GLK_BURL3
ID GLK_BURL3 Reviewed; 642 AA.
AC Q39IQ1;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Bifunctional protein glk;
DE Includes:
DE RecName: Full=Glucokinase;
DE EC=2.7.1.2;
DE AltName: Full=Glucose kinase;
DE Includes:
DE RecName: Full=Putative HTH-type transcriptional regulator;
GN Name=glk; OrderedLocusNames=Bcep18194_A4068;
OS Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS R18194 / 383).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=482957;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia sp. 383.";
RL Submitted (OCT-2005) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the bacterial
CC glucokinase family. {ECO:0000305}.
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DR EMBL; CP000151; ABB07665.1; -; Genomic_DNA.
DR RefSeq; WP_011351246.1; NZ_CABVQB010000008.1.
DR AlphaFoldDB; Q39IQ1; -.
DR SMR; Q39IQ1; -.
DR EnsemblBacteria; ABB07665; ABB07665; Bcep18194_A4068.
DR GeneID; 45093964; -.
DR KEGG; bur:Bcep18194_A4068; -.
DR PATRIC; fig|482957.22.peg.949; -.
DR HOGENOM; CLU_016801_0_0_4; -.
DR OMA; WSHVSFE; -.
DR OrthoDB; 992687at2; -.
DR Proteomes; UP000002705; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
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 CDD; cd05013; SIS_RpiR; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_00524; Glucokinase; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR003836; Glucokinase.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR000281; HTH_RpiR.
DR InterPro; IPR035472; RpiR-like_SIS.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF02685; Glucokinase; 1.
DR Pfam; PF01418; HTH_6; 1.
DR Pfam; PF01380; SIS; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
DR SUPFAM; SSF53697; SSF53697; 1.
DR TIGRFAMs; TIGR00749; glk; 1.
DR PROSITE; PS00356; HTH_LACI_1; 1.
DR PROSITE; PS51071; HTH_RPIR; 1.
DR PROSITE; PS51464; SIS; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA-binding; Glycolysis; Kinase; Membrane;
KW Multifunctional enzyme; Nucleotide-binding; Transcription;
KW Transcription regulation; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..642
FT /note="Bifunctional protein glk"
FT /id="PRO_0000268800"
FT TRANSMEM 576..596
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 341..417
FT /note="HTH rpiR-type"
FT DOMAIN 461..600
FT /note="SIS"
FT DNA_BIND 377..396
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 1..340
FT /note="Glucokinase"
FT REGION 341..642
FT /note="Putative HTH-type transcriptional regulator"
FT BINDING 23..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 642 AA; 68507 MW; 79F479F63D4FEF3E CRC64;
MSTGAQSKAA VAGQHADGPR LLADVGGTNA RFALETGPGD ITQIRVYPGA DYPTLTDAIR
KYLKDVKITR VNHAAIAIAN PVDGDQVTMT NHDWSFSIEA TRRALGFDTL LVVNDFTALA
MALPGLTDAQ RVQIGGGARR QNSVIGLLGP GTGLGVSGLI PADDRWIALG SEGGHASFAP
QDEREDLVLQ YARKKFPHVS FERVCAGPGM EIIYRALAAR DKKRVAATVD TVEIVERAHA
GDALALETVE CFCGILGAFA GSVALTLGAL GGVYIGGGVA LKLGELFTRS SFRARFEAKG
RFTHYLENIP TYLITAEYPA FLGVSAILAE QLSNRSGGAS SAVFERIRQM RDALTPAERR
VADLALNHPR SIINDPIVDI ARKADVSQPT VIRFCRSLGC QGLSDFKLKL ATGLTGTIPM
SHSQVHLGDT ATDFGAKVLD NTVSAILQLR EHLNFEHVEN AIEILNGARR IEFYGLGNSN
IVAQDAHYKF FRFGIPTIAY GDLYMQAASA ALLGKGDVIV AVSKSGRAPE LLRVLDVAMQ
AGAKVIAITS SNTPLAKRAT VALETDHIEM RESQLSMISR ILHLLMIDIL AVGVAIRRAS
TNGELPEAVA QAKARASDDE TADVLDWLSH GASPAAKDVA RD