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   27-MAR-2024, entry version 106.
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; Pseudomonadota; 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_WNDV01000014.1.
DR   AlphaFoldDB; Q39IQ1; -.
DR   SMR; Q39IQ1; -.
DR   GeneID; 45093964; -.
DR   KEGG; bur:Bcep18194_A4068; -.
DR   PATRIC; fig|482957.22.peg.949; -.
DR   HOGENOM; CLU_016801_0_0_4; -.
DR   Proteomes; UP000002705; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 3.30.420.40; -; 1.
DR   Gene3D; 3.40.367.20; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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   NCBIfam; TIGR00749; glk; 1.
DR   PANTHER; PTHR47690; GLUCOKINASE; 1.
DR   PANTHER; PTHR47690:SF1; GLUCOKINASE; 1.
DR   Pfam; PF02685; Glucokinase; 1.
DR   Pfam; PF01418; HTH_6; 1.
DR   Pfam; PF01380; SIS; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF53697; SIS domain; 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
//