ID GLK_ZYMMO Reviewed; 324 AA.
AC P21908; Q5NQL1;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 27-NOV-2024, entry version 120.
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=ZMO0369;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=2254282; DOI=10.1128/jb.172.12.7227-7240.1990;
RA Barnell W.O., Yi K.C., Conway T.;
RT "Sequence and genetic organization of a Zymomonas mobilis gene cluster that
RT encodes several enzymes of glucose metabolism.";
RL J. Bacteriol. 172:7227-7240(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Ahn J.Y., Kang H.S.;
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose + ATP = D-glucose 6-phosphate + ADP + 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; M60615; AAA27694.1; -; Genomic_DNA.
DR EMBL; AF313764; AAG29867.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV88993.1; -; Genomic_DNA.
DR PIR; D37855; D37855.
DR AlphaFoldDB; P21908; -.
DR SMR; P21908; -.
DR STRING; 264203.ZMO0369; -.
DR KEGG; zmo:ZMO0369; -.
DR eggNOG; COG0837; Bacteria.
DR HOGENOM; CLU_042582_1_0_5; -.
DR Proteomes; UP000001173; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005536; F:D-glucose binding; IEA:InterPro.
DR GO; GO:0004340; F:glucokinase activity; IEA:UniProtKB-UniRule.
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; IPR050201; Bacterial_glucokinase.
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; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..324
FT /note="Glucokinase"
FT /id="PRO_0000215147"
FT BINDING 6..11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00524"
FT CONFLICT 258
FT /note="A -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 313..324
FT /note="AAAYANKYSEVE -> QLPMPTNILKLNNIF (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 34897 MW; BAAC13AAB6DB8716 CRC64;
MEIVAIDIGG THARFSIAEV SNGRVLSLGE ETTFKTAEHA SLQLAWERFG EKLGRPLPRA
AAIAWAGPVH GEVLKLTNNP WVLRPATLNE KLDIDTHVLI NDFGAVAHAV AHMDSSYLDH
ICGPDEALPS DGVITILGPG TGLGVAHLLR TEGRYFVIET EGGHIDFAPL DRLEDKILAR
LRERFRRVSI ERIISGPGLG NIYEALAAIE GVPFSLLDDI KLWQMALEGK DNLAEAALDR
FCLSLGAIAG DLALAQGATS VVIGGGVGLR IASHLPESGF RQRFVSKGRF ERVMSKIPVK
LITYPQPGLL GAAAAYANKY SEVE
//
