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P22073

- BGLA_PAEPO

UniProt

P22073 - BGLA_PAEPO

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Protein
Beta-glucosidase A
Gene
bglA
Organism
Paenibacillus polymyxa (Bacillus polymyxa)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

BglA is intracellular and cleaves cellobiose probably through inorganic phosphate mediated hydrolysis.

Catalytic activityi

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei166 – 1661Proton donor Reviewed prediction
Active sitei352 – 3521Nucleophile By similarity

GO - Molecular functioni

  1. beta-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-glucosidase A (EC:3.2.1.21)
Short name:
BGA
Alternative name(s):
Amygdalase
Beta-D-glucoside glucohydrolase
Cellobiase
Gentiobiase
Gene namesi
Name:bglA
OrganismiPaenibacillus polymyxa (Bacillus polymyxa)
Taxonomic identifieri1406 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448Beta-glucosidase A
PRO_0000063871Add
BLAST

Interactioni

Subunit structurei

Homooctamer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53
Beta strandi11 – 155
Helixi18 – 214
Helixi27 – 293
Helixi34 – 396
Turni42 – 443
Helixi46 – 483
Beta strandi51 – 533
Helixi54 – 563
Helixi57 – 7115
Beta strandi74 – 796
Helixi82 – 854
Beta strandi89 – 913
Helixi95 – 11016
Beta strandi114 – 1229
Helixi126 – 1305
Turni131 – 1344
Helixi138 – 15316
Helixi155 – 1573
Beta strandi160 – 1656
Helixi167 – 1759
Helixi187 – 21125
Beta strandi214 – 2207
Beta strandi226 – 2316
Helixi233 – 24614
Helixi248 – 2569
Helixi261 – 2699
Helixi280 – 2845
Beta strandi289 – 2946
Beta strandi299 – 3035
Turni308 – 3114
Beta strandi312 – 3143
Helixi331 – 3399
Helixi340 – 3434
Beta strandi348 – 3536
Helixi369 – 38719
Beta strandi392 – 3987
Helixi406 – 4116
Beta strandi416 – 4194
Turni421 – 4233
Beta strandi426 – 4283
Helixi430 – 44112
Beta strandi443 – 4453

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BGAX-ray2.40A/B/C/D2-448[»]
1BGGX-ray2.30A/B/C/D1-448[»]
1E4IX-ray2.00A2-448[»]
1TR1X-ray2.20A/B/C/D2-448[»]
1UYQX-ray2.20A2-448[»]
ProteinModelPortaliP22073.
SMRiP22073. Positions 2-448.

Miscellaneous databases

EvolutionaryTraceiP22073.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR017736. Glyco_hydro_1_beta-glucosidase.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10353. PTHR10353. 1 hit.
PfamiPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSiPR00131. GLHYDRLASE1.
SUPFAMiSSF51445. SSF51445. 1 hit.
TIGRFAMsiTIGR03356. BGL. 1 hit.
PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22073-1 [UniParc]FASTAAdd to Basket

« Hide

MTIFQFPQDF MWGTATAAYQ IEGAYQEDGR GLSIWDTFAH TPGKVFNGDN    50
GNVACDSYHR YEEDIRLMKE LGIRTYRFSV SWPRIFPNGD GEVNQEGLDY 100
YHRVVDLLND NGIEPFCTLY HWDLPQALQD AGGWGNRRTI QAFVQFAETM 150
FREFHGKIQH WLTFNEPWCI AFLSNMLGVH APGLTNLQTA IDVGHHLLVA 200
HGLSVRRFRE LGTSGQIGIA PNVSWAVPYS TSEEDKAACA RTISLHSDWF 250
LQPIYQGSYP QFLVDWFAEQ GATVPIQDGD MDIIGEPIDM IGINYYSMSV 300
NRFNPEAGFL QSEEINMGLP VTDIGWPVES RGLYEVLHYL QKYGNIDIYI 350
TENGACINDE VVNGKVQDDR RISYMQQHLV QVHRTIHDGL HVKGYMAWSL 400
LDNFEWAEGY NMRFGMIHVD FRTQVRTPKE SYYWYRNVVS NNWLETRR 448
Length:448
Mass (Da):51,649
Last modified:August 1, 1991 - v1
Checksum:iD971D2E61B6627C1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M60210 Genomic DNA. Translation: AAA22263.1.
PIRiJW0037.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M60210 Genomic DNA. Translation: AAA22263.1 .
PIRi JW0037.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P22073.
SMRi P22073. Positions 2-448.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH1. Glycoside Hydrolase Family 1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P22073.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR017736. Glyco_hydro_1_beta-glucosidase.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
PANTHERi PTHR10353. PTHR10353. 1 hit.
Pfami PF00232. Glyco_hydro_1. 1 hit.
[Graphical view ]
PRINTSi PR00131. GLHYDRLASE1.
SUPFAMi SSF51445. SSF51445. 1 hit.
TIGRFAMsi TIGR03356. BGL. 1 hit.
PROSITEi PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
    Strain: ATCC 842 / DSM 36 / JCM 2507 / NBRC 15309 / NCIMB 8158 / NCTC 10343 / NRRL B-4317 / VKM B-514.

Entry informationi

Entry nameiBGLA_PAEPO
AccessioniPrimary (citable) accession number: P22073
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: October 16, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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