GLKA_THELN
ID GLKA_THELN Reviewed; 467 AA.
AC Q7M537; H3ZQW1; Q7SIF2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=ADP-dependent glucose/glucosamine kinase {ECO:0000255|HAMAP-Rule:MF_00809, ECO:0000305};
DE EC=2.7.1.- {ECO:0000269|PubMed:11098152};
DE EC=2.7.1.147 {ECO:0000255|HAMAP-Rule:MF_00809, ECO:0000269|PubMed:11098152, ECO:0000269|PubMed:23818958};
DE AltName: Full=ADP-dependent glucokinase {ECO:0000255|HAMAP-Rule:MF_00809, ECO:0000303|PubMed:11098152};
DE Short=ADP-GK {ECO:0000255|HAMAP-Rule:MF_00809, ECO:0000303|PubMed:11098152};
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}; ORFNames=OCC_09701;
OS Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523849;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=11098152; DOI=10.1093/oxfordjournals.jbchem.a022836;
RA Koga S., Yoshioka I., Sakuraba H., Takahashi M., Sakasegawa S., Shimizu S.,
RA Ohshima T.;
RT "Biochemical characterization, cloning, and sequencing of ADP-dependent
RT (AMP-forming) glucokinase from two hyperthermophilic archaea, Pyrococcus
RT furiosus and Thermococcus litoralis.";
RL J. Biochem. 128:1079-1085(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=22493191; DOI=10.1128/jb.00123-12;
RA Gardner A.F., Kumar S., Perler F.B.;
RT "Genome sequence of the model hyperthermophilic archaeon Thermococcus
RT litoralis NS-C.";
RL J. Bacteriol. 194:2375-2376(2012).
RN [3]
RP MUTAGENESIS OF ASP-451.
RX PubMed=12909015; DOI=10.1016/s0022-2836(03)00792-7;
RA Ito S., Fushinobu S., Jeong J.-J., Yoshioka I., Koga S., Shoun H.,
RA Wakagi T.;
RT "Crystal structure of an ADP-dependent glucokinase from Pyrococcus
RT furiosus: implications for a sugar-induced conformational change in ADP-
RT dependent kinase.";
RL J. Mol. Biol. 331:871-883(2003).
RN [4] {ECO:0007744|PDB:1GC5}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ADP, AND SUBUNIT.
RX PubMed=11286887; DOI=10.1016/s0969-2126(01)00577-9;
RA Ito S., Fushinobu S., Yoshioka I., Koga S., Matsuzawa H., Wakagi T.;
RT "Structural basis for the ADP-specificity of a novel glucokinase from a
RT hyperthermophilic archaeon.";
RL Structure 9:205-214(2001).
RN [5] {ECO:0007744|PDB:4B8R, ECO:0007744|PDB:4B8S}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH AMP
RP AND GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=23818958; DOI=10.1371/journal.pone.0066687;
RA Rivas-Pardo J.A., Herrera-Morande A., Castro-Fernandez V., Fernandez F.J.,
RA Vega M.C., Guixe V.;
RT "Crystal structure, SAXS and kinetic mechanism of hyperthermophilic ADP-
RT dependent glucokinase from Thermococcus litoralis reveal a conserved
RT mechanism for catalysis.";
RL PLoS ONE 8:e66687-e66687(2013).
CC -!- FUNCTION: Catalyzes the ADP-dependent phosphorylation of D-glucose to
CC D-glucose 6-phosphate and glucosamine to glucosamine 6-phosphate
CC (PubMed:11098152, PubMed:23818958). Can also use CDP as the phosphoryl
CC group donor and D-1,5-anhydroglucitol as the phosphoryl group acceptor
CC (PubMed:11098152). {ECO:0000269|PubMed:11098152,
CC ECO:0000269|PubMed:23818958}.
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 ECO:0000269|PubMed:11098152, ECO:0000269|PubMed:23818958};
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 ECO:0000269|PubMed:11098152};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00809,
CC ECO:0000269|PubMed:11098152};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00809};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 mM for D-glucose (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:11098152};
CC KM=0.218 mM for D-glucose {ECO:0000269|PubMed:23818958};
CC KM=1.9 mM for D-glucosamine (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:11098152};
CC KM=2.0 mM for D-1,5-anhydroglucitol (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:11098152};
CC KM=0.057 mM for ADP (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:11098152};
CC KM=0.0086 mM for Mg-ADP {ECO:0000269|PubMed:23818958};
CC KM=0.56 mM for CDP (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:11098152};
CC KM=0.037 mM for magnesium ions (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:11098152};
CC Vmax=73 umol/min/mg enzyme with glucose and ADP as substrates (at 37
CC degrees Celsius) {ECO:0000269|PubMed:11098152};
CC pH dependence:
CC Optimum pH is about 7.5. {ECO:0000269|PubMed:11098152};
CC Temperature dependence:
CC Optimum temperature may be above 100 degrees Celsius. Activity
CC observed at 100 degrees Celsius is about 8 times that at 37 degrees
CC Celsius. Thermostable up to 95 degrees Celsius. Retains full activity
CC after heating at 90 degrees Celsius for 10 min and more than 95% of
CC the full activity at 100 degrees Celsius for 10 min.
CC {ECO:0000269|PubMed:11098152};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis. {ECO:0000255|HAMAP-
CC Rule:MF_00809}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11098152,
CC ECO:0000269|PubMed:11286887}.
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, ECO:0000305}.
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DR EMBL; E14589; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; CP006670; EHR77687.1; -; Genomic_DNA.
DR PIR; JC7551; JC7551.
DR PDB; 1GC5; X-ray; 2.30 A; A=1-467.
DR PDB; 4B8R; X-ray; 2.05 A; A=1-467.
DR PDB; 4B8S; X-ray; 2.58 A; A=1-467.
DR PDBsum; 1GC5; -.
DR PDBsum; 4B8R; -.
DR PDBsum; 4B8S; -.
DR AlphaFoldDB; Q7M537; -.
DR SMR; Q7M537; -.
DR STRING; 523849.OCC_09701; -.
DR EnsemblBacteria; EHR77687; EHR77687; OCC_09701.
DR KEGG; tlt:OCC_09701; -.
DR HOGENOM; CLU_046643_0_0_2; -.
DR OMA; IHYIYEF; -.
DR OrthoDB; 15153at2157; -.
DR BRENDA; 2.7.1.147; 6302.
DR UniPathway; UPA00109; -.
DR EvolutionaryTrace; Q7M537; -.
DR Proteomes; UP000015502; 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:0000287; F:magnesium ion binding; IEA:InterPro.
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; IPR015990; ADP_PFK/GK_arc.
DR InterPro; IPR031299; GlkA.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR21208; PTHR21208; 1.
DR Pfam; PF04587; ADP_PFK_GK; 1.
DR PIRSF; PIRSF015883; ADP-Pfk_glckin; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR PROSITE; PS51255; ADPK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Glucose metabolism;
KW Glycolysis; Kinase; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..467
FT /note="ADP-dependent glucose/glucosamine kinase"
FT /id="PRO_0000184775"
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 ECO:0000269|PubMed:23818958, ECO:0007744|PDB:4B8S"
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 120
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000269|PubMed:23818958,
FT ECO:0007744|PDB:4B8S"
FT BINDING 184
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809,
FT ECO:0000269|PubMed:23818958, ECO:0007744|PDB:4B8S"
FT BINDING 211
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000269|PubMed:23818958,
FT ECO:0007744|PDB:4B8S"
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 ECO:0000269|PubMed:11286887, ECO:0000269|PubMed:23818958,
FT ECO:0007744|PDB:1GC5, ECO:0007744|PDB:4B8S"
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 ECO:0000269|PubMed:11286887, ECO:0000269|PubMed:23818958,
FT ECO:0007744|PDB:1GC5, ECO:0007744|PDB:4B8S"
FT BINDING 440
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809,
FT ECO:0000269|PubMed:11286887, ECO:0000269|PubMed:23818958,
FT ECO:0007744|PDB:1GC5, ECO:0007744|PDB:4B8S"
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 ECO:0000269|PubMed:23818958, ECO:0007744|PDB:4B8S"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT MUTAGEN 451
FT /note="D->A,N,S: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:12909015"
FT HELIX 5..26
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:4B8R"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:4B8R"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 49..59
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:4B8R"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:4B8R"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:4B8R"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:4B8R"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:4B8R"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:4B8R"
FT STRAND 154..163
FT /evidence="ECO:0007829|PDB:4B8R"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:4B8R"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:4B8R"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:4B8R"
FT TURN 212..217
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:4B8R"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 256..271
FT /evidence="ECO:0007829|PDB:4B8R"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 286..293
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 294..298
FT /evidence="ECO:0007829|PDB:4B8R"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 319..326
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 330..344
FT /evidence="ECO:0007829|PDB:4B8R"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:4B8R"
FT STRAND 354..363
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 367..385
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 391..399
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 404..416
FT /evidence="ECO:0007829|PDB:4B8R"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:4B8R"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:4B8R"
FT STRAND 431..436
FT /evidence="ECO:0007829|PDB:4B8R"
FT HELIX 449..465
FT /evidence="ECO:0007829|PDB:4B8R"
SQ SEQUENCE 467 AA; 53621 MW; 8E8245E8C07212F1 CRC64;
MKESLKDRIR LWKRLYVNAF ENALNAIPNV KGVLLAYNTN IDAIKYLDKD DLEKRVTEIG
KEKVFEIIEN PPEKISSIEE LLGGILRSIK LGKAMEWFVE SEEVRRYLRE WGWDELRIGG
QAGIMANLLG GVYRIPTIVH VPQNPKLQAE LFVDGPIYVP VFEGNKLKLV HPKDAIAEEE
ELIHYIYEFP RGFQVFDVQA PRENRFIANA DDYNARVYMR REFREGFEEI TRNVELAIIS
GLQVLKEYYP DGTTYRDVLD RVESHLNILN RYNVKSHFEF AYTANRRVRE ALVELLPKFT
SVGLNEVELA SIMEIIGDEE LAKEVLEGHI FSVIDAMNVL MDETGIERIH FHTYGYYLAL
TQYRGEEVRD ALLFASLAAA AKAMKGNLER IEQIRDALSV PTNERAIVLE EELEKEFTEF
ENGLIDMVDR QLAFVPTKIV ASPKSTVGIG DTISSSAFVS EFGMRKR
