Q03506 (BGLA_BACCI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-glucosidase
EC=3.2.1.21

Alternative name(s):
Amygdalase
Beta-D-glucoside glucohydrolase
Cellobiase
Gentiobiase

Gene names

Name:

bglA

Organism

Bacillus circulans

Taxonomic identifier

1397 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	450 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
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 Direct protein sequencing
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

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 450

449

Beta-glucosidase

PRO_0000063870

Sites

Active site

166

1

Proton donor Potential

Active site

355

1

Nucleophile By similarity

Secondary structure

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450

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Beta strand

11 – 15

5

Helix

18 – 21

4

Helix

34 – 40

7

Turn

42 – 44

3

Helix

46 – 48

3

Turn

51 – 55

5

Helix

61 – 71

11

Beta strand

74 – 79

6

Helix

82 – 85

4

Beta strand

89 – 92

4

Helix

95 – 110

16

Beta strand

114 – 122

9

Helix

126 – 129

4

Turn

130 – 132

3

Helix

133 – 135

3

Helix

138 – 154

17

Turn

155 – 157

3

Beta strand

160 – 165

6

Helix

167 – 175

9

Helix

187 – 210

24

Beta strand

215 – 220

6

Beta strand

225 – 231

7

Helix

233 – 244

12

Turn

245 – 247

3

Helix

248 – 255

8

Helix

261 – 269

9

Helix

280 – 284

5

Beta strand

289 – 294

6

Beta strand

298 – 303

6

Helix

307 – 309

3

Turn

310 – 313

4

Beta strand

314 – 316

3

Helix

333 – 345

13

Beta strand

351 – 355

5

Helix

373 – 391

19

Beta strand

396 – 402

7

Helix

410 – 412

3

Beta strand

420 – 424

5

Turn

425 – 428

4

Beta strand

429 – 432

4

Helix

434 – 445

12

Beta strand

446 – 449

4

Sequences

	Sequence		Length	Mass (Da)
	Q03506 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: C52C1DB233B72790	FASTA	450	51,303
	10 20 30 40 50 60 MSIHMFPSDF KWGVATAAYQ IEGAYNEDGR GMSIWDTFAH TPGKVKNGDN GNVACDSYHR 70 80 90 100 110 120 VEEDVQLLKD LGVKVYRFSI SWPRVLPQGT GEVNRAGLDY YHRLVDELLA NGIEPFCTLY 130 140 150 160 170 180 HWDLPQALQD QGGWGSRITI DAFAEYAELM FKELGGKIKQ WITFNEPWCM AFLSNYLGVH 190 200 210 220 230 240 APGNKDLQLA IDVSHHLLVA HGRAVTLFRE LGISGEIGIA PNTSWAVPYR RTKEDMEACL 250 260 270 280 290 300 RVNGWSGDWY LDPIYFGEYP KFMLDWYENL GYKPPIVDGD MELIHQPIDF IGINYYTSSM 310 320 330 340 350 360 NRYNPGEAGG MLSSEAISMG APKTDIGWEI YAEGLYDLLR YTADKYGNPT LYITENGACY 370 380 390 400 410 420 NDGLSLDGRI HDQRRIDYLA MHLIQASRAI EDGINLKGYM EWSLMDNFEW AEGYGMRFGL 430 440 450 VHVDYDTLVR TPKDSFYWYK GVISRGWLDL

References

[1]	"Purification, characterization, gene cloning, and sequencing of a new beta-glucosidase from Bacillus circulans subsp. alkalophilus." Paavilainen S.K., Hellman J., Korpela T. Appl. Environ. Microbiol. 59:927-932(1993) [PubMed: 8481013] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-29. Strain: ATCC 21783 / subsp. Alkalophilus.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M96979 Genomic DNA. Translation: AAA22266.1.

PIR

A48969.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QOX	X-ray	2.70	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P	2-449	[»]

ProteinModelPortal

Q03506.

SMR

Q03506. Positions 2-450.

ModBase

Search...

Protein family/group databases

CAZy

GH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR017736. Glyco_hydro_1_beta-glucosidase.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[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.

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

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_BACCI

Accession

Primary (citable) accession number: Q03506

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	January 23, 2007
Last modified:	May 31, 2011
This is version 73 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program