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P17411 (CHBF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
6-phospho-beta-glucosidase

EC=3.2.1.86
Alternative name(s):
Cellobiose-6-phosphate hydrolase
Phospho-chitobiase
Gene names
Name:chbF
Synonyms:celF, ydjD
Ordered Locus Names:b1734, JW1723
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Catalytic activity

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

Cofactor

NAD.

Divalent metal ion. Manganese, cobalt and nickel ions enhance activity whereas magnesium, calcium, strontium and zinc ions do not.

Subunit structure

Homotetramer.

Induction

By N,N'-diacetylchitobiose.

Sequence similarities

Belongs to the glycosyl hydrolase 4 family.

Caution

Was originally (Ref.1) 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.

Mass spectrometry

Molecular mass is 50386 Da from positions 2 - 450. Determined by ESI. Ref.6

Sequence caution

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

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 4504496-phospho-beta-glucosidase
PRO_0000169858

Regions

Nucleotide binding5 – 7369NAD By similarity

Sites

Active site2581Proton acceptor By similarity
Metal binding1721Manganese By similarity
Metal binding2031Manganese By similarity
Binding site961Substrate By similarity
Binding site1501Substrate By similarity
Site1121Increases basicity of active site Tyr By similarity

Sequences

Sequence LengthMass (Da)Tools
P17411 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 7A3BB7299E3ECF5B

FASTA45050,513
        10         20         30         40         50         60 
MSQKLKVVTI GGGSSYTPEL LEGFIKRYHE LPVSELWLVD VEGGKPKLDI IFDLCQRMID 

        70         80         90        100        110        120 
NAGVPMKLYK TLDRREALKD ADFVTTQLRV GQLPARELDE RIPLSHGYLG QETNGAGGLF 

       130        140        150        160        170        180 
KGLRTIPVIF DIVKDVEELC PNAWVINFTN PAGMVTEAVY RHTGFKRFIG VCNIPIGMKM 

       190        200        210        220        230        240 
FIRDVLMLKD SDDLSIDLFG LNHMVFIKDV LINGKSRFAE LLDGVASGQL KASSVKNIFD 

       250        260        270        280        290        300 
LPFSEGLIRS LNLLPCSYLL YYFKQKEMLA IEMGEYYKGG ARAQVVQKVE KQLFELYKNP 

       310        320        330        340        350        360 
ELKVKPKELE QRGGAYYSDA ACEVINAIYN DKQAEHYVNI PHHGQIDNIP ADWAVEMTCK 

       370        380        390        400        410        420 
LGRDGATPHP RITHFDDKVM GLIHTIKGFE IAASNAALSG EFNDVLLALN LSPLVHSDRD 

       430        440        450 
AELLAREMIL AHEKWLPNFA DCIAELKKAH 

« Hide

References

« Hide 'large scale' references
[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]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRF64932.
RefSeqNP_416248.1. NC_000913.3.
YP_489995.1. NC_007779.1.

3D structure databases

ProteinModelPortalP17411.
SMRP17411. Positions 4-439.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP17411. 4 interactions.
STRING511145.b1734.

Protein family/group databases

CAZyGH4. Glycoside Hydrolase Family 4.

Proteomic databases

PaxDbP17411.
PRIDEP17411.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74804; AAC74804; b1734.
BAA15515; BAA15515; BAA15515.
GeneID12930138.
946266.
KEGGecj:Y75_p1709.
eco:b1734.
PATRIC32118777. VBIEscCol129921_1806.

Organism-specific databases

EchoBASEEB0142.
EcoGeneEG10144. chbF.

Phylogenomic databases

eggNOGCOG1486.
HOGENOMHOG000239811.
KOK01222.
OMAPSGHITE.
OrthoDBEOG6CP3SG.
PhylomeDBP17411.

Enzyme and pathway databases

BioCycEcoCyc:EG10144-MONOMER.
ECOL316407:JW1723-MONOMER.
MetaCyc:EG10144-MONOMER.
SABIO-RKP17411.

Gene expression databases

GenevestigatorP17411.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProIPR019802. 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]
PfamPF02056. Glyco_hydro_4. 1 hit.
PF11975. Glyco_hydro_4C. 1 hit.
[Graphical view]
PRINTSPR00732. GLHYDRLASE4.
SUPFAMSSF56327. SSF56327. 1 hit.
PROSITEPS01324. GLYCOSYL_HYDROL_F4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP17411.

Entry information

Entry nameCHBF_ECOLI
AccessionPrimary (citable) accession number: P17411
Secondary accession number(s): P37795, P78290
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 127 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene