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Database: UniProt
Entry: B4W8G0_9CAUL
LinkDB: B4W8G0_9CAUL
Original site: B4W8G0_9CAUL 
ID   B4W8G0_9CAUL            Unreviewed;       323 AA.
AC   B4W8G0;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Glucokinase {ECO:0000256|HAMAP-Rule:MF_00524};
DE            EC=2.7.1.2 {ECO:0000256|HAMAP-Rule:MF_00524};
DE   AltName: Full=Glucose kinase {ECO:0000256|HAMAP-Rule:MF_00524};
GN   Name=glk {ECO:0000256|HAMAP-Rule:MF_00524};
GN   ORFNames=BBAL3_208 {ECO:0000313|EMBL:EDX79051.1};
OS   Brevundimonas sp. BAL3.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=391600 {ECO:0000313|EMBL:EDX79051.1, ECO:0000313|Proteomes:UP000003957};
RN   [1] {ECO:0000313|EMBL:EDX79051.1, ECO:0000313|Proteomes:UP000003957}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAL3 {ECO:0000313|EMBL:EDX79051.1,
RC   ECO:0000313|Proteomes:UP000003957};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00524};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00524}.
CC   -!- SIMILARITY: Belongs to the bacterial glucokinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00524, ECO:0000256|RuleBase:RU004046}.
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DR   EMBL; DS989898; EDX79051.1; -; Genomic_DNA.
DR   RefSeq; WP_008258989.1; NZ_DS989898.1.
DR   AlphaFoldDB; B4W8G0; -.
DR   STRING; 391600.BBAL3_208; -.
DR   eggNOG; COG0837; Bacteria.
DR   HOGENOM; CLU_042582_1_0_5; -.
DR   OrthoDB; 9800595at2; -.
DR   Proteomes; UP000003957; Unassembled WGS sequence.
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   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.40.367.20; -; 1.
DR   HAMAP; MF_00524; Glucokinase; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR003836; Glucokinase.
DR   NCBIfam; TIGR00749; glk; 1.
DR   PANTHER; PTHR47690; GLUCOKINASE; 1.
DR   PANTHER; PTHR47690:SF1; GLUCOKINASE; 1.
DR   Pfam; PF02685; Glucokinase; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00524};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00524};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_00524};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00524, ECO:0000313|EMBL:EDX79051.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00524};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00524}.
FT   BINDING         9..14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00524"
SQ   SEQUENCE   323 AA;  34316 MW;  2D438422F0343E60 CRC64;
     MNDKTLLVGD VGGTNARFAL ARMVDGKPVL DHHESFPAER YPTFLKGVAA FIDGCEIKPT
     GGVIAVAGPV TDGAIDLTNS PWQVSESELQ TLGLKPVKLI NDFEALAWGA PVVPEDQLES
     LGGPVDGDPH CTVAVLGPGT GFGVSALVRD AHGKEMAMPS EGGHACFPPG DPVEDEILRI
     LRRRYDRVSI ERLICGPGLL NMHRALAEID GRETHIEDPA QITETAMKDP NSPCGATLAR
     FCAILGAVAG DIALTTGARG GVYIAGGIVP RILPFIKASP FRQRFERKGR FKDYMAEIPT
     KVIMHKHAAL LGAARVAFAE AEG
//
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