P17411 (CHBF_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	450 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	Cobalt Manganese Metal-binding NAD Nickel
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	carbohydrate catabolic process Inferred from genetic interaction Ref.7. Source: EcoCyc
Molecular function	6-phospho-beta-glucosidase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6
	Chain	2 – 450	449	6-phospho-beta-glucosidase		PRO_0000169858
Regions
	Nucleotide binding	5 – 73	69	NAD By similarity
Sites
	Active site	258	1	Proton acceptor By similarity
	Metal binding	172	1	Manganese By similarity
	Metal binding	203	1	Manganese By similarity
	Binding site	96	1	Substrate By similarity
	Binding site	150	1	Substrate By similarity
	Site	112	1	Increases basicity of active site Tyr By similarity

Sequences

	Sequence		Length	Mass (Da)
	P17411 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 7A3BB7299E3ECF5B	FASTA	450	50,513
	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

References

	« Hide 'large scale' referencesShow '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: 2179047] [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. , 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: 9097039] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 8121401] [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: 10572139] [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: 9405618] [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: 10913117] [Abstract] Cited for: FUNCTION.

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.
PIR	F64932.
RefSeq	NP_416248.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P17411.
SMR	P17411. Positions 4-442.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-9267N.
IntAct	P17411. 4 interactions.
Protein family/group databases
CAZy	GH4. Glycoside Hydrolase Family 4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000000376; EBESCP00000000376; EBESCG00000000309. EBESCT00000014735; EBESCP00000014026; EBESCG00000013795.
GeneID	946266.
GenomeReviews	Gene locus JW1723 in contig AP009048_GR. Gene locus b1734 in contig U00096_GR.
KEGG	ecj:JW1723. eco:b1734.
PATRIC	32118777. VBIEscCol129921_1806.
Organism-specific databases
EchoBASE	EB0142.
EcoGene	EG10144. chbF.
Phylogenomic databases
eggNOG	COG1486.
GeneTree	EBGT00050000010199.
HOGENOM	HBG511715.
OMA	AKDERIP.
PhylomeDB	P17411.
ProtClustDB	CLSK880178.
Enzyme and pathway databases
BioCyc	EcoCyc:EG10144-MONOMER. MetaCyc:EG10144-MONOMER.
Gene expression databases
Genevestigator	P17411.
Family and domain databases
InterPro	IPR019802. 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]
Gene3D	G3DSA:3.90.110.10. lact_mal_DH. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K01222.
Pfam	PF02056. Glyco_hydro_4. 1 hit. PF11975. Glyco_hydro_4C. 1 hit. [Graphical view]
PRINTS	PR00732. GLHYDRLASE4.
SUPFAM	SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.
PROSITE	PS01324. GLYCOSYL_HYDROL_F4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CHBF_ECOLI

Accession

Primary (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:	January 25, 2012
This is version 109 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program