ID   GLK_BURPS               Reviewed;         641 AA.
AC   Q63RQ7;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 109.
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=BPSL2614;
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA   Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA   Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA   Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA   Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA   Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA   Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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; BX571965; CAH36622.1; -; Genomic_DNA.
DR   RefSeq; WP_004541285.1; NZ_CP009538.1.
DR   RefSeq; YP_109210.1; NC_006350.1.
DR   AlphaFoldDB; Q63RQ7; -.
DR   SMR; Q63RQ7; -.
DR   STRING; 272560.BPSL2614; -.
DR   KEGG; bps:BPSL2614; -.
DR   PATRIC; fig|272560.51.peg.2740; -.
DR   eggNOG; COG0837; Bacteria.
DR   eggNOG; COG1737; Bacteria.
DR   Proteomes; UP000000605; 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; Reference proteome;
KW   Transcription; Transcription regulation; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..641
FT                   /note="Bifunctional protein glk"
FT                   /id="PRO_0000268799"
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..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;  68347 MW;  DF273867FE0AD163 CRC64;
     MSTGAQTKAA AASQHADGPR LLADVGGTNA RFALETGPGE ITQIRVYPGA EYPTLTDAIR
     KYLKDAKIGR VNHAAIAIAN PVDGDQVRMT NHNWSFSIEA TRRALGFDTL LVVNDFTALA
     MALPGLTDAQ RVQIGGGARR QNSVIGLMGP GTGLGVSGLI PADDRWIALG SEGGHATFAP
     MDEREDLVLQ YARRKYPHVS FERVCAGPGM EIIYRALAAR DKKRIAANVD TADIVERAHA
     GDALALEAVE CFCAILGTFA 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 AVGVAIRRAA
     PNAELAEAMA RAKARAGASA GDEAADVLDW LSHGAAPAAK D
//