GLK_PARXL
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 03-AUG-2022, entry version 96.
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; Proteobacteria; 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 EnsemblBacteria; ABE29531; ABE29531; Bxe_A3454.
DR KEGG; bxb:DR64_1155; -.
DR KEGG; bxe:Bxe_A3454; -.
DR eggNOG; COG0837; Bacteria.
DR eggNOG; COG1737; Bacteria.
DR OMA; WSHVSFE; -.
DR OrthoDB; 992687at2; -.
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; 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; Cytoplasm; DNA-binding; Glycolysis; Kinase;
KW Multifunctional enzyme; Nucleotide-binding; Reference proteome;
KW Transcription; 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