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UniProtKB/Swiss-Prot entry P22073

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name BGLA_PAEPO
Primary accession number P22073
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1991
Sequence was last modified on August 1, 1991 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 64)
Name and origin of the protein
Protein name Beta-glucosidase A
Synonyms BGA
EC 3.2.1.21
Gentiobiase
Cellobiase
Beta-D-glucoside glucohydrolase
Amygdalase
Gene name
Name: bglA
From
Paenibacillus polymyxa (Bacillus polymyxa) [TaxID: 1406] 
Taxonomy Bacteria; Firmicutes; Bacillales; Paenibacillaceae; Paenibacillus.
Protein existence 1: Evidence at protein level;
References
[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).
[2]
 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
STRAIN=ATCC 842 / DSM 36 / IFO 15309 / NCIB 8158 / NCTC 10343;
DOI=10.1006/jmbi.1997.1467; PubMed=9466926 [NCBI, ExPASy, EBI, Israel, Japan]
Sanz-Aparicio J., Hermoso J.A., Martinez-Ripoll M., Lequerica J.L., Polaina J.;
"Crystal structure of beta-glucosidase A from Bacillus polymyxa: insights into the catalytic activity in family 1 glycosyl hydrolases.";
J. Mol. Biol. 275:491-502(1998).
Comments
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
M60210; AAA22263.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JW0037; JW0037.
3D structure databases
PDB
1BGA; X-ray; 2.40 A; A/B/C/D=2-448.[ExPASy / RCSB / EBI]
1BGG; X-ray; 2.30 A; A/B/C/D=1-448.[ExPASy / RCSB / EBI]
1E4I; X-ray; 2.00 A; A=2-448.[ExPASy / RCSB / EBI]
1TR1; X-ray; 2.20 A; A/B/C/D=2-448.[ExPASy / RCSB / EBI]
1UYQ; X-ray; 2.20 A; A=2-448.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BGA; -.
1BGG; -.
1E4I; -.
1TR1; -.
1UYQ; -.
ModBase P22073.
Ontologies
GO
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 P22073.
Other
LinkHub P22073; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase; Polysaccharide degradation.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   448  448     Beta-glucosidase A. PRO_0000063871
ACT_SITE   166   166        Proton donor (Potential). 
ACT_SITE   352   352        Nucleophile (By similarity). 
STRAND   3     5  3      
STRAND   11    15  5      
HELIX   18    21  4      
HELIX   27    29  3      
HELIX   34    39  6      
TURN   42    44  3      
HELIX   46    48  3      
STRAND   51    53  3      
HELIX   57    70  14      
STRAND   74    79  6      
HELIX   82    85  4      
STRAND   86    91  6      
HELIX   95   110  16      
STRAND   114   122  9      
HELIX   126   130  5      
HELIX   133   135  3      
HELIX   138   153  16      
HELIX   155   157  3      
STRAND   160   165  6      
HELIX   167   175  9      
HELIX   187   210  24      
STRAND   214   220  7      
STRAND   226   231  6      
HELIX   233   246  14      
HELIX   248   256  9      
HELIX   261   268  8      
TURN   269   271  3      
HELIX   280   284  5      
STRAND   289   294  6      
STRAND   299   303  5      
HELIX   308   310  3      
STRAND   312   315  4      
HELIX   331   339  9      
HELIX   340   343  4      
STRAND   348   353  6      
HELIX   369   387  19      
STRAND   392   398  7      
HELIX   406   411  6      
STRAND   416   419  4      
TURN   421   423  3      
STRAND   426   428  3      
HELIX   430   441  12      
STRAND   443   445  3      
Sequence information
Length: 448 AA [This is the length of the unprocessed precursor] Molecular weight: 51649 Da [This is the MW of the unprocessed precursor] CRC64: D971D2E61B6627C1 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MTIFQFPQDF MWGTATAAYQ IEGAYQEDGR GLSIWDTFAH TPGKVFNGDN GNVACDSYHR 

        70         80         90        100        110        120 
YEEDIRLMKE LGIRTYRFSV SWPRIFPNGD GEVNQEGLDY YHRVVDLLND NGIEPFCTLY 

       130        140        150        160        170        180 
HWDLPQALQD AGGWGNRRTI QAFVQFAETM FREFHGKIQH WLTFNEPWCI AFLSNMLGVH 

       190        200        210        220        230        240 
APGLTNLQTA IDVGHHLLVA HGLSVRRFRE LGTSGQIGIA PNVSWAVPYS TSEEDKAACA 

       250        260        270        280        290        300 
RTISLHSDWF LQPIYQGSYP QFLVDWFAEQ GATVPIQDGD MDIIGEPIDM IGINYYSMSV 

       310        320        330        340        350        360 
NRFNPEAGFL QSEEINMGLP VTDIGWPVES RGLYEVLHYL QKYGNIDIYI TENGACINDE 

       370        380        390        400        410        420 
VVNGKVQDDR RISYMQQHLV QVHRTIHDGL HVKGYMAWSL LDNFEWAEGY NMRFGMIHVD 

       430        440 
FRTQVRTPKE SYYWYRNVVS NNWLETRR
P22073 in FASTA format

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