ID   GLK_CAUVN               Reviewed;         331 AA.
AC   B8GXA8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Glucokinase {ECO:0000255|HAMAP-Rule:MF_00524};
DE            EC=2.7.1.2 {ECO:0000255|HAMAP-Rule:MF_00524};
DE   AltName: Full=Glucose kinase {ECO:0000255|HAMAP-Rule:MF_00524};
GN   Name=glk {ECO:0000255|HAMAP-Rule:MF_00524}; OrderedLocusNames=CCNA_02133;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
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:0000255|HAMAP-Rule:MF_00524};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00524}.
CC   -!- SIMILARITY: Belongs to the bacterial glucokinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00524}.
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DR   EMBL; CP001340; ACL95598.1; -; Genomic_DNA.
DR   RefSeq; WP_010919917.1; NC_011916.1.
DR   RefSeq; YP_002517506.1; NC_011916.1.
DR   AlphaFoldDB; B8GXA8; -.
DR   SMR; B8GXA8; -.
DR   PRIDE; B8GXA8; -.
DR   EnsemblBacteria; ACL95598; ACL95598; CCNA_02133.
DR   GeneID; 7330439; -.
DR   KEGG; ccs:CCNA_02133; -.
DR   PATRIC; fig|565050.3.peg.2091; -.
DR   HOGENOM; CLU_042582_1_0_5; -.
DR   OMA; GIANRFP; -.
DR   OrthoDB; 992687at2; -.
DR   PhylomeDB; B8GXA8; -.
DR   Proteomes; UP000001364; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004340; F:glucokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00524; Glucokinase; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR003836; Glucokinase.
DR   Pfam; PF02685; Glucokinase; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
DR   TIGRFAMs; TIGR00749; glk; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..331
FT                   /note="Glucokinase"
FT                   /id="PRO_1000146249"
FT   BINDING         13..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00524"
SQ   SEQUENCE   331 AA;  34714 MW;  BCDBDD25EE9549AC CRC64;
     MDGNHSGGLG LVGDIGGTNA RFALVEFDGQ DPRLIEPTAY RGEDYGTAED AIEEYLRKVG
     VKHPDQAVVA VAGPIDHGQV HMTNLDWRIS EDGLRRAGGF RNAKLINDFT AQALAAPRVG
     PKDLRQIGEL PTSGEGDLAI LGPGTGFGVA GLVRRHGQEI PLATEGGHVA FAPVDDVEIE
     VLRALTRRLD GGRVSVERIL SGPGMEDLHV DLAAAEGRGV EALTAKQITE RAVEGCADSL
     ATVNRFCAIL GSTAGDIALT LGARGGVFIA GGIAPRIIDI LEKSPFRERF DSKGRLSGFT
     RSIPTHVILH PHTALIGAAV ALTPEGRAAV S