NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1732212 [NCBI, ExPASy, EBI, Israel, Japan]
el Hassouni M., Henrissat B., Chippaux M., Barras F.;
"Nucleotide sequences of the arb genes, which control beta-glucoside utilization in Erwinia chrysanthemi: comparison with the Escherichia coli bgl operon and evidence for a new beta-glycohydrolase family including enzymes from eubacteria, archeabacteria, and humans.";
J. Bacteriol. 174:765-777(1992).

Comments

CATALYTIC ACTIVITY: 6-phospho-beta-D-glucosyl-(1,4)-D-glucose + H₂O = D-glucose + D-glucose 6-phosphate.
PATHWAY: Carbohydrate metabolism; beta-glucoside metabolism .
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

M81772; AAA24815.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C42603; C42603.

3D structure databases

HSSP

P11546; 1PBG. [HSSP ENTRY / PDB]

ModBase

P26206.

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; 1.
Pfam graphical view of domain structure.

PRINTS

PR00131; GLHYDRLASE1.

PROSITE

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

Other

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

Keywords

Glycosidase; Hydrolase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 465`	`465`	`6-phospho-beta-glucosidase.`	`PRO_0000063899`
`ACT_SITE`	`173 173`		`Proton donor (Potential).`
`ACT_SITE`	`362 362`		`Nucleophile (By similarity).`

Sequence information

Length: 465 AA [This is the length of the unprocessed precursor]

Molecular weight: 52983 Da [This is the MW of the unprocessed precursor]

CRC64: B3D4E1C4AF0AC36B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSNPFPAHFL WGGAIAANQV EGAYLTDGKG LSTSDLQPQG IFGEIVTRQP GDSGIKDVAI 

        70         80         90        100        110        120 
DFYHRYPQDI ALFAEMGFTC LRISIAWTRI FPQGDEAEPN EAGLAFYDRL FDELAKYGIQ 

       130        140        150        160        170        180 
PLVTLSHYEM PYGLVEKHGG WGNRLTIDCF ERYARTVFAR YRHKVKRWLT FNEINMSLHA 

       190        200        210        220        230        240 
PFTGVGLPPD SDKAAIYQAI HHQLVASARA VKACHDMIPD AQIGNMLLGA MLYPLTSKPE 

       250        260        270        280        290        300 
DVMESLHQNR EWLFFGDVQV RGAYPGYMHR YFREQGITLN ITAQDKQDLK ATVDFISFSY 

       310        320        330        340        350        360 
YMTGCVTTDE AQLEKTRGNI LNMVPNPYLE SSEWGWQIDP LGLRYLLNFL YDRYQKPLFI 

       370        380        390        400        410        420 
VENGLGAKDK IEENGDIYDD YRIRYLNDHL VQVGEAIDDG VEVLGYTCWG PIDLVSASKA 

       430        440        450        460 
EMSKRYGFIY VDRDDAGHGS LERRRKKSFY WYQSVIASHG KTLTR

P26206 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