ID A0A0N1BLI6_9PROT Unreviewed; 322 AA.
AC A0A0N1BLI6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=IP88_03065 {ECO:0000313|EMBL:KPF78851.1};
OS alpha proteobacterium AAP81b.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1523432 {ECO:0000313|EMBL:KPF78851.1, ECO:0000313|Proteomes:UP000037971};
RN [1] {ECO:0000313|EMBL:KPF78851.1, ECO:0000313|Proteomes:UP000037971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP81b {ECO:0000313|EMBL:KPF78851.1,
RC ECO:0000313|Proteomes:UP000037971};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPF78851.1}.
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DR EMBL; LJHX01000026; KPF78851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1BLI6; -.
DR STRING; 1523432.IP88_03065; -.
DR PATRIC; fig|1523432.3.peg.1741; -.
DR OrthoDB; 9800595at2; -.
DR Proteomes; UP000037971; 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 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:KPF78851.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00524};
KW Reference proteome {ECO:0000313|Proteomes:UP000037971};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00524}.
FT BINDING 7..12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00524"
SQ SEQUENCE 322 AA; 33041 MW; 8E0E149425A7E37D CRC64;
MTNIVAMDIG GTNARFALAT VAPGAAPVLS EPVKLRAADY PTLAAAWAEF AARCPEPLPR
AAALAVACPV DGDILKLTNS PWVLRKSTLK AQLGLDDLVI VNDFGAVTRA VPHLAAANLV
HLCGPDTGLP AAGAISVIGP GTGLGVGLLL RDEAGDRVVE TEGGHMDFAP CDAIEDMLLQ
RLRARYGRVS VERVCAGPGL VDIYETLAHA EGAAVTILDD KELWPVAIDG SNPLAAAALL
RFCAALGCAT GNLALAHLAK AVVLAGGIPP RILPILKDSG FGARFRAKGR FEGLMAAIPV
YACVHPDPGL MGAAAACSAR FA
//
