GLK_BURP1
ID GLK_BURP1 Reviewed; 641 AA.
AC Q3JPP0;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=BURPS1710b_3090;
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
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; CP000124; ABA49272.1; -; Genomic_DNA.
DR RefSeq; WP_004266877.1; NC_007434.1.
DR AlphaFoldDB; Q3JPP0; -.
DR SMR; Q3JPP0; -.
DR EnsemblBacteria; ABA49272; ABA49272; BURPS1710b_3090.
DR GeneID; 56528585; -.
DR KEGG; bpm:BURPS1710b_3090; -.
DR HOGENOM; CLU_016801_0_0_4; -.
DR OMA; WSHVSFE; -.
DR OrthoDB; 992687at2; -.
DR Proteomes; UP000002700; 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_0000268798"
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; 68377 MW; 3FD23867FE0AD167 CRC64;
MSTGAQTKAA AASQHADGPR LLADVGGTNA RFALETGPGE ITQIRVYPGA EYPTLTDAIR
KYLKDAKIGR VNHAAIAIAN PVDGDQVRMT NHNWSFSIEA TRRALGFDTL LVVNDFTALA
MALPGLTDAQ RVQIGGGTRR 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