GLK_STRM5
ID GLK_STRM5 Reviewed; 335 AA.
AC B4SRZ6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=Smal_1530;
OS Stenotrophomonas maltophilia (strain R551-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=391008;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R551-3;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL Submitted (JUN-2008) 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: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; CP001111; ACF51235.1; -; Genomic_DNA.
DR RefSeq; WP_012510708.1; NC_011071.1.
DR AlphaFoldDB; B4SRZ6; -.
DR SMR; B4SRZ6; -.
DR STRING; 391008.Smal_1530; -.
DR EnsemblBacteria; ACF51235; ACF51235; Smal_1530.
DR KEGG; smt:Smal_1530; -.
DR eggNOG; COG0837; Bacteria.
DR HOGENOM; CLU_042582_1_0_6; -.
DR OMA; NNHWRLS; -.
DR OrthoDB; 992687at2; -.
DR BioCyc; SMAL391008:SMAL_RS07895-MON; -.
DR Proteomes; UP000001867; 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 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_1000127726"
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; 35246 MW; EB81A67BEDCB1DF6 CRC64;
MSASSQPVLV ADIGGTNARF ALADTSLDAP LQQDSIREYA VAEFPSLGDA ARHHLEQIGA
TASRGVFAVA GRVDGDEARI TNHPWVISRS RTAAMLGFDE LHLINDFAAQ AMAISLLQSD
DVVQVGGAAW VPGKPGQPRN YAVIGPGTGL GVGGLILRHG RCYPLETEGG HVSFPPGTPE
EIRILEILSE QFGRVSNERL ICGPGLVNIH RAVCEMAGID PGQLQPVDVT ARALHGDPQA
MRTVDVFCAV FGAIAGDLVL TQGAWDGVFL TGGLTPKMLD SLQHSGFRQR FEHKGRFSSI
MARVPSLAVM HPHAGLLGAA AYAADAERDA PGVAA