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Protein

6-phospho-beta-glucosidase

Gene

chbF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes a wide variety of P-beta-glucosides including cellobiose-6P, salicin-6P, arbutin-6P, gentiobiose-6P, methyl-beta-glucoside-6P and p-nitrophenyl-beta-D-glucopyranoside-6P. Is also able to hydrolyze phospho-N,N'-diacetylchitobiose.1 Publication

Catalytic activityi

6-phospho-beta-D-glucosyl-(1,4)-D-glucose + H2O = D-glucose + D-glucose 6-phosphate.

Cofactori

Protein has several cofactor binding sites:
  • NAD(+)
  • Mn2+, Co2+, Ni2+Note: Divalent metal ion. Manganese, cobalt and nickel ions enhance activity whereas magnesium, calcium, strontium and zinc ions do not.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei96 – 961SubstrateBy similarity
Sitei112 – 1121Increases basicity of active site TyrBy similarity
Binding sitei150 – 1501SubstrateBy similarity
Metal bindingi172 – 1721ManganeseBy similarity
Metal bindingi203 – 2031ManganeseBy similarity
Active sitei258 – 2581Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi5 – 7369NADBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Cobalt, Manganese, Metal-binding, NAD, Nickel

Enzyme and pathway databases

BioCyciEcoCyc:EG10144-MONOMER.
ECOL316407:JW1723-MONOMER.
MetaCyc:EG10144-MONOMER.
BRENDAi3.2.1.86. 2026.
SABIO-RKP17411.

Protein family/group databases

CAZyiGH4. Glycoside Hydrolase Family 4.

Names & Taxonomyi

Protein namesi
Recommended name:
6-phospho-beta-glucosidase (EC:3.2.1.86)
Alternative name(s):
Cellobiose-6-phosphate hydrolase
Phospho-chitobiase
Gene namesi
Name:chbF
Synonyms:celF, ydjD
Ordered Locus Names:b1734, JW1723
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10144. chbF.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 4504496-phospho-beta-glucosidasePRO_0000169858Add
BLAST

Proteomic databases

PaxDbiP17411.
PRIDEiP17411.

Expressioni

Inductioni

By N,N'-diacetylchitobiose.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

IntActiP17411. 4 interactions.
STRINGi511145.b1734.

Structurei

3D structure databases

ProteinModelPortaliP17411.
SMRiP17411. Positions 4-439.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 4 family.Curated

Phylogenomic databases

eggNOGiCOG1486.
HOGENOMiHOG000239811.
InParanoidiP17411.
KOiK01222.
OMAiCNVPINF.
OrthoDBiEOG6CP3SG.
PhylomeDBiP17411.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProiIPR019802. GlycHydrolase_4_CS.
IPR001088. Glyco_hydro_4.
IPR022616. Glyco_hydro_4_C.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF02056. Glyco_hydro_4. 1 hit.
PF11975. Glyco_hydro_4C. 1 hit.
[Graphical view]
PRINTSiPR00732. GLHYDRLASE4.
SUPFAMiSSF56327. SSF56327. 1 hit.
PROSITEiPS01324. GLYCOSYL_HYDROL_F4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17411-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQKLKVVTI GGGSSYTPEL LEGFIKRYHE LPVSELWLVD VEGGKPKLDI
60 70 80 90 100
IFDLCQRMID NAGVPMKLYK TLDRREALKD ADFVTTQLRV GQLPARELDE
110 120 130 140 150
RIPLSHGYLG QETNGAGGLF KGLRTIPVIF DIVKDVEELC PNAWVINFTN
160 170 180 190 200
PAGMVTEAVY RHTGFKRFIG VCNIPIGMKM FIRDVLMLKD SDDLSIDLFG
210 220 230 240 250
LNHMVFIKDV LINGKSRFAE LLDGVASGQL KASSVKNIFD LPFSEGLIRS
260 270 280 290 300
LNLLPCSYLL YYFKQKEMLA IEMGEYYKGG ARAQVVQKVE KQLFELYKNP
310 320 330 340 350
ELKVKPKELE QRGGAYYSDA ACEVINAIYN DKQAEHYVNI PHHGQIDNIP
360 370 380 390 400
ADWAVEMTCK LGRDGATPHP RITHFDDKVM GLIHTIKGFE IAASNAALSG
410 420 430 440 450
EFNDVLLALN LSPLVHSDRD AELLAREMIL AHEKWLPNFA DCIAELKKAH
Length:450
Mass (Da):50,513
Last modified:January 23, 2007 - v4
Checksum:i7A3BB7299E3ECF5B
GO

Sequence cautioni

The sequence CAA37073.1 differs from that shown. Reason: Frameshift at several positions. Curated
The sequence CAA47257.1 differs from that shown. Reason: Frameshift at several positions. Curated
The sequence CAA47259.1 differs from that shown. Reason: Frameshift at several positions. Curated

Mass spectrometryi

Molecular mass is 50386 Da from positions 2 - 450. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52890 Genomic DNA. Translation: CAA37073.1. Frameshift.
U00096 Genomic DNA. Translation: AAC74804.1.
AP009048 Genomic DNA. Translation: BAA15515.1.
X66725 Genomic DNA. Translation: CAA47257.1. Frameshift.
X66725 Genomic DNA. Translation: CAA47259.1. Frameshift.
PIRiF64932.
RefSeqiNP_416248.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC74804; AAC74804; b1734.
BAA15515; BAA15515; BAA15515.
GeneIDi946266.
KEGGiecj:Y75_p1709.
eco:b1734.
PATRICi32118777. VBIEscCol129921_1806.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52890 Genomic DNA. Translation: CAA37073.1. Frameshift.
U00096 Genomic DNA. Translation: AAC74804.1.
AP009048 Genomic DNA. Translation: BAA15515.1.
X66725 Genomic DNA. Translation: CAA47257.1. Frameshift.
X66725 Genomic DNA. Translation: CAA47259.1. Frameshift.
PIRiF64932.
RefSeqiNP_416248.1. NC_000913.3.

3D structure databases

ProteinModelPortaliP17411.
SMRiP17411. Positions 4-439.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP17411. 4 interactions.
STRINGi511145.b1734.

Protein family/group databases

CAZyiGH4. Glycoside Hydrolase Family 4.

Proteomic databases

PaxDbiP17411.
PRIDEiP17411.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74804; AAC74804; b1734.
BAA15515; BAA15515; BAA15515.
GeneIDi946266.
KEGGiecj:Y75_p1709.
eco:b1734.
PATRICi32118777. VBIEscCol129921_1806.

Organism-specific databases

EchoBASEiEB0142.
EcoGeneiEG10144. chbF.

Phylogenomic databases

eggNOGiCOG1486.
HOGENOMiHOG000239811.
InParanoidiP17411.
KOiK01222.
OMAiCNVPINF.
OrthoDBiEOG6CP3SG.
PhylomeDBiP17411.

Enzyme and pathway databases

BioCyciEcoCyc:EG10144-MONOMER.
ECOL316407:JW1723-MONOMER.
MetaCyc:EG10144-MONOMER.
BRENDAi3.2.1.86. 2026.
SABIO-RKP17411.

Miscellaneous databases

PROiP17411.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProiIPR019802. GlycHydrolase_4_CS.
IPR001088. Glyco_hydro_4.
IPR022616. Glyco_hydro_4_C.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF02056. Glyco_hydro_4. 1 hit.
PF11975. Glyco_hydro_4C. 1 hit.
[Graphical view]
PRINTSiPR00732. GLHYDRLASE4.
SUPFAMiSSF56327. SSF56327. 1 hit.
PROSITEiPS01324. GLYCOSYL_HYDROL_F4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization and nucleotide sequence of the cryptic cel operon of Escherichia coli K12."
    Parker L.L., Hall B.G.
    Genetics 124:455-471(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "A luxAB transcriptional fusion to the cryptic celF gene of Escherichia coli displays increased luminescence in the presence of nickel."
    Guzzo A., Dubow M.S.
    Mol. Gen. Genet. 242:455-460(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 362-450.
    Strain: K12.
  6. "Cellobiose-6-phosphate hydrolase (CelF) of Escherichia coli: characterization and assignment to the unusual family 4 of glycosylhydrolases."
    Thompson J., Ruvinov S.B., Freedberg D.I., Hall B.G.
    J. Bacteriol. 181:7339-7345(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-31, CHARACTERIZATION, MASS SPECTROMETRY.
  7. "Wild-type Escherichia coli grows on the chitin disaccharide, N,N'-diacetylchitobiose, by expressing the cel operon."
    Keyhani N.O., Roseman S.
    Proc. Natl. Acad. Sci. U.S.A. 94:14367-14371(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF CHB OPERON.
  8. "The chitin disaccharide, N,N'-diacetylchitobiose, is catabolized by Escherichia coli and is transported/phosphorylated by the phosphoenolpyruvate:glycose phosphotransferase system."
    Keyhani N.O., Wang L.-X., Lee Y.C., Roseman S.
    J. Biol. Chem. 275:33084-33090(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiCHBF_ECOLI
AccessioniPrimary (citable) accession number: P17411
Secondary accession number(s): P37795, P78290
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 134 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally (PubMed:2179047) characterized as part of a cryptic cel operon for a cellobiose degradation system. The Cel+ phenotype is due to mutations making expression chitobiose-independent and altering the substrate specificity.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.