GLKA_PYRFU
ID GLKA_PYRFU Reviewed; 455 AA.
AC Q9V2Z6; Q7LX13;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 126.
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:8530474};
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}; OrderedLocusNames=PF0312;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10409652; DOI=10.1074/jbc.274.30.21023;
RA Tuininga J.E., Verhees C.H., van der Oost J., Kengen S.W.M., Stams A.J.M.,
RA de Vos W.M.;
RT "Molecular and biochemical characterization of the ADP-dependent
RT phosphofructokinase from the hyperthermophilic archaeon Pyrococcus
RT furiosus.";
RL J. Biol. Chem. 274:21023-21028(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-40, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [4]
RP PROTEIN SEQUENCE OF 2-11, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND COFACTOR.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=8530474; DOI=10.1074/jbc.270.51.30453;
RA Kengen S.W.M., Tuininga J.E., de Bok F.A.M., Stams A.J.M., de Vos W.M.;
RT "Purification and characterization of a novel ADP-dependent glucokinase
RT from the hyperthermophilic archaeon Pyrococcus furiosus.";
RL J. Biol. Chem. 270:30453-30457(1995).
RN [5] {ECO:0007744|PDB:1UA4}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH AMP AND GLUCOSE, AND
RP SUBUNIT.
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).
CC -!- FUNCTION: Catalyzes the ADP-dependent phosphorylation of D-glucose to
CC D-glucose 6-phosphate and glucosamine to glucosamine 6-phosphate. Can
CC also use CDP as the phosphoryl group donor and D-1,5-anhydroglucitol as
CC the phosphoryl group acceptor. {ECO:0000269|PubMed:11098152,
CC ECO:0000269|PubMed:8530474}.
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:8530474};
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, ECO:0000269|PubMed:8530474};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00584};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.64 mM for D-glucose (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:11098152, ECO:0000269|PubMed:8530474};
CC KM=0.73 mM for D-glucose (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:11098152, ECO:0000269|PubMed:8530474};
CC KM=0.54 mM for D-glucosamine (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:11098152, ECO:0000269|PubMed:8530474};
CC KM=8.3 mM for D-1,5-anhydroglucitol (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:11098152, ECO:0000269|PubMed:8530474};
CC KM=0.07 mM for ADP (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:11098152, ECO:0000269|PubMed:8530474};
CC KM=0.033 mM for ADP (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:11098152, ECO:0000269|PubMed:8530474};
CC KM=0.83 mM for CDP (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:11098152, ECO:0000269|PubMed:8530474};
CC KM=0.041 mM for magnesium ions (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:11098152, ECO:0000269|PubMed:8530474};
CC Vmax=249 umol/min/mg enzyme toward glucose (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:11098152, ECO:0000269|PubMed:8530474};
CC Vmax=194 umol/min/mg enzyme toward ADP (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:11098152, ECO:0000269|PubMed:8530474};
CC Vmax=160 umol/min/mg enzyme toward glucose (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:11098152, ECO:0000269|PubMed:8530474};
CC pH dependence:
CC Optimum pH is about 7.5. {ECO:0000269|PubMed:11098152,
CC ECO:0000269|PubMed:8530474};
CC Temperature dependence:
CC Optimum temperature is 105 degrees Celsius. Activity observed at 100
CC degrees Celsius is about 8 times that at 37 degrees Celsius.
CC Thermostable up to 95 degrees Celsius. Retains full activity after
CC heating at 90 degrees Celsius for 10 minutes and more than 95% of the
CC full activity at 100 degrees Celsius for 10 minutes. Has a half-life
CC of 220 minutes at 100 degrees Celsius. Inactive after heating at 110
CC degrees Celsius for 30 minutes. {ECO:0000269|PubMed:11098152,
CC ECO:0000269|PubMed:8530474};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis. {ECO:0000255|HAMAP-
CC Rule:MF_00809}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11098152,
CC ECO:0000269|PubMed:12909015}.
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; AF127910; AAD48401.1; -; Genomic_DNA.
DR EMBL; E14588; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; AE009950; AAL80436.1; -; Genomic_DNA.
DR PIR; JC7550; JC7550.
DR RefSeq; WP_011011427.1; NC_018092.1.
DR PDB; 1UA4; X-ray; 1.90 A; A=1-455.
DR PDBsum; 1UA4; -.
DR AlphaFoldDB; Q9V2Z6; -.
DR SMR; Q9V2Z6; -.
DR STRING; 186497.PF0312; -.
DR PRIDE; Q9V2Z6; -.
DR EnsemblBacteria; AAL80436; AAL80436; PF0312.
DR GeneID; 41712104; -.
DR KEGG; pfu:PF0312; -.
DR PATRIC; fig|186497.12.peg.327; -.
DR eggNOG; arCOG03370; Archaea.
DR HOGENOM; CLU_046643_0_0_2; -.
DR OMA; IHYIYEF; -.
DR OrthoDB; 15153at2157; -.
DR PhylomeDB; Q9V2Z6; -.
DR BioCyc; MetaCyc:MON-11804; -.
DR BRENDA; 2.7.1.147; 5243.
DR SABIO-RK; Q9V2Z6; -.
DR UniPathway; UPA00109; -.
DR EvolutionaryTrace; Q9V2Z6; -.
DR PRO; PR:Q9V2Z6; -.
DR Proteomes; UP000001013; 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;
KW Direct protein sequencing; Glucose metabolism; Glycolysis; Kinase;
KW Magnesium; Metal-binding; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11098152,
FT ECO:0000269|PubMed:8530474"
FT CHAIN 2..455
FT /note="ADP-dependent glucose/glucosamine kinase"
FT /id="PRO_0000184772"
FT DOMAIN 2..455
FT /note="ADPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00584"
FT ACT_SITE 440
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00584"
FT BINDING 34
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809,
FT ECO:0000269|PubMed:12909015, ECO:0007744|PDB:1UA4"
FT BINDING 88
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809,
FT ECO:0000269|PubMed:12909015, ECO:0007744|PDB:1UA4"
FT BINDING 112..113
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809,
FT ECO:0000269|PubMed:12909015, ECO:0007744|PDB:1UA4"
FT BINDING 176
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809,
FT ECO:0000269|PubMed:12909015, ECO:0007744|PDB:1UA4"
FT BINDING 195
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000269|PubMed:12909015,
FT ECO:0007744|PDB:1UA4"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00584"
FT BINDING 292
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809,
FT ECO:0000269|PubMed:12909015, ECO:0007744|PDB:1UA4"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00584"
FT BINDING 342..343
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809,
FT ECO:0000269|PubMed:12909015, ECO:0007744|PDB:1UA4"
FT BINDING 429
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809,
FT ECO:0000269|PubMed:12909015, ECO:0007744|PDB:1UA4"
FT BINDING 439
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809,
FT ECO:0000269|PubMed:12909015, ECO:0007744|PDB:1UA4"
FT BINDING 440
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809,
FT ECO:0000269|PubMed:12909015, ECO:0007744|PDB:1UA4"
FT BINDING 440
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00584"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:1UA4"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:1UA4"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 53..61
FT /evidence="ECO:0007829|PDB:1UA4"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:1UA4"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:1UA4"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:1UA4"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:1UA4"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:1UA4"
FT STRAND 146..155
FT /evidence="ECO:0007829|PDB:1UA4"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1UA4"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:1UA4"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:1UA4"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:1UA4"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 243..258
FT /evidence="ECO:0007829|PDB:1UA4"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 273..282
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:1UA4"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 293..302
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 306..311
FT /evidence="ECO:0007829|PDB:1UA4"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 320..334
FT /evidence="ECO:0007829|PDB:1UA4"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:1UA4"
FT STRAND 344..353
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 356..375
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 381..386
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 396..407
FT /evidence="ECO:0007829|PDB:1UA4"
FT STRAND 413..416
FT /evidence="ECO:0007829|PDB:1UA4"
FT STRAND 419..425
FT /evidence="ECO:0007829|PDB:1UA4"
FT HELIX 438..452
FT /evidence="ECO:0007829|PDB:1UA4"
SQ SEQUENCE 455 AA; 51266 MW; 8262ACBF19BED113 CRC64;
MPTWEELYKN AIEKAIKSVP KVKGVLLGYN TNIDAIKYLD SKDLEERIIK AGKEEVIKYS
EELPDKINTV SQLLGSILWS IRRGKAAELF VESCPVRFYM KRWGWNELRM GGQAGIMANL
LGGVYGVPVI VHVPQLSRLQ ANLFLDGPIY VPTLENGEVK LIHPKEFSGD EENCIHYIYE
FPRGFRVFEF EAPRENRFIG SADDYNTTLF IREEFRESFS EVIKNVQLAI LSGLQALTKE
NYKEPFEIVK SNLEVLNERE IPVHLEFAFT PDEKVREEIL NVLGMFYSVG LNEVELASIM
EILGEKKLAK ELLAHDPVDP IAVTEAMLKL AKKTGVKRIH FHTYGYYLAL TEYKGEHVRD
ALLFAALAAA AKAMKGNITS LEEIREATSV PVNEKATQVE EKLRAEYGIK EGIGEVEGYQ
IAFIPTKIVA KPKSTVGIGD TISSSAFIGE FSFTL
