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P40740 (BGLH_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 98. 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 BglH
EC=3.2.1.86
Alternative name(s):
6-phospho-beta-glucosidase
Gene names
Name:bglH
Ordered Locus Names:BSU39260
ORF Names:N17D
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length469 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

Significantly expressed throughout all stages of growth or development. Ref.4

Induction

Highly up-regulated by aryl-beta-D-glucosides such as salicin or 4-methylumbelliferyl-beta-D-glucopyranoside (MUG). 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 – 469469Aryl-phospho-beta-D-glucosidase BglH
PRO_0000063873

Sites

Active site1751Proton donor Potential
Active site3681Nucleophile By similarity

Experimental info

Sequence conflict4021A → R in CAA84287. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P40740 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 4C0CA25F964C1CC1

FASTA46953,289
        10         20         30         40         50         60 
MSSNEKRFPE GFLWGGAVAA NQVEGAYNEG GKGLSTADVS PNGIMSPFDE SMTSLNLYHN 

        70         80         90        100        110        120 
GIDFYHRYKE DIALFAEMGF KAFRTSIAWT RIFPNGDEEE PNEEGLRFYD DLFDELLKHH 

       130        140        150        160        170        180 
IEPVVTISHY EMPLGLVKNY GGWKNRKVIE FYERYAKTVF KRYQHKVKYW MTFNEINVVL 

       190        200        210        220        230        240 
HAPFTGGGLV FEEGENKLNA MYQAAHHQFV ASALAVKAGH DIIPDSKIGC MIAATTTYPM 

       250        260        270        280        290        300 
TSKPEDVFAA MENERKTLFF SDVQARGAYP GYMKRYLAEN NIEIEMAEGD EELLKEHTVD 

       310        320        330        340        350        360 
YIGFSYYMSM AASTDPEELA KSGGNLLGGV KNPYLKSSEW GWQIDPKGLR ITLNTLYDRY 

       370        380        390        400        410        420 
QKPLFIVENG LGAVDKVEED GTIQDDYRIN YLRDHLIEAR EAIADGVELI GYTSWGPIDL 

       430        440        450        460 
VSASTAEMKK RYGFIYVDRD NEGNGTFNRI KKKSFNWYQQ VIATNGESL

« Hide

References

« Hide 'large scale' references
[1]"New beta-glucoside (bgl) genes in Bacillus subtilis: the bglP gene product has both transport and regulatory functions similar to those of BglF, its Escherichia coli homolog."
Le Coq D., Lindner C., Krueger S., Steinmetz M., Stuelke J.
J. Bacteriol. 177:1527-1535(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[2]"Cloning and sequencing of a 29 kb region of the Bacillus subtilis genome containing the hut and wapA loci."
Yoshida K., Sano H., Seki S., Oda M., Fujimura M., Fujita Y.
Microbiology 141:337-343(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / BGSC1A1.
[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		Z34526 Genomic DNA. Translation: CAA84287.1.
D31856 Genomic DNA. Translation: BAA06653.1.
D29985 Genomic DNA. Translation: BAA06257.1.
AL009126 Genomic DNA. Translation: CAB15962.2.
PIRH69593.
RefSeqNP_391805.2. NC_000964.3.

3D structure databases

ProteinModelPortalP40740.
SMRP40740. Positions 1-469.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU39260.

Protein family/group databases

CAZyGH1. Glycoside Hydrolase Family 1.

Proteomic databases

PaxDbP40740.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15962; CAB15962; BSU39260.
GeneID937512.
KEGGbsu:BSU39260.
PATRIC18979912. VBIBacSub10457_4118.

Organism-specific databases

GenoListBSU39260. [Micado]

Phylogenomic databases

eggNOGCOG2723.
HOGENOMHOG000088631.
KOK01223.
OMAQDDYRIN.
ProtClustDBCLSK928157.

Enzyme and pathway databases

BioCycBSUB:BSU39260-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 nameBGLH_BACSU
AccessionPrimary (citable) accession number: P40740
Secondary accession number(s): O32287
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 30, 2000
Last modified: May 1, 2013
This is version 98 of the entry and version 2 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