ID   GLK_PYRCJ               Reviewed;         296 AA.
AC   A3MUZ0;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Glucokinase {ECO:0000303|PubMed:29275440};
DE            EC=2.7.1.2 {ECO:0000269|PubMed:29275440};
DE   AltName: Full=ATP-dependent glucokinase {ECO:0000303|PubMed:29275440};
DE            Short=ATP-GLK {ECO:0000305};
DE   AltName: Full=Glucose kinase {ECO:0000305};
GN   OrderedLocusNames=Pcal_1032 {ECO:0000312|EMBL:ABO08457.1};
OS   Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=410359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21063 / JCM 11548 / VA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBUNIT.
RX   PubMed=29275440; DOI=10.1007/s00792-017-0993-4;
RA   Bibi T., Ali M., Rashid N., Muhammad M.A., Akhtar M.;
RT   "Enhancement of gene expression in Escherichia coli and characterization of
RT   highly stable ATP-dependent glucokinase from Pyrobaculum calidifontis.";
RL   Extremophiles 22:247-257(2018).
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-glucose to D-glucose 6-
CC       phosphate using ATP as the phosphate donor. Has a broad hexose
CC       specificity, and in addition to glucose, which shows the highest
CC       catalytic efficiency, it can also phosphorylate fructose, mannose,
CC       galactose and sorbitol. Can also use CTP, GTP or UTP as phosphoryl
CC       donor. {ECO:0000269|PubMed:29275440}.
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:29275440};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000269|PubMed:29275440};
CC       Note=Mg(2+) is the most effective ion. {ECO:0000269|PubMed:29275440};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=660 uM for glucose {ECO:0000269|PubMed:29275440};
CC         KM=900 uM for ATP {ECO:0000269|PubMed:29275440};
CC         Vmax=550 umol/min/mg enzyme {ECO:0000269|PubMed:29275440};
CC         Note=kcat is 289 sec(-1) with glucose as substrate.
CC         {ECO:0000269|PubMed:29275440};
CC       pH dependence:
CC         Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:29275440};
CC       Temperature dependence:
CC         Optimum temperature is 95 degrees Celsius. Highly thermostable.
CC         {ECO:0000269|PubMed:29275440};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:29275440}.
CC   -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
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DR   EMBL; CP000561; ABO08457.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3MUZ0; -.
DR   SMR; A3MUZ0; -.
DR   STRING; 410359.Pcal_1032; -.
DR   EnsemblBacteria; ABO08457; ABO08457; Pcal_1032.
DR   KEGG; pcl:Pcal_1032; -.
DR   eggNOG; arCOG04280; Archaea.
DR   HOGENOM; CLU_036604_0_1_2; -.
DR   OMA; DHLVMIT; -.
DR   BRENDA; 2.7.1.2; 7282.
DR   Proteomes; UP000001431; Chromosome.
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   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000600; ROK.
DR   PANTHER; PTHR18964; PTHR18964; 1.
DR   Pfam; PF00480; ROK; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Carbohydrate metabolism; Glucose metabolism; Kinase;
KW   Magnesium; Nucleotide-binding; Transferase.
FT   CHAIN           1..296
FT                   /note="Glucokinase"
FT                   /id="PRO_0000448974"
SQ   SEQUENCE   296 AA;  31573 MW;  D1CA455C89A2D7CE CRC64;
     MAKYLGIDVG ATWTRAILVD EGGSVLSRAK IRTGVSPVAE IAEVVAGWDF DAVGVGSIGP
     MDLKTGVVVN SPNSPSRRFP LVEPLKKFKR PVVVANDCVA AVWGEYVFKY HVDNMAYLTL
     STGVGVGAIV NGVLLLGKDG NAHELGHAVI DFKSPRRCGC GGLGHFEAFV GGANMPSFYQ
     EVAGEGPLLP EEIFKRAREG YRKAVEFLDV WLDALAAGVA TILAAYDPEL LIVGGSIALN
     NWDIVGRELP KRLVKYLGVR GAEIRPASFG DDEVAIGAAA LAYKTPETLK KFGYPR