHR21208; 1.
DR Pfam; PF04587; ADP_PFK_GK; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR PROSITE; PS51255; ADPK; 1.
PE 1: Evidence at protein level;
KW Glycolysis; Glycoprotein; Kinase; Magnesium; Metal-binding;
KW Reference proteome; Secreted; Signal; Transferase.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..502
FT /note="Probable ADP-dependent glucokinase"
FT /id="PRO_0000346790"
FT DOMAIN 44..497
FT /note="ADPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00584"
FT ACT_SITE 481
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00584"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00584"
FT BINDING 320
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00584"
FT BINDING 481
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00584"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 502 AA; 56762 MW; 1D9B57E5382FFF73 CRC64;
MFSETFVPSI FSYKHRLLHL SVLFFIVPYW YSYYNDQHRL SSYSVETAMF LSWERAIVKP
GAMFKKAVIG FNCNVDLIVS GVRVVDALNT TCSEGKDQET LETLADLHQT FAHFFQRGAA
AERYMSSEDQ FNLLVAESEA STRSHHHIGG NAALMADRIA ANFPSTEVYL VGPIGPRSQA
LLHPSVKRTN STRILKDELH VILEYKQGEI LGDWVAPSSS RFITSHDHFS GSMVVMEMFF
KAIAQFRPDL VVITGVHLLE FQSKEMRQEK MRLIKRNLLQ IPPKVPIHLE LGSLADEIFS
TDVINKILPY VDSLGINEQE LTFLSHIANG PHMEEYPVQA GTVHVHKVVE MLHWLLKTYG
RDPTGQIASK TGYRLSRIHF HCLTYHIMVS SGTDWSNLAA GLAAGARIAG RLSCNIGANT
MDSELLEIRT PANFVLDKKI EKNYQFEAHN PIASWMREDV LFVFTPVLVC RLPSKTVGID
DAISATGLLY SQFYRLNRPT HW
