GLK_THEMA
ID GLK_THEMA Reviewed; 317 AA.
AC Q9X1I0;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Glucokinase {ECO:0000305};
DE EC=2.7.1.2 {ECO:0000269|PubMed:14553940};
DE AltName: Full=ATP-dependent glucokinase {ECO:0000303|PubMed:14553940};
DE Short=ATP-GLK {ECO:0000303|PubMed:14553940};
DE AltName: Full=Glucose kinase {ECO:0000305};
GN Name=glk {ECO:0000303|PubMed:14553940};
GN OrderedLocusNames=TM_1469 {ECO:0000312|EMBL:AAD36537.1};
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RX PubMed=14553940; DOI=10.1016/s0378-1097(03)00642-6;
RA Hansen T., Schoenheit P.;
RT "ATP-dependent glucokinase from the hyperthermophilic bacterium Thermotoga
RT maritima represents an extremely thermophilic ROK glucokinase with high
RT substrate specificity.";
RL FEMS Microbiol. Lett. 226:405-411(2003).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-glucose to D-glucose 6-
CC phosphate using ATP as the phosphate donor. Can also phosphorylate 2-
CC deoxyglucose, with lower efficiency. ITP can also serve as a phosphoryl
CC donor. {ECO:0000269|PubMed:14553940}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.2;
CC Evidence={ECO:0000269|PubMed:14553940};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:14553940};
CC Note=Mg(2+) is the most effective ion. It can be efficiently replaced
CC with Mn(2+) or Co(2+) and to some extent with Ni(2+).
CC {ECO:0000269|PubMed:14553940};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 mM for glucose {ECO:0000269|PubMed:14553940};
CC KM=1.1 mM for 2-deoxyglucose {ECO:0000269|PubMed:14553940};
CC KM=0.36 mM for ATP {ECO:0000269|PubMed:14553940};
CC pH dependence:
CC Optimum pH is 7.3. {ECO:0000269|PubMed:14553940};
CC Temperature dependence:
CC Optimum temperature is 93 degrees Celsius.
CC {ECO:0000269|PubMed:14553940};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14553940}.
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
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DR EMBL; AE000512; AAD36537.1; -; Genomic_DNA.
DR PIR; F72246; F72246.
DR RefSeq; NP_229269.1; NC_000853.1.
DR AlphaFoldDB; Q9X1I0; -.
DR SMR; Q9X1I0; -.
DR STRING; 243274.THEMA_06955; -.
DR EnsemblBacteria; AAD36537; AAD36537; TM_1469.
DR KEGG; tma:TM1469; -.
DR PATRIC; fig|243274.5.peg.1485; -.
DR InParanoid; Q9X1I0; -.
DR OMA; DHLVMIT; -.
DR BioCyc; MetaCyc:MON-6111; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004340; F:glucokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000600; ROK.
DR InterPro; IPR004654; ROK_glcA.
DR PANTHER; PTHR18964; PTHR18964; 1.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
DR TIGRFAMs; TIGR00744; ROK_glcA_fam; 1.
DR PROSITE; PS01125; ROK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Glucose metabolism; Kinase;
KW Magnesium; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..317
FT /note="Glucokinase"
FT /id="PRO_0000448972"
SQ SEQUENCE 317 AA; 33891 MW; 30B1DE9D69FFFA3F CRC64;
MPKLKLIGVD LGGTTFSVGL VSEDGKILKK VTRDTLVENG KEDVIRRIAE TILEVSDGEE
APYVGIGSPG SIDRENGIVR FSPNFPDWHN VPLTDELAKR TGKKVFLEND ANAFVLGEKW
FGAGRGHDHI VALTLGTGIG GGVVTHGYLL TGRDGIGAEL GHVVVEPNGP MCNCGTRGCL
EAVASATAIR RFLREGYKKY HSSLVYKLAG SPEKADAKHL FDAARQGDRF ALMIRDRVVD
ALARAVAGYI HIFNPEIVII GGGISRAGEI LFGPLREKVV DYIMPSFVGT YEVVASPLVE
DAGILGAASI IKERIGG
