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P42973 (BGLA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aryl-phospho-beta-D-glucosidase BglA
EC=3.2.1.86
Alternative name(s):
6-phospho-beta-glucosidase
Gene names
Name:bglA
Ordered Locus Names:BSU40110
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the hydrolysis of aryl-phospho-beta-D-glucosides such as 4-methylumbelliferyl-phospho-beta-D-glucopyranoside (MUG-P), phosphoarbutin and phosphosalicin. Plays a major role in the utilization of arbutin or salicin as the sole carbon source. BglA and BglH are the major proteins contributing to hydrolysis of MUG-P by extracts of late-exponential-phase or stationary-phase B.subtilis cells. Ref.4

Catalytic activity

6-phospho-beta-D-glucosyl-(1,4)-D-glucose + H2O = D-glucose + D-glucose 6-phosphate.

Developmental stage

Expressed during stationary-phase and exponential-phase of growth. Ref.4

Induction

Up-regulated by the aryl-beta-D-glucoside salicin. Ref.1 Ref.4

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_function6-phospho-beta-glucosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 479479Aryl-phospho-beta-D-glucosidase BglA
PRO_0000063896

Sites

Active site1761Proton donor Potential
Active site3771Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
P42973 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: FC9FA6131A14257A

FASTA47954,841
        10         20         30         40         50         60 
MGNMPKDFLW GGALAAHQFE GGWNQGGKGP SVVDVMTAGA HGVPRKITDT IEENEFYPNH 

        70         80         90        100        110        120 
EAIDFYHRYK EDIALFAEMG LKCLRTSIGW SRIFPKGDEA EPNEAGLQFY DDVFDELLKH 

       130        140        150        160        170        180 
GIEPVITLSH FEMPLHLARE YGGFRNRKVV DFFVNFAEAC FTRYKDKVKY WMTFNEINNQ 

       190        200        210        220        230        240 
MDVNNPLFLW TNSGVVVGEN ENAKEVMYQT AHHELVASAL AVAKGKDINP EFQIGAMVSH 

       250        260        270        280        290        300 
VPIYPFSSNP EDVMLAEEEM RQRYFFPDVQ VRGYYPSYAL KEFEREGYNI TFEDGDDEIL 

       310        320        330        340        350        360 
RNGTVDYLGF SYYMSTTVKS DVKNDNTGDI VNGGLPNGVE NPYITSSDWG WAIDPTGLRY 

       370        380        390        400        410        420 
TLNRFYDRYQ IPLFIVENGF GAVDTLEEDG KVHDPERIQY LKSHIEALKK AVTYDGVDLI 

       430        440        450        460        470 
GYTPWGIIDI VSFTTGEMKK RYGMIYVDRD NEGNGSMKRY KKDSFEWYKN VIQTNGEEL

« Hide

References

« Hide 'large scale' references
[1]"A Bacillus subtilis bglA gene encoding phospho-beta-glucosidase is inducible and closely linked to a NADH dehydrogenase-encoding gene."
Zhang J., Aronson A.I.
Gene 140:85-90(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
Strain: 168 / JH642.
[2]"Sequence analysis of the 36-kb region between gntZ and trnY genes of Bacillus subtilis genome."
Kasahara Y., Nakai S., Ogasawara N.
DNA Res. 4:155-159(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"Identification of aryl-phospho-beta-D-glucosidases in Bacillus subtilis."
Setlow B., Cabrera-Hernandez A., Cabrera-Martinez R.M., Setlow P.
Arch. Microbiol. 181:60-67(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS AN ARYL-PHOSPHO-BETA-D-GLUCOSIDASE, DEVELOPMENTAL STAGE, INDUCTION.
Strain: 168 / PS832.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L19710 Genomic DNA. Translation: AAA22660.1.
D78193 Genomic DNA. Translation: BAA11270.1.
AL009126 Genomic DNA. Translation: CAB16048.1.
PIRI39953.
RefSeqNP_391891.1. NC_000964.3.

3D structure databases

ProteinModelPortalP42973.
SMRP42973. Positions 1-479.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU40110.

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Proteomic databases

PaxDbP42973.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB16048; CAB16048; BSU40110.
GeneID937718.
KEGGbsu:BSU40110.
PATRIC18980092. VBIBacSub10457_4208.

Organism-specific databases

GenoListBSU40110. [Micado]

Phylogenomic databases

eggNOGCOG2723.
HOGENOMHOG000088631.
KOK01223.
OMAEGTCAYL.
ProtClustDBCLSK884519.

Enzyme and pathway databases

BioCycBSUB:BSU40110-MONOMER.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10353. PTHR10353. 1 hit.
PfamPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSPR00131. GLHYDRLASE1.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBGLA_BACSU
AccessionPrimary (citable) accession number: P42973
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents