GLK_XANOM
ID GLK_XANOM Reviewed; 335 AA.
AC Q2P3D0;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=XOO2192;
OS Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=342109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 311018;
RA Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT large numbers of effector genes and insertion sequences to its race
RT diversity.";
RL Jpn. Agric. Res. Q. 39:275-287(2005).
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: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; AP008229; BAE68947.1; -; Genomic_DNA.
DR RefSeq; WP_011258988.1; NC_007705.1.
DR AlphaFoldDB; Q2P3D0; -.
DR SMR; Q2P3D0; -.
DR KEGG; xom:XOO2192; -.
DR HOGENOM; CLU_042582_1_0_6; -.
DR OMA; NNHWRLS; -.
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 HAMAP; MF_00524; Glucokinase; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR003836; Glucokinase.
DR Pfam; PF02685; Glucokinase; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
DR TIGRFAMs; TIGR00749; glk; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..335
FT /note="Glucokinase"
FT /id="PRO_0000268793"
FT BINDING 11..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00524"
SQ SEQUENCE 335 AA; 35585 MW; 545F3029CB235DB5 CRC64;
MTAPSKPVLV ADIGGTNARF ALADVDASVP LLDDTSREFA VVDFTSLGEA ARYYLDQIGV
QATQGVFAVA GRVDGDEARI TNHPWVISRS RTASMLGFST LHLINDFAAQ AMAISLLRPQ
DVVQVGGASW RPAPIDQPRN YGVIGPGTGL GVGGLIIRHG RCFPLETEGG HVSFPPGTPE
EIRILEILSE QFGRVSNERL ICGPGLVNIH RALSEIAGVD PGPLQPKDIT ARAAAGDPRS
SRTIDLFCAI FGAIAGDMVL MQGAWDGVFL TGGLVPKVLD SLQHSGFRQR FEHKGRFSAI
MSRVPSLAVM HPHAGLLGAA AYAVDAQRQP PGEQR