ID G7Z2G5_AZOL4 Unreviewed; 323 AA.
AC G7Z2G5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
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 ECO:0000313|EMBL:CBS85580.1};
GN OrderedLocusNames=AZOLI_0164 {ECO:0000313|EMBL:CBS85580.1};
OS Azospirillum lipoferum (strain 4B).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS85580.1, ECO:0000313|Proteomes:UP000005667};
RN [1] {ECO:0000313|Proteomes:UP000005667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RX PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA Zhulin I.B.;
RT "Azospirillum genomes reveal transition of bacteria from aquatic to
RT terrestrial environments.";
RL PLoS Genet. 7:E1002430-E1002430(2011).
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; FQ311868; CBS85580.1; -; Genomic_DNA.
DR RefSeq; WP_014246647.1; NC_016622.1.
DR AlphaFoldDB; G7Z2G5; -.
DR STRING; 862719.AZOLI_0164; -.
DR KEGG; ali:AZOLI_0164; -.
DR HOGENOM; CLU_042582_1_0_5; -.
DR OrthoDB; 9800595at2; -.
DR Proteomes; UP000005667; 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 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:CBS85580.1};
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; 33388 MW; 9EE841F8000E0DB1 CRC64;
MAVSPILVAD IGGTNARFGL IDGRTVRDTR VLRCADYASI EDAATAYLSA IGLAAPGTPG
RPRRGAFAVA GPVTGDRIAM TNLVWQFSVG RVRDALGLEG LAVINDFTAV ALSVPRLAEE
DRRQVGEGSP QPGAVVAVLG PGSGLGVSGL VPGANGRWTA LSGEGGHVTM APMSDRESAV
LGQLRKGFDH VSAERVLSGP GLVNLYTALS ILDGREPAAL TPAQITDNAL AGTEPHCVEA
VEMFCAMLGT VAGNLALTLG ARGGVYIAGG IVPRLGTLFA HSRFRKRFAE KGRMRDFLAP
IPTYVVIHEL PAFLGLAEAA GTE
//