[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; PubMed=1630307 [NCBI, ExPASy, EBI, Israel, Japan] Hall B.G., Xu L.; "Nucleotide sequence, function, activation, and evolution of the cryptic asc operon of Escherichia coli K12."; Mol. Biol. Evol. 9:688-706(1992).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).

Comments

FUNCTION: Can hydrolyze salicin, cellobiose, and probably arbutin.
CATALYTIC ACTIVITY: 6-phospho-beta-D-glucosyl-(1,4)-D-glucose + H₂O = D-glucose + D-glucose 6-phosphate.
SIMILARITY: Belongs to the glycosyl hydrolase 1 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M73326; AAA16430.1; -; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U29579; AAA69226.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75758.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76793.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

H65051; H65051.

RefSeq

AP_003283.1; -.
NP_417196.1; -.

3D structure databases

HSSP

P11546; 1PBG. [HSSP ENTRY / PDB]

ModBase

P24240.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10085-MON; -.
MetaCyc:EG10085-MON; -.

Organism-specific databases

EchoBASE

EB0083; -.

EcoGene

EG10085; ascB.

Ontologies

GO:0008706;	Molecular function: 6-phospho-beta-glucosidase activity (inferred from electronic annotation from EC).
GO:0043169;	Molecular function: cation binding (inferred from electronic annotation from InterPro).
GO:0005975;	Biological process: carbohydrate metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001360; Glyco_hydro_1.
IPR013781; Glyco_hydro_sub_cat.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.80; Glyco_hydro_cat; 1.

PANTHER

PTHR10353; Glyco_hydro_1; 1.

Pfam

PF00232; Glyco_hydro_1; 2.
Pfam graphical view of domain structure.

PRINTS

PR00131; GLHYDRLASE1.

PROSITE

PS00572; GLYCOSYL_HYDROL_F1_1; 1.
PS00653; GLYCOSYL_HYDROL_F1_2; 1.

ProtoNet

P24240.

Genome annotation databases

GeneID

947460; -.

GenomeReviews

U00096_GR; b2716.
AP009048_GR; JW2686.

KEGG

ecj:JW2686; -.
eco:b2716; -.

Phylogenomic databases

HOGENOM

P24240; -.

Genome annotation databases

CMR

P24240; b2716.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Glycosidase; Hydrolase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 474`	`474`	`6-phospho-beta-glucosidase ascB.`	`PRO_0000063895`
`ACT_SITE`	`180 180`		`Proton donor (Potential).`
`ACT_SITE`	`372 372`		`Nucleophile (By similarity).`
`CONFLICT`	`405 406`		`EA -> GT (in Ref. 1; AAA16430).`
`CONFLICT`	`428 428`		`S -> C (in Ref. 1; AAA16430).`
`CONFLICT`	`455 456`		`RK -> HR (in Ref. 1; AAA16430).`

Sequence information

Length: 474 AA [This is the length of the unprocessed precursor]

Molecular weight: 53935 Da [This is the MW of the unprocessed precursor]

CRC64: 02ACE6BEBF211011 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSVFPESFLW GGALAANQSE GAFREGDKGL TTVDMIPHGE HRMAVKLGLE KRFQLRDDEF 

        70         80         90        100        110        120 
YPSHEATDFY HRYKEDIALM AEMGFKVFRT SIAWSRLFPQ GDEITPNQQG IAFYRSVFEE 

       130        140        150        160        170        180 
CKKYGIEPLV TLCHFDVPMH LVTEYGSWRN RKLVEFFSRY ARTCFEAFDG LVKYWLTFNE 

       190        200        210        220        230        240 
INIMLHSPFS GAGLVFEEGE NQDQVKYQAA HHQLVASALA TKIAHEVNPQ NQVGCMLAGG 

       250        260        270        280        290        300 
NFYPYSCKPE DVWAALEKDR ENLFFIDVQA RGTYPAYSAR VFREKGVTIN KAPGDDEILK 

       310        320        330        340        350        360 
NTVDFVSFSY YASRCASAEM NANNSSAANV VKSLRNPYLQ VSDWGWGIDP LGLRITMNMM 

       370        380        390        400        410        420 
YDRYQKPLFL VENGLGAKDE FAANGEINDD YRISYLREHI RAMGEAIADG IPLMGYTTWG 

       430        440        450        460        470 
CIDLVSASTG EMSKRYGFVF VDRDDAGNGT LTRTRKKSFW WYKKVIASNG EDLE

P24240 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools