GLKA_THEKO
ID GLKA_THEKO Reviewed; 453 AA.
AC Q5JE39;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=ADP-dependent glucose/glucosamine kinase {ECO:0000255|HAMAP-Rule:MF_00809, ECO:0000305};
DE EC=2.7.1.- {ECO:0000269|PubMed:29146530};
DE EC=2.7.1.147 {ECO:0000255|HAMAP-Rule:MF_00809, ECO:0000269|PubMed:29146530};
DE AltName: Full=ADP-dependent glucokinase {ECO:0000255|HAMAP-Rule:MF_00809, ECO:0000303|PubMed:29146530};
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, ECO:0000303|PubMed:29146530};
DE Short=GlcN kinase {ECO:0000255|HAMAP-Rule:MF_00809, ECO:0000303|PubMed:29146530};
GN Name=glkA {ECO:0000255|HAMAP-Rule:MF_00809}; OrderedLocusNames=TK1110;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=29146530; DOI=10.1016/j.jbiosc.2017.10.005;
RA Aslam M., Takahashi N., Matsubara K., Imanaka T., Kanai T., Atomi H.;
RT "Identification of the glucosamine kinase in the chitinolytic pathway of
RT Thermococcus kodakarensis.";
RL J. Biosci. Bioeng. 125:320-326(2018).
CC -!- FUNCTION: Catalyzes the ADP-dependent phosphorylation of D-glucose to
CC D-glucose 6-phosphate and glucosamine to glucosamine 6-phosphate.
CC Involved in chitin degradation. {ECO:0000269|PubMed:29146530}.
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:29146530};
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:29146530};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.08 mM for ADP {ECO:0000269|PubMed:29146530};
CC Vmax=290 umol/min/mg enzyme toward glucose
CC {ECO:0000269|PubMed:29146530};
CC Vmax=142 umol/min/mg enzyme toward glucosamine
CC {ECO:0000269|PubMed:29146530};
CC Vmax=250 umol/min/mg enzyme toward ADP {ECO:0000269|PubMed:29146530};
CC Note=kcat is 248 sec(-1) with glucose as substrate. kcat is 120 sec(-
CC 1) with glucosamine as substrate. kcat is 210 sec(-1) with ADP as
CC substrate. {ECO:0000269|PubMed:29146530};
CC -!- PATHWAY: Glycan degradation; chitin degradation.
CC {ECO:0000269|PubMed:29146530}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis. {ECO:0000255|HAMAP-
CC Rule:MF_00809}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00809}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene severely affects growth in
CC chitin-containig media and leads to an almost complete loss of chitin-
CC dependent hydrogen production. {ECO:0000269|PubMed:29146530}.
CC -!- SIMILARITY: Belongs to the ADP-dependent glucokinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00809, ECO:0000305}.
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DR EMBL; AP006878; BAD85299.1; -; Genomic_DNA.
DR RefSeq; WP_011250061.1; NC_006624.1.
DR AlphaFoldDB; Q5JE39; -.
DR SMR; Q5JE39; -.
DR STRING; 69014.TK1110; -.
DR EnsemblBacteria; BAD85299; BAD85299; TK1110.
DR GeneID; 3234742; -.
DR KEGG; tko:TK1110; -.
DR PATRIC; fig|69014.16.peg.1086; -.
DR eggNOG; arCOG03370; Archaea.
DR HOGENOM; CLU_046643_0_0_2; -.
DR InParanoid; Q5JE39; -.
DR OMA; IHYIYEF; -.
DR OrthoDB; 15153at2157; -.
DR PhylomeDB; Q5JE39; -.
DR BioCyc; MetaCyc:MON-16781; -.
DR BRENDA; 2.7.1.147; 5246.
DR UniPathway; UPA00109; -.
DR UniPathway; UPA00349; -.
DR Proteomes; UP000000536; 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:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-UniPathway.
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 Carbohydrate metabolism; Cytoplasm; Glucose metabolism; Glycolysis; Kinase;
KW Magnesium; Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..453
FT /note="ADP-dependent glucose/glucosamine kinase"
FT /id="PRO_0000184774"
FT DOMAIN 1..453
FT /note="ADPK"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT ACT_SITE 439
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 33
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 87
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 111..112
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 175
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 265
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 291
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 341..342
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 428
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 438
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 439
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
FT BINDING 439
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00809"
SQ SEQUENCE 453 AA; 50735 MW; 3C2A09D9DEDE8577 CRC64;
MNWDGLYASA FERIRDNIGK VGNVLLAYNT NIDAIKYLER EDLERRIGAA GREEVLPYSE
KLPKRIESVP QLLGSILWSI RRGKAAELFV ESCSTRFYMR RWGWDELRMG GQVGIMANLL
GGVYGVPVIA HVPQLSRLQA ELFKDGPIYV PKVEGGKLKL VHPKEFKADE ENCIHYIYEF
PRGFRVFDFE APRENRFIGS ADDYNTNVVI RPEFEEHFGE IAEKTELAII SGLQALTEGN
YREPFETIKE HLDVLEGKGI PAHLEFAFTP DETVRKEILG VLGKFWSVGL NEVELASIMD
VMGEKTLAEK LLAHDPVDPI VVTKAMLKLA EKTGVRRIHF HTYGYYLALT DYRGEFVRDA
LLFAALAAAA KAKLGDVRNI DDVVKAMDVP VNEKAKGVEE ALTKEYGMEN GIAEVNGYQL
AFIPTKIVAK PKSTVGIGDT ISSSAFVGEF ALR
