ID F0LGU3_THEBM Unreviewed; 466 AA.
AC F0LGU3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 OrderedLocusNames=TERMP_00004 {ECO:0000313|EMBL:ADT82982.1};
OS Thermococcus barophilus (strain DSM 11836 / MP).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=391623 {ECO:0000313|EMBL:ADT82982.1, ECO:0000313|Proteomes:UP000007478};
RN [1] {ECO:0000313|EMBL:ADT82982.1, ECO:0000313|Proteomes:UP000007478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11836 / MP {ECO:0000313|Proteomes:UP000007478};
RX PubMed=21217005; DOI=10.1128/JB.01490-10;
RA Vannier P., Marteinsson V.T., Fridjonsson O.H., Oger P., Jebbar M.;
RT "Complete genome sequence of the hyperthermophilic, piezophilic,
RT heterotrophic, and carboxydotrophic archaeon Thermococcus barophilus MP.";
RL J. Bacteriol. 193:1481-1482(2011).
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; CP002372; ADT82982.1; -; Genomic_DNA.
DR AlphaFoldDB; F0LGU3; -.
DR KEGG; tba:TERMP_00004; -.
DR PATRIC; fig|391623.17.peg.4; -.
DR eggNOG; arCOG03370; Archaea.
DR HOGENOM; CLU_046643_0_0_2; -.
DR UniPathway; UPA00109; -.
DR Proteomes; UP000007478; 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; 3.30.1110.20; -; 1.
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; ADP-DEPENDENT GLUCOKINASE; 1.
DR PANTHER; PTHR21208:SF1; ADP-DEPENDENT GLUCOKINASE; 1.
DR Pfam; PF04587; ADP_PFK_GK; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR PROSITE; PS51255; ADPK; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00809};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00809};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00809};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00809};
KW Reference proteome {ECO:0000313|Proteomes:UP000007478};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00809}.
FT ACT_SITE 451
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809"
FT BINDING 42
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809"
FT BINDING 96
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809"
FT BINDING 120..121
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809"
FT BINDING 184
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809"
FT BINDING 305
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809"
FT BINDING 352..353
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809"
FT BINDING 440
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809"
FT BINDING 450
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809"
FT BINDING 451
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00809"
SQ SEQUENCE 466 AA; 53057 MW; FEAE62878A008F8A CRC64;
MKESLKEKIR IWKSLYVNAF ENATNALPGV RGVLLAYNTN IDALKYLDKE DLEERIEKVG
KKRVFELMEN PPEKVTSLEE LFAGILRSIK LGKAMEWFVE DRGVRNYLRE WGWDELRIGG
QAGIMANLLG GVYRIPTIVH VPQNPKLQAE LFVDGPIYVP VFDGEFKLVH PKEAVKENEE
ELIHYIFEFP RGFHVFDIVA PRENRFIANA DDYNAKVYIR DEFKEHFNKI VKNVDLAIIS
GLQVLKESYE DGTTYRDVLN EVEAQLDMLN KRNVKIHFEF AYTANKKVRG ALINLLPKFT
SVGLNEVELA SLMEIIGDEE LAREVLEGNV FSVIDAMHLL MDETGIKRIH FHTYGYYVAL
TQYRGEEVRD ALLFAALAAA AKAMYGSIEN LSQIRDALSV PTNERAFLTE EELEKEFGEV
ENGIIDMTDR QLAFIPTKIV ASPKSTVGIG DTISSSAFVS EFAMKR
//
