Reviewed, UniProtKB/Swiss-Prot P22073 (BGLA_PAEPO)

Names and origin

Protein names

Recommended name:
    Beta-glucosidase A
      Short name=BGA
    EC=3.2.1.21
Alternative name(s):
    Gentiobiase
    Cellobiase
    Beta-D-glucoside glucohydrolase
    Amygdalase

Gene names

Name:

bglA

Organism

Paenibacillus polymyxa (Bacillus polymyxa)

Taxonomic identifier

1406 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Paenibacillaceae › Paenibacillus

Protein attributes

Sequence length	448 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	BglA is intracellular and cleaves cellobiose probably through inorganic phosphate mediated hydrolysis.
Catalytic activity	Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Subunit structure	Homooctamer.
Sequence similarities	Belongs to the glycosyl hydrolase 1 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	beta-glucosidase activity Inferred from electronic annotation. Source: EC cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 448

448

Beta-glucosidase A

PRO_0000063871

Sites

Active site

166

1

Proton donor Potential

Active site

352

1

Nucleophile By similarity

Secondary structure

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448

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Beta strand

11 – 15

5

Helix

18 – 21

4

Helix

27 – 29

3

Helix

34 – 39

6

Turn

42 – 44

3

Helix

46 – 48

3

Beta strand

51 – 53

3

Helix

57 – 70

14

Beta strand

74 – 79

6

Helix

82 – 85

4

Beta strand

86 – 91

6

Helix

95 – 110

16

Beta strand

114 – 122

9

Helix

126 – 130

5

Helix

133 – 135

3

Helix

138 – 153

16

Helix

155 – 157

3

Beta strand

160 – 165

6

Helix

167 – 175

9

Helix

187 – 210

24

Beta strand

214 – 220

7

Beta strand

226 – 231

6

Helix

233 – 246

14

Helix

248 – 256

9

Helix

261 – 268

8

Turn

269 – 271

3

Helix

280 – 284

5

Beta strand

289 – 294

6

Beta strand

299 – 303

5

Helix

308 – 310

3

Beta strand

312 – 315

4

Helix

331 – 339

9

Helix

340 – 343

4

Beta strand

348 – 353

6

Helix

369 – 387

19

Beta strand

392 – 398

7

Helix

406 – 411

6

Beta strand

416 – 419

4

Turn

421 – 423

3

Beta strand

426 – 428

3

Helix

430 – 441

12

Beta strand

443 – 445

3

Sequences

	Sequence		Length	Mass (Da)
	P22073-1 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: D971D2E61B6627C1	FASTA	448	51,649
	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

References

[1]	"Sequences and homology analysis of two genes encoding beta-glucosidases from Bacillus polymyxa." Gonzalez-Candelas L., Ramon D., Polaina J. Gene 95:31-38(1990) [PubMed: 2123813] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Crystal structure of beta-glucosidase A from Bacillus polymyxa: insights into the catalytic activity in family 1 glycosyl hydrolases." Sanz-Aparicio J., Hermoso J.A., Martinez-Ripoll M., Lequerica J.L., Polaina J. J. Mol. Biol. 275:491-502(1998) [PubMed: 9466926] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). Strain: ATCC 842 / DSM 36 / IFO 15309 / NCIB 8158 / NCTC 10343.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M60210 Genomic DNA. Translation: AAA22263.1.

PIR

JW0037.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BGA	X-ray	2.40	A/B/C/D	2-448	[»]
1BGG	X-ray	2.30	A/B/C/D	1-448	[»]
1E4I	X-ray	2.00	A	2-448	[»]
1TR1	X-ray	2.20	A/B/C/D	2-448	[»]
1UYQ	X-ray	2.20	A	2-448	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH1. Glycoside Hydrolase Family 1.

Enzyme and pathway databases

BRENDA

3.2.1.21. 276031.

Family and domain databases

InterPro

IPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR017736. Glyco_hydro_1_beta-glucosidase.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

PANTHER

PTHR10353. Glyco_hydro_1. 1 hit.

Pfam

PF00232. Glyco_hydro_1. 1 hit.
[Graphical view]

PRINTS

PR00131. GLHYDRLASE1.

TIGRFAMs

TIGR03356. BGL. 1 hit.

PROSITE

PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

BGLA_PAEPO

Accession

Primary (citable) accession number: P22073

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)