ID   GLK_BURTA               Reviewed;         641 AA.
AC   Q2SYA5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=BTH_I1550;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(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   -!- 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; CP000086; ABC37839.1; -; Genomic_DNA.
DR   RefSeq; WP_011402098.1; NZ_CP008785.1.
DR   AlphaFoldDB; Q2SYA5; -.
DR   SMR; Q2SYA5; -.
DR   PRIDE; Q2SYA5; -.
DR   EnsemblBacteria; ABC37839; ABC37839; BTH_I1550.
DR   KEGG; bte:BTH_I1550; -.
DR   HOGENOM; CLU_016801_0_0_4; -.
DR   OMA; WSHVSFE; -.
DR   OrthoDB; 992687at2; -.
DR   Proteomes; UP000001930; Chromosome I.
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..641
FT                   /note="Bifunctional protein glk"
FT                   /id="PRO_0000268801"
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          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          341..641
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   641 AA;  68475 MW;  06726A47707F8B7F CRC64;
     MSTGAQTKAA EASQHADGPR LLADVGGTNA RFALETGPGE ITQIRVYPGA EYPTLTDAIR
     RYLKDVKIGR VNHAAIAIAN PVDGDQVRMT NHNWSFSIEA TRRALGFDTL LVVNDFTALA
     MALPGLTDAQ RVQIGAGARR QNSVIGLMGP GTGLGVSGLI PADDRWIALG SEGGHATFAP
     MDEREDLVLQ YARRKYPHVS FERVCAGPGM EIIYRALAAR DKKRIAANVV TADIVERAHA
     GDALALEAVE CFCGILGTFA GNLAVTLGAL GGIYIGGGVV PKLGELFMRS PFRARFEAKG
     RFEAYLANIP TYLITAEYPA FLGVSAILAE QLSNRTGGAS SAVFERIRQM RDALTPAERR
     VADLALNHPR SIINDPIVDI ARKADVSQPT VIRFCRSLGC QGLSDFKLKL ATGLTGTIPM
     SHSQVHLGDT ATDFGAKVLD NTVSAILQLR EHLNFEHVEQ AIDILNNARR IEFYGLGNSN
     IVAQDAHYKF FRFGIPTIAY GDLYMQAASA ALLGKGDVIV AVSKSGRAPE LLRVLDVAMQ
     AGAKVIAITS SNTPLAKRAT VALETDHIEM RESQLSMISR ILHLVMIDIL AVGVAIRRAS
     PNAELAEAMA RAKARAGASA GDEAADVLDW LSHGAAPAAK E