GLK_BACSU
ID GLK_BACSU Reviewed; 321 AA.
AC P54495;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Glucokinase;
DE EC=2.7.1.2 {ECO:0000269|PubMed:9620975};
DE AltName: Full=Glucose kinase {ECO:0000303|PubMed:8969508};
GN Name=glcK {ECO:0000303|PubMed:8969508}; Synonyms=yqgR;
GN OrderedLocusNames=BSU24850;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 152 AND 198.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PROBABLE
RP SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE, AND ATP-BINDING.
RC STRAIN=168;
RX PubMed=9620975; DOI=10.1128/jb.180.12.3222-3226.1998;
RA Skarlatos P., Dahl M.K.;
RT "The glucose kinase of Bacillus subtilis.";
RL J. Bacteriol. 180:3222-3226(1998).
CC -!- FUNCTION: An ATP-dependent kinase that phosphorylates glucose to make
CC glucose-6-phosphate, not active on fructose, galactose or mannose.
CC Restores glucose kinase activity in E.coli glk mutants.
CC {ECO:0000269|PubMed:9620975}.
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:9620975};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC Evidence={ECO:0000269|PubMed:9620975};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.77 mM for ATP {ECO:0000269|PubMed:9620975};
CC KM=0.24 mM for glucose {ECO:0000269|PubMed:9620975};
CC Vmax=93 umol/min/mg enzyme {ECO:0000269|PubMed:9620975};
CC Temperature dependence:
CC Optimum temperature is 32 degrees Celsius. Enzyme is stable up to 40
CC degrees Celsius. {ECO:0000269|PubMed:9620975};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:9620975}.
CC -!- INDUCTION: Constitutively expressed, activity is maximal at the end of
CC vegetative growth and declines during stationary phase when grown in
CC rich broth (LB) (at protein level). Expressed in a similar fashion in
CC minimal medium containing glucose, fructose, trehalose, maltose or
CC sucrose. {ECO:0000269|PubMed:9620975}.
CC -!- DISRUPTION PHENOTYPE: Loss of glucokinase activity, no growth phenotype
CC on glucose, fructose, maltose, sucrose or trehalose-containing minimal
CC media. {ECO:0000269|PubMed:9620975}.
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
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DR EMBL; D84432; BAA12521.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14416.2; -; Genomic_DNA.
DR PIR; B69632; B69632.
DR RefSeq; NP_390365.2; NC_000964.3.
DR RefSeq; WP_003230132.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P54495; -.
DR SMR; P54495; -.
DR STRING; 224308.BSU24850; -.
DR jPOST; P54495; -.
DR PaxDb; P54495; -.
DR PRIDE; P54495; -.
DR EnsemblBacteria; CAB14416; CAB14416; BSU_24850.
DR GeneID; 938206; -.
DR KEGG; bsu:BSU24850; -.
DR PATRIC; fig|224308.179.peg.2704; -.
DR eggNOG; COG1940; Bacteria.
DR InParanoid; P54495; -.
DR OMA; DHLVMIT; -.
DR PhylomeDB; P54495; -.
DR BioCyc; BSUB:BSU24850-MON; -.
DR BioCyc; MetaCyc:MON-5981; -.
DR BRENDA; 2.7.1.2; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004340; F:glucokinase activity; IMP:CACAO.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..321
FT /note="Glucokinase"
FT /id="PRO_0000095676"
FT BINDING 8..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:9620975"
FT CONFLICT 152
FT /note="V -> L (in Ref. 1; BAA12521)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="E -> G (in Ref. 1; BAA12521)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 33604 MW; F8162AE8BB49D3CD CRC64;
MDEIWFAGID LGGTTIKLAF INQYGEIQHK WEVPTDKTGD TITVTIAKTI DSKLDELQKP
KHIIKYIGMG APGPVDMAAG VVYETVNLGW KNYALKNHLE TETGIPAVIE NDANIAALGE
MWKGAGDGAK DVILVTLGTG VGGGIIANGE IVHGINGAGG EIGHICSIPE GGAPCNCGKT
GCIETIASAT GIVRIAKEKI ANAKKTTRLK ATEQLSARDV FEAAGENDEI ALEVVDYVAK
HLGLVLGNLA SSLNPSKIVL GGGVSRAGEL LRSKVEKTFR KCAFPRAAQA ADISIAALGN
DAGVIGGAWI AKNEWLKHQN C
