ID Q6SFD6_9BACT Unreviewed; 328 AA.
AC Q6SFD6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 52.
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:AAR38284.1};
GN ORFNames=MBMO_EBAC000-69B03.33 {ECO:0000313|EMBL:AAR38284.1};
OS uncultured marine bacterium 581.
OC Bacteria; environmental samples.
OX NCBI_TaxID=257401 {ECO:0000313|EMBL:AAR38284.1};
RN [1] {ECO:0000313|EMBL:AAR38284.1}
RP NUCLEOTIDE SEQUENCE.
RA Heidelberg J.F., Eisen J.A., Nelson W.C., DeLong E.F.;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAR38284.1}
RP NUCLEOTIDE SEQUENCE.
RA DeLong E.F.;
RT "Monterey Bay Coastal Ocean Microbial Observatory environmental clone
RT sequencing.";
RL Submitted (DEC-2003) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY458648; AAR38284.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6SFD6; -.
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:AAR38284.1};
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 328 AA; 34482 MW; 8B6C4338AC1DD569 CRC64;
METKWHLLGD IGGTNARFGI CDDQKAPYQL IGSYEVAAFP TFSNVLEQLQ SDLIKAGLSM
ADAGESCLAV AGPPDVQPVS FTNSAWRFDR ELVMSTLGLQ SVSIINDFAA AARALPLLSE
NHLEKVGGGR AEPGSPCVAL GPGTGLGVAT LATTHSGEPL VISGEGGHVD FAPVTNVEAA
VLDFLRARYG RVSIERLCCG EGINNIYQAL ADYRNLKIKY SSAAEIGAAA LSADDALSKE
TMAMFFAVLG AAAGNFALTL GAKGGIYIAG GIVPRYLDLL RRSDFRARFL AKGRFADYLS
DIPTFVVTHS QLGLLGASAS LNDPHIRG
//
