ID   GLK_PARXL               Reviewed;         638 AA.
AC   Q143F8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 103.
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=Bxeno_A0993; ORFNames=Bxe_A3454;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the bacterial
CC       glucokinase family. {ECO:0000305}.
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DR   EMBL; CP000270; ABE29531.1; -; Genomic_DNA.
DR   RefSeq; WP_007175889.1; NZ_CP008760.1.
DR   AlphaFoldDB; Q143F8; -.
DR   SMR; Q143F8; -.
DR   STRING; 266265.Bxe_A3454; -.
DR   KEGG; bxb:DR64_1155; -.
DR   KEGG; bxe:Bxe_A3454; -.
DR   eggNOG; COG0837; Bacteria.
DR   eggNOG; COG1737; Bacteria.
DR   OrthoDB; 257751at2; -.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; 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; Cytoplasm; DNA-binding; Glycolysis; Kinase;
KW   Multifunctional enzyme; Nucleotide-binding; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..638
FT                   /note="Bifunctional protein glk"
FT                   /id="PRO_0000268802"
FT   DOMAIN          342..418
FT                   /note="HTH rpiR-type"
FT   DOMAIN          462..601
FT                   /note="SIS"
FT   DNA_BIND        378..397
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   REGION          1..341
FT                   /note="Glucokinase"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..638
FT                   /note="Putative HTH-type transcriptional regulator"
FT   BINDING         24..29
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   638 AA;  67858 MW;  6C68510E194AA57F CRC64;
     MSTGVQTKAA PGAGQHADGP RLLADIGGTN ARFALETSPG EIGSVKVYPC ADYPGVAEVI
     KRYLKDTKIG RVNHAAIAIA NPVDGDQVSM TNHDWSFSIE ATRRALGFDT LLVVNDFTAL
     AMALPGLTDA QRVQVGGGTR RPNSVIGLLG PGTGMGVSGL IPADDRWIAL GSEGGHATFA
     PADEREDIVL QYARKKWSHV SFERVAAGPG IEVIYRALAG RDKKRVAANV DTIEIVKRAM
     EGEPLAAESV DVFCGILGTF AGNIAVTLGA LGGIYIGGGV VPRLGELFAR SSFRKRFEAK
     GRFEAYLQNV PTYVITAEYP AFLGVSAILA EQLSNRAGGS SSAVFERIRQ MRDALTPAER
     RVADLALNHP RSIINDPIVD IARKADVSQP TVIRFCRSLG CQGLSDFKLK LATGLTGTIP
     VSHSQVHLGD TATDFGAKVL DNTVSAILQL REHLNFEHVE RAIDLLNGAR RIEFYGLGNS
     NIVAQDAHYK FFRFGIPTIA YGDLYMQAAS AALLGKGDVI VAVSKSGRAP ELLRVLDVAM
     QAGAKVIAIT SSNTPLAKRA TVALETDHIE IRESQLSMIS RILHLVMIDI LAVGVAIRRA
     VPSADVAETV AKARQGADDD ATAVLDWLSH GAASSARD
//