BGLK_KLEPN
ID BGLK_KLEPN Reviewed; 297 AA.
AC Q93LQ8;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Beta-glucoside kinase;
DE EC=2.7.1.85;
GN Name=bglK;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-28, CATALYTIC
RP ACTIVITY, FUNCTION, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION, SUBUNIT,
RP INDUCTION, AND MUTAGENESIS OF ASP-7; GLY-9; ASP-103; GLY-131 AND GLY-133.
RC STRAIN=ATCC 23357 / A-11;
RX PubMed=12110692; DOI=10.1074/jbc.m206397200;
RA Thompson J., Lichtenthaler F.W., Peters S., Pikis A.;
RT "Beta-glucoside kinase (BglK) from Klebsiella pneumoniae. Purification,
RT properties, and preparative synthesis of 6-phospho-beta-D-glucosides.";
RL J. Biol. Chem. 277:34310-34321(2002).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of a wide variety
CC of beta-D-glucosides, to produce 6-phospho-beta-D-glucosides including
CC cellobiose-6'-P, gentiobiose-6'-P, cellobiitol-6-P, salicin-6-P, and
CC arbutin-6-P. Is not able to phosphorylate alpha-D-glucosides. May have
CC a dual role of kinase and transcriptional regulator of the cellobiose-
CC PTS operon. {ECO:0000269|PubMed:12110692}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-cellobiose = 6-phospho-beta-D-glucosyl-(1->4)-D-
CC glucose + ADP + H(+); Xref=Rhea:RHEA:21944, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17057, ChEBI:CHEBI:30616, ChEBI:CHEBI:58312,
CC ChEBI:CHEBI:456216; EC=2.7.1.85;
CC Evidence={ECO:0000269|PubMed:12110692};
CC -!- ACTIVITY REGULATION: Is inhibited by N-ethylmaleimide in vitro, but ATP
CC affords considerable protection against the inhibitor.
CC {ECO:0000269|PubMed:12110692}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.11 mM for n-octyl-beta-D-glucopyranoside;
CC KM=0.18 mM for salicin;
CC KM=0.21 mM for arbutin;
CC KM=0.47 mM for cellobiose;
CC KM=0.47 mM for amygdalin;
CC KM=0.56 mM for gentiobiose;
CC KM=0.63 mM for laminaribiose;
CC KM=0.65 mM for phenyl-beta-D-glucopyranoside;
CC KM=1.56 mM for cellobiitol;
CC KM=2.03 mM for isopropyl-beta-D-thioglucopyranoside;
CC KM=2.23 mM for methyl-beta-D-glucopyranoside;
CC KM=3.15 mM for sophorose;
CC KM=10.54 mM for thiocellobiose;
CC KM=40.29 mM for glucose;
CC KM=0.24 mM for ATP;
CC Vmax=106.81 umol/min/mg enzyme with n-octyl-beta-D-glucopyranoside as
CC substrate;
CC Vmax=102.42 umol/min/mg enzyme with salicin as substrate;
CC Vmax=131.23 umol/min/mg enzyme with arbutin as substrate;
CC Vmax=86.82 umol/min/mg enzyme with cellobiose as substrate;
CC Vmax=94.21 umol/min/mg enzyme with amygdalin as substrate;
CC Vmax=74.59 umol/min/mg enzyme with gentiobiose as substrate;
CC Vmax=121.23 umol/min/mg enzyme with laminaribiose as substrate;
CC Vmax=150.00 umol/min/mg enzyme with phenyl-beta-D-glucopyranoside as
CC substrate;
CC Vmax=85.72 umol/min/mg enzyme with cellobiitol as substrate;
CC Vmax=107.30 umol/min/mg enzyme with isopropyl-beta-D-
CC thioglucopyranoside as substrate;
CC Vmax=132.12 umol/min/mg enzyme with methyl-beta-D-glucopyranoside as
CC substrate;
CC Vmax=105.46 umol/min/mg enzyme with sophorose as substrate;
CC Vmax=49.27 umol/min/mg enzyme with thiocellobiose as substrate;
CC Vmax=86.29 umol/min/mg enzyme with glucose as substrate;
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12110692}.
CC -!- INDUCTION: Highly induced by cellobiose. To a lesser extent, is also
CC induced by gentiobiose, cellobiitol, and methyl-beta-glucoside, but not
CC by arbutin, salicin, esculin or phenyl-beta-glucoside.
CC {ECO:0000269|PubMed:12110692}.
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
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DR EMBL; AY035305; AAK58463.1; -; Genomic_DNA.
DR RefSeq; WP_002913833.1; NZ_WYAM01000007.1.
DR AlphaFoldDB; Q93LQ8; -.
DR SMR; Q93LQ8; -.
DR OrthoDB; 1130699at2; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047700; F:beta-glucoside kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000600; ROK.
DR PANTHER; PTHR18964; PTHR18964; 1.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..297
FT /note="Beta-glucoside kinase"
FT /id="PRO_0000390475"
FT BINDING 5..11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 7
FT /note="D->G: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:12110692"
FT MUTAGEN 9
FT /note="G->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:12110692"
FT MUTAGEN 103
FT /note="D->G: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:12110692"
FT MUTAGEN 131
FT /note="G->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:12110692"
FT MUTAGEN 133
FT /note="G->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:12110692"
SQ SEQUENCE 297 AA; 32697 MW; D1C8F19FCE6ECB79 CRC64;
MKIAAFDIGG TALKMGVMAR DGRLLETARQ SINDSDGDRI LQAMLSWLAA HPSCEGIAIS
APGYIDPHSG LITMGGAIRR FDNFAMKSWL ETRTGLPVSV ENDANCVLLA ERWQGKAAEM
ANFLVLTIGT GIGGAIFCQH QLINGARFRA GEFGYMLTDR PGGRDPRRYS MNENCTLRVL
RHRYAQHIGA PLDSVTGELI FDRYDAGDPV CQRLVAEFFN GLGHGLYNLV HIFDPQTIFI
GGGVVERPGF LTLLRQHLAW FGIADYLDTV SHGNDAGLIG AVYHFNQLYR SPDDDRH
