CHBF_ECOLI
ID CHBF_ECOLI Reviewed; 450 AA.
AC P17411; P37795; P78290;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=6-phospho-beta-glucosidase;
DE EC=3.2.1.86 {ECO:0000269|PubMed:10572139};
DE AltName: Full=Cellobiose-6-phosphate hydrolase;
DE AltName: Full=Phospho-chitobiase;
GN Name=chbF; Synonyms=celF, ydjD; OrderedLocusNames=b1734, JW1723;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2179047; DOI=10.1093/genetics/124.3.455;
RA Parker L.L., Hall B.G.;
RT "Characterization and nucleotide sequence of the cryptic cel operon of
RT Escherichia coli K12.";
RL Genetics 124:455-471(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 362-450.
RC STRAIN=K12;
RX PubMed=8121401; DOI=10.1007/bf00281796;
RA Guzzo A., Dubow M.S.;
RT "A luxAB transcriptional fusion to the cryptic celF gene of Escherichia
RT coli displays increased luminescence in the presence of nickel.";
RL Mol. Gen. Genet. 242:455-460(1994).
RN [6]
RP PROTEIN SEQUENCE OF 2-31, MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=10572139; DOI=10.1128/jb.181.23.7339-7345.1999;
RA Thompson J., Ruvinov S.B., Freedberg D.I., Hall B.G.;
RT "Cellobiose-6-phosphate hydrolase (CelF) of Escherichia coli:
RT characterization and assignment to the unusual family 4 of
RT glycosylhydrolases.";
RL J. Bacteriol. 181:7339-7345(1999).
RN [7]
RP IDENTIFICATION OF CHB OPERON.
RX PubMed=9405618; DOI=10.1073/pnas.94.26.14367;
RA Keyhani N.O., Roseman S.;
RT "Wild-type Escherichia coli grows on the chitin disaccharide, N,N'-
RT diacetylchitobiose, by expressing the cel operon.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14367-14371(1997).
RN [8]
RP FUNCTION.
RX PubMed=10913117; DOI=10.1074/jbc.m001043200;
RA Keyhani N.O., Wang L.-X., Lee Y.C., Roseman S.;
RT "The chitin disaccharide, N,N'-diacetylchitobiose, is catabolized by
RT Escherichia coli and is transported/phosphorylated by the
RT phosphoenolpyruvate:glycose phosphotransferase system.";
RL J. Biol. Chem. 275:33084-33090(2000).
CC -!- FUNCTION: Hydrolyzes a wide variety of P-beta-glucosides including
CC cellobiose-6P, salicin-6P, arbutin-6P, gentiobiose-6P, methyl-beta-
CC glucoside-6P and p-nitrophenyl-beta-D-glucopyranoside-6P. Is also able
CC to hydrolyze phospho-N,N'-diacetylchitobiose.
CC {ECO:0000269|PubMed:10572139, ECO:0000269|PubMed:10913117}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-phospho-beta-D-glucosyl-(1->4)-D-glucose + H2O = D-glucose +
CC D-glucose 6-phosphate; Xref=Rhea:RHEA:10772, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58312, ChEBI:CHEBI:61548; EC=3.2.1.86;
CC Evidence={ECO:0000269|PubMed:10572139};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10773;
CC Evidence={ECO:0000269|PubMed:10572139};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:10572139};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10572139};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:10572139};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:10572139};
CC Note=Divalent metal ion. Manganese, cobalt and nickel ions enhance
CC activity whereas magnesium, calcium, strontium and zinc ions do not.
CC {ECO:0000269|PubMed:10572139};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.30 mM for cellobiose-6P {ECO:0000269|PubMed:10572139};
CC KM=0.44 mM for salicin-6P {ECO:0000269|PubMed:10572139};
CC KM=0.35 mM for arbutin-6P {ECO:0000269|PubMed:10572139};
CC KM=12.50 mM for gentiobiose-6P {ECO:0000269|PubMed:10572139};
CC KM=2.22 mM for methyl-beta-glucoside-6P
CC {ECO:0000269|PubMed:10572139};
CC KM=0.44 mM for p-nitrophenyl-beta-D-glucopyranoside-6P
CC {ECO:0000269|PubMed:10572139};
CC Vmax=1.74 umol/min/mg enzyme toward cellobiose-6P
CC {ECO:0000269|PubMed:10572139};
CC Vmax=1.38 umol/min/mg enzyme toward salicin-6P
CC {ECO:0000269|PubMed:10572139};
CC Vmax=2.13 umol/min/mg enzyme toward arbutin-6P
CC {ECO:0000269|PubMed:10572139};
CC Vmax=1.11 umol/min/mg enzyme toward gentiobiose-6P
CC {ECO:0000269|PubMed:10572139};
CC Vmax=0.56 umol/min/mg enzyme toward methyl-beta-glucoside-6P
CC {ECO:0000269|PubMed:10572139};
CC Vmax=1.33 umol/min/mg enzyme toward p-nitrophenyl-beta-D-
CC glucopyranoside-6P {ECO:0000269|PubMed:10572139};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10572139}.
CC -!- INDUCTION: By N,N'-diacetylchitobiose.
CC -!- MASS SPECTROMETRY: Mass=50386; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10572139};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:2179047) characterized as part of a
CC cryptic cel operon for a cellobiose degradation system. The Cel+
CC phenotype is due to mutations making expression chitobiose-independent
CC and altering the substrate specificity. {ECO:0000305|PubMed:2179047}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA37073.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA47257.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA47259.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X52890; CAA37073.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAC74804.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15515.1; -; Genomic_DNA.
DR EMBL; X66725; CAA47257.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X66725; CAA47259.1; ALT_FRAME; Genomic_DNA.
DR PIR; F64932; F64932.
DR RefSeq; NP_416248.1; NC_000913.3.
DR RefSeq; WP_000078765.1; NZ_LN832404.1.
DR AlphaFoldDB; P17411; -.
DR SMR; P17411; -.
DR BioGRID; 4259132; 399.
DR IntAct; P17411; 4.
DR STRING; 511145.b1734; -.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR PaxDb; P17411; -.
DR PRIDE; P17411; -.
DR EnsemblBacteria; AAC74804; AAC74804; b1734.
DR EnsemblBacteria; BAA15515; BAA15515; BAA15515.
DR GeneID; 946266; -.
DR KEGG; ecj:JW1723; -.
DR KEGG; eco:b1734; -.
DR PATRIC; fig|1411691.4.peg.522; -.
DR EchoBASE; EB0142; -.
DR eggNOG; COG1486; Bacteria.
DR HOGENOM; CLU_045951_0_1_6; -.
DR InParanoid; P17411; -.
DR OMA; NEHASHI; -.
DR PhylomeDB; P17411; -.
DR BioCyc; EcoCyc:EG10144-MON; -.
DR BioCyc; MetaCyc:EG10144-MON; -.
DR BRENDA; 3.2.1.86; 2026.
DR SABIO-RK; P17411; -.
DR PRO; PR:P17411; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0103047; F:methyl beta-D-glucoside 6-phosphate glucohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.90.110.10; -; 1.
DR InterPro; IPR019802; GlycHydrolase_4_CS.
DR InterPro; IPR001088; Glyco_hydro_4.
DR InterPro; IPR022616; Glyco_hydro_4_C.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR32092; PTHR32092; 1.
DR Pfam; PF02056; Glyco_hydro_4; 1.
DR Pfam; PF11975; Glyco_hydro_4C; 1.
DR PRINTS; PR00732; GLHYDRLASE4.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cobalt; Direct protein sequencing; Glycosidase;
KW Hydrolase; Manganese; Metal-binding; NAD; Nickel; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10572139"
FT CHAIN 2..450
FT /note="6-phospho-beta-glucosidase"
FT /id="PRO_0000169858"
FT ACT_SITE 258
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 5..73
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT SITE 112
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000250"
SQ SEQUENCE 450 AA; 50513 MW; 7A3BB7299E3ECF5B CRC64;
MSQKLKVVTI GGGSSYTPEL LEGFIKRYHE LPVSELWLVD VEGGKPKLDI IFDLCQRMID
NAGVPMKLYK TLDRREALKD ADFVTTQLRV GQLPARELDE RIPLSHGYLG QETNGAGGLF
KGLRTIPVIF DIVKDVEELC PNAWVINFTN PAGMVTEAVY RHTGFKRFIG VCNIPIGMKM
FIRDVLMLKD SDDLSIDLFG LNHMVFIKDV LINGKSRFAE LLDGVASGQL KASSVKNIFD
LPFSEGLIRS LNLLPCSYLL YYFKQKEMLA IEMGEYYKGG ARAQVVQKVE KQLFELYKNP
ELKVKPKELE QRGGAYYSDA ACEVINAIYN DKQAEHYVNI PHHGQIDNIP ADWAVEMTCK
LGRDGATPHP RITHFDDKVM GLIHTIKGFE IAASNAALSG EFNDVLLALN LSPLVHSDRD
AELLAREMIL AHEKWLPNFA DCIAELKKAH
