ID A0A218NZQ0_THECE Unreviewed; 454 AA. AC A0A218NZQ0; DT 27-SEP-2017, integrated into UniProtKB/TrEMBL. DT 27-SEP-2017, sequence version 1. DT 03-AUG-2022, entry version 23. DE RecName: Full=ADP-dependent glucose/glucosamine kinase {ECO:0000256|HAMAP-Rule:MF_00809}; DE EC=2.7.1.147 {ECO:0000256|HAMAP-Rule:MF_00809}; DE AltName: Full=ADP-dependent glucokinase {ECO:0000256|HAMAP-Rule:MF_00809}; DE Short=ADP-GK {ECO:0000256|HAMAP-Rule:MF_00809}; DE Short=ADPGK {ECO:0000256|HAMAP-Rule:MF_00809}; DE AltName: Full=Glucosamine kinase {ECO:0000256|HAMAP-Rule:MF_00809}; DE Short=GlcN kinase {ECO:0000256|HAMAP-Rule:MF_00809}; GN Name=glkA {ECO:0000256|HAMAP-Rule:MF_00809}; GN ORFNames=A3L02_00520 {ECO:0000313|EMBL:ASI98158.1}; OS Thermococcus celer Vu 13 = JCM 8558. OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=1293037 {ECO:0000313|EMBL:ASI98158.1, ECO:0000313|Proteomes:UP000197156}; RN [1] {ECO:0000313|EMBL:ASI98158.1, ECO:0000313|Proteomes:UP000197156} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Vu 13 {ECO:0000313|EMBL:ASI98158.1, RC ECO:0000313|Proteomes:UP000197156}; RA Oger P.M.; RT "Complete genome sequence of Thermococcus celer."; RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the ADP-dependent phosphorylation of D-glucose to CC D-glucose 6-phosphate and glucosamine to glucosamine 6-phosphate. CC {ECO:0000256|HAMAP-Rule:MF_00809}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ADP + D-glucosamine = AMP + D-glucosamine 6-phosphate + H(+); CC Xref=Rhea:RHEA:62084, ChEBI:CHEBI:15378, ChEBI:CHEBI:58723, CC ChEBI:CHEBI:58725, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00809}; 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; Evidence={ECO:0000256|HAMAP-Rule:MF_00809}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00809}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00809}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis. {ECO:0000256|HAMAP- CC Rule:MF_00809}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00809}. CC -!- SIMILARITY: Belongs to the ADP-dependent glucokinase family. CC {ECO:0000256|HAMAP-Rule:MF_00809}. 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; CP014854; ASI98158.1; -; Genomic_DNA. DR EnsemblBacteria; ASI98158; ASI98158; A3L02_00520. DR KEGG; tce:A3L02_00520; -. DR UniPathway; UPA00109; -. DR Proteomes; UP000197156; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043843; F:ADP-specific glucokinase activity; IEA:UniProtKB-EC. DR GO; GO:0004340; F:glucokinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.1190.20; -; 1. DR HAMAP; MF_00809; ADP_glucokinase; 1. DR InterPro; IPR007666; ADP_PFK/GK. DR InterPro; IPR031299; GlkA. 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 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00809}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00809}; KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526, ECO:0000256|HAMAP- KW Rule:MF_00809}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP- KW Rule:MF_00809}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00809, ECO:0000313|EMBL:ASI98158.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00809}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00809}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00809}. FT REGION 111..112 FT /note="Glucose binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809" FT ACT_SITE 439 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809" FT BINDING 33 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809" FT BINDING 87 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809" FT BINDING 175 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809" FT BINDING 265 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809" FT BINDING 291 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809" FT BINDING 294 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809" FT BINDING 341..342 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809" FT BINDING 428 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809" FT BINDING 438 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809" FT BINDING 439 FT /ligand="D-glucose" FT /ligand_id="ChEBI:CHEBI:4167" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809" FT BINDING 439 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809" SQ SEQUENCE 454 AA; 50717 MW; BCA1E9001AD1530C CRC64; MPWDALYSSA FNKVRENIGR VGEVLLAYNT NIDAIRYLDS GDLEGRIEKA GKDEVLRYSE ELPERITSIG ELLGGILWSV KRGKAAELFV ESCTVRFYMK RWGWDELRMG GQVGIMANLL GGVYGVPVIA HVPQLSRLQA GLFKEGPIHV PKVEDGRLRL VHPRDFAGDE ENCFHYIYEF PRGFGVFEFR APRENRFIGS ADDYNPNVYI RPEFREHFEE IAEKAELGII SGLQALRREN YREPFEELKR HLEVLGERNV PVHLEFAFTA DETVRKALVG LLGSFHSVGL NEVEMASIME VLGEKGLREK LLASDPVDPV VVTGAMLKLA EKTGVRRIHF HTYGYYLALT AYKGEFVRDA LLFASLAAAA KAKLGDVRSI DDIVRAMDVP VNEKAMAVEK RLAKAYGMER GIAEVGGYQL SFVPTKIVAK PKSTVGIGDT ISSSAFVGEF ALRP //