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   24-JAN-2024, entry version 176.
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; Pseudomonadota; 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=1.3 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=12.5 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
CC         p-nitrophenyl-beta-D-glucopyranoside-6P
CC         {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};
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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; 511145-b1734; -.
DR   EnsemblBacteria; AAC74804; AAC74804; b1734.
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   OrthoDB; 9767022at2; -.
DR   PhylomeDB; P17411; -.
DR   BioCyc; EcoCyc:EG10144-MONOMER; -.
DR   BioCyc; MetaCyc:EG10144-MONOMER; -.
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   GO; GO:0052777; P:diacetylchitobiose catabolic process; IMP:EcoCyc.
DR   CDD; cd05296; GH4_P_beta_glucosidase; 1.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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:SF5; 6-PHOSPHO-BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR   Pfam; PF02056; Glyco_hydro_4; 1.
DR   Pfam; PF11975; Glyco_hydro_4C; 1.
DR   PRINTS; PR00732; GLHYDRLASE4.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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
//