GLKA_THESM
ID GLKA_THESM Reviewed; 467 AA.
AC C6A124;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=ADP-dependent glucose/glucosamine kinase {ECO:0000255|HAMAP-Rule:MF_00809};
DE EC=2.7.1.- {ECO:0000255|HAMAP-Rule:MF_00809};
DE EC=2.7.1.147 {ECO:0000255|HAMAP-Rule:MF_00809};
DE AltName: Full=ADP-dependent glucokinase {ECO:0000255|HAMAP-Rule:MF_00809};
DE Short=ADP-GK {ECO:0000255|HAMAP-Rule:MF_00809};
DE Short=ADPGK {ECO:0000255|HAMAP-Rule:MF_00809};
DE AltName: Full=Glucosamine kinase {ECO:0000255|HAMAP-Rule:MF_00809};
DE Short=GlcN kinase {ECO:0000255|HAMAP-Rule:MF_00809};
GN Name=glkA {ECO:0000255|HAMAP-Rule:MF_00809}; OrderedLocusNames=TSIB_0252;
OS Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=604354;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12597 / MM 739;
RX PubMed=19447963; DOI=10.1128/aem.00718-09;
RA Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT analysis.";
RL Appl. Environ. Microbiol. 75:4580-4588(2009).
CC -!- FUNCTION: Catalyzes the ADP-dependent phosphorylation of D-glucose to
CC D-glucose 6-phosphate and glucosamine to glucosamine 6-phosphate.
CC {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00809};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00809};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00809};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis. {ECO:0000255|HAMAP-
CC Rule:MF_00809}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00809}.
CC -!- SIMILARITY: Belongs to the ADP-dependent glucokinase family.
CC {ECO:0000255|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; CP001463; ACS89319.1; -; Genomic_DNA.
DR RefSeq; WP_012766280.1; NC_012883.1.
DR AlphaFoldDB; C6A124; -.
DR SMR; C6A124; -.
DR STRING; 604354.TSIB_0252; -.
DR EnsemblBacteria; ACS89319; ACS89319; TSIB_0252.
DR GeneID; 8095225; -.
DR KEGG; tsi:TSIB_0252; -.
DR eggNOG; arCOG03370; Archaea.
DR HOGENOM; CLU_046643_0_0_2; -.
DR OMA; IHYIYEF; -.
DR OrthoDB; 15153at2157; -.
DR UniPathway; UPA00109; -.
DR Proteomes; UP000009079; 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; Cytoplasm; Glucose metabolism; Glycolysis; Kinase;
KW Magnesium; Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..467
FT /note="ADP-dependent glucose/glucosamine kinase"
FT /id="PRO_1000213009"
FT DOMAIN 10..467
FT /note="ADPK"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT ACT_SITE 451
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 42
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 96
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 120..121
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 184
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 305
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 352..353
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 440
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 450
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 451
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
SQ SEQUENCE 467 AA; 53457 MW; 15CF2405F8039EAC CRC64;
MKESLKERIK LWKNLYMNAF ENAVNAIPNV EGVLLAYNTN IDVIKYLNKD DLERRINQIG
KERVFEVIKA PTERISSLEH LFGGILRSIK LGKAIEWFVE NEEIRRYLRE WGWDELRIGG
QAGIMANLIG GVYRIPTIVH VPQNPKLQAD LFVDGPIYVP IFEGKELKLV HPKEAVKEEN
ELIHYIYEFP RGFQVFDIQA PRENRFIANA DDYNARVYMR KEFKESFEKI AKGVELAIIS
GLQVLKEYYS DGTTYRDVLD RVESHLNILN RYGVRSHFEF AYTPNRLVRE ELIGILSKFT
SVGLNEVELA SIVEIIGDET LAKEVLEGHV FPIIDAINLL MDETGIDRIH LHTYGYYLAL
TKYRSEEVRD ALLFASLAAA AKAMKGNIEK IDHVKDALSV PTNERAIVFE EELEKEFTEF
ENGLIDMVDR QLAFVPTKIV TSPKSTVGIG DTISSSAFVS EFAMRKS
