ID   ADPGK_BOVIN             Reviewed;         497 AA.
AC   A2VE47;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   02-SEP-2026, entry version 88.
DE   RecName: Full=ADP-dependent glucokinase;
DE            Short=ADP-GK;
DE            Short=ADPGK;
DE            EC=2.7.1.147;
DE   Flags: Precursor;
GN   Name=ADPGK;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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=D-glucose + ADP = D-glucose 6-phosphate + AMP + 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; Evidence={ECO:0000255|PROSITE-
CC         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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC133568; AAI33569.1; -; mRNA.
DR   RefSeq; NP_001075907.1; NM_001082438.2.
DR   AlphaFoldDB; A2VE47; -.
DR   SMR; A2VE47; -.
DR   FunCoup; A2VE47; 2091.
DR   STRING; 9913.ENSBTAP00000002065; -.
DR   PaxDb; 9913-ENSBTAP00000002065; -.
DR   Ensembl; ENSBTAT00000002065.5; ENSBTAP00000002065.4; ENSBTAG00000001578.5.
DR   Ensembl; ENSBTAT00085039037; ENSBTAP00085036395; ENSBTAG00085008776.
DR   Ensembl; ENSBTAT00090057310; ENSBTAP00090030451; ENSBTAG00090027234.
DR   GeneID; 518158; -.
DR   KEGG; bta:518158; -.
DR   CTD; 83440; -.
DR   VEuPathDB; HostDB:ENSBTAG00000001578; -.
DR   VGNC; VGNC:25689; ADPGK.
DR   eggNOG; KOG4184; Eukaryota.
DR   GeneTree; ENSGT00390000017953; -.
DR   HOGENOM; CLU_032362_0_0_1; -.
DR   InParanoid; A2VE47; -.
DR   OMA; FIHYMGR; -.
DR   OrthoDB; 5847021at2759; -.
DR   Reactome; R-BTA-70171; Glycolysis.
DR   UniPathway; UPA00109; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000001578; Expressed in diaphragm and 105 other cell types or 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:0006006; P:glucose metabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01938; ADPGK_ADPPFK; 1.
DR   FunFam; 3.40.1190.20:FF:000020; ADP-dependent glucokinase isoform X1; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR007666; ADP_PFK/GK.
DR   InterPro; IPR029056; Ribokinase-like.
DR   PANTHER; PTHR21208; ADP-DEPENDENT GLUCOKINASE; 1.
DR   PANTHER; PTHR21208:SF0; ADP-DEPENDENT GLUCOKINASE; 1.
DR   Pfam; PF04587; ADP_PFK_GK; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
DR   PROSITE; PS51255; ADPK; 1.
PE   2: Evidence at transcript level;
KW   Glycolysis; Kinase; Magnesium; Metal-binding; Reference proteome; Secreted;
KW   Signal; Transferase.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..497
FT                   /note="ADP-dependent glucokinase"
FT                   /id="PRO_0000346789"
FT   DOMAIN          52..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         297
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00584"
FT   BINDING         328
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"
SQ   SEQUENCE   497 AA;  54086 MW;  AFFC94E7DEB10179 CRC64;
     MALWRGSAYA GFLALAVGCV FLLEPQLPGS ALRSLWSSLQ LGPAPAPPGV GSPEGRLAAA
     WDALIVRPAR RWRRVAVGVN ACVDVVLSGV KLLQALGLSP GNGKDHSELH SRNDLEEAFV
     HFMGKGAAAE RFFSDKETFH DIAQVASEFP EAQHYVGGNA ALIGQKFAAN SDLKVLLCGP
     VGPKLHELLD DNVFVPPESL QEVDEFHLIL EYQAGEEWDQ LKAPHANRFI FSHDLSNGAM
     NMLEVFVSSL EEFQPDLVVL SGLHMMEGQS KEFQRKRLLE VVTSISDIPT GVPVHLELAS
     MTNKELMSTI VHQQVFPAVT SLGLNEQELL FLSQSASGPH SSLSSWNGVP DVGVVSDILF
     WILKEHGKSE SRASDLSRIH FHTLAYHILA TVDGHWANQL AAVAAGARVA ATQACATETI
     DTRRVSLKAP HEFMTSRLEA GSRVVLNPNE PVVEWHREGV SFHFTPVLVC KDPVRTVGLG
     DAISAEGLFY SEVHPHL
//