[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0378-1119(90)90410-S; PubMed=2123813 [NCBI, ExPASy, EBI, Israel, Japan] Gonzalez-Candelas L., Ramon D., Polaina J.; "Sequences and homology analysis of two genes encoding beta-glucosidases from Bacillus polymyxa."; Gene 95:31-38(1990).

Comments

CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
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

M60211; AAA22264.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JW0038; JW0038.

3D structure databases

PDB

2JIE; X-ray; 2.30 A; A=2-448.	[ExPASy / RCSB / EBI]
2O9P; X-ray; 2.10 A; A=2-448.	[ExPASy / RCSB / EBI]
2O9R; X-ray; 2.30 A; A=4-448.	[ExPASy / RCSB / EBI]
2O9T; X-ray; 2.15 A; A=2-448.	[ExPASy / RCSB / EBI]
2Z1S; X-ray; 2.46 A; A=2-448.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2JIE; -.
2O9P; -.
2O9R; -.
2O9T; -.
2Z1S; -.

ModBase

P22505.

Ontologies

GO:0008422;	Molecular function: beta-glucosidase activity (inferred from electronic annotation from EC).
GO:0043169;	Molecular function: cation binding (inferred from electronic annotation from InterPro).
GO:0030245;	Biological process: cellulose catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001360; Glyco_hydro_1.
IPR017736; Glyco_hydro_1_beta-glucosidase.
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.

ProtoNet

P22505.

Other

UniRef

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

Keywords

3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase; Polysaccharide degradation.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 448`	`448`	`Beta-glucosidase B.`	`PRO_0000063872`
`ACT_SITE`	`167 167`		`Proton donor (Potential).`
`ACT_SITE`	`356 356`		`Nucleophile (By similarity).`
`STRAND`	`13 17`	`5`
`HELIX`	`20 23`	`4`
`HELIX`	`36 40`	`5`
`HELIX`	`48 50`	`3`
`STRAND`	`53 55`	`3`
`HELIX`	`59 72`	`14`
`STRAND`	`77 81`	`5`
`HELIX`	`84 87`	`4`
`HELIX`	`96 112`	`17`
`STRAND`	`115 123`	`9`
`HELIX`	`127 131`	`5`
`HELIX`	`134 136`	`3`
`HELIX`	`139 154`	`16`
`STRAND`	`155 158`	`4`
`STRAND`	`160 166`	`7`
`HELIX`	`168 176`	`9`
`STRAND`	`178 181`	`4`
`HELIX`	`188 211`	`24`
`STRAND`	`216 223`	`8`
`STRAND`	`227 232`	`6`
`HELIX`	`234 247`	`14`
`HELIX`	`249 257`	`9`
`HELIX`	`262 268`	`7`
`HELIX`	`269 275`	`7`
`HELIX`	`282 286`	`5`
`STRAND`	`292 296`	`5`
`STRAND`	`301 305`	`5`
`STRAND`	`308 312`	`5`
`STRAND`	`314 317`	`4`
`STRAND`	`321 323`	`3`
`HELIX`	`332 344`	`13`
`STRAND`	`352 357`	`6`
`HELIX`	`373 389`	`17`
`TURN`	`390 393`	`4`
`STRAND`	`396 402`	`7`
`HELIX`	`410 415`	`6`
`STRAND`	`420 423`	`4`
`TURN`	`425 427`	`3`
`STRAND`	`430 432`	`3`
`HELIX`	`434 445`	`12`

Sequence information

Length: 448 AA [This is the length of the unprocessed precursor]

Molecular weight: 51573 Da [This is the MW of the unprocessed precursor]

CRC64: 628F44507C21EF1F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSENTFIFPA TFMWGTSTSS YQIEGGTDEG GRTPSIWDTF CQIPGKVIGG DCGDVACDHF 

        70         80         90        100        110        120 
HHFKEDVQLM KQLGFLHYRF SVAWPRIMPA AGIINEEGLL FYEHLLDEIE LAGLIPMLTL 

       130        140        150        160        170        180 
YHWDLPQWIE DEGGWTQRET IQHFKTYASV IMDRFGERIN WWNTINEPYC ASILGYGTGE 

       190        200        210        220        230        240 
HAPGHENWRE AFTAAHHILM CHGIASNLHK EKGLTGKIGI TLNMEHVDAA SERPEDVAAA 

       250        260        270        280        290        300 
IRRDGFINRW FAEPLFNGKY PEDMVEWYGT YLNGLDFVQP GDMELIQQPG DFLGINYYTR 

       310        320        330        340        350        360 
SIIRSTNDAS LLQVEQVHME EPVTDMGWEI HPESFYKLLT RIEKDFSKGL PILITENGAA 

       370        380        390        400        410        420 
MRDELVNGQI EDTGRHGYIE EHLKACHRFI EEGGQLKGYF VWSFLDNFEW AWGYSKRFGI 

       430        440 
VHINYETQER TPKQSALWFK QMMAKNGF

P22505 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