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Protein

Aryl-phospho-beta-D-glucosidase BglA

Gene

bglA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei176 – 1761Proton donorSequence Analysis
Active sitei377 – 3771NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BioCyciBSUB:BSU40110-MONOMER.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Recommended name:
Aryl-phospho-beta-D-glucosidase BglA (EC:3.2.1.86)
Alternative name(s):
6-phospho-beta-glucosidase
Gene namesi
Name:bglA
Ordered Locus Names:BSU40110
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU40110. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 479479Aryl-phospho-beta-D-glucosidase BglAPRO_0000063896Add
BLAST

Proteomic databases

PaxDbiP42973.

Expressioni

Developmental stagei

Expressed during stationary-phase and exponential-phase of growth.1 Publication

Inductioni

Up-regulated by the aryl-beta-D-glucoside salicin.2 Publications

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100021631.

Structurei

3D structure databases

ProteinModelPortaliP42973.
SMRiP42973. Positions 1-479.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family.Curated

Phylogenomic databases

eggNOGiCOG2723.
HOGENOMiHOG000088631.
InParanoidiP42973.
KOiK01223.
OMAiMRGYYPA.
OrthoDBiEOG6F81PM.
PhylomeDBiP42973.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
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.
PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42973-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNMPKDFLW GGALAAHQFE GGWNQGGKGP SVVDVMTAGA HGVPRKITDT
60 70 80 90 100
IEENEFYPNH EAIDFYHRYK EDIALFAEMG LKCLRTSIGW SRIFPKGDEA
110 120 130 140 150
EPNEAGLQFY DDVFDELLKH GIEPVITLSH FEMPLHLARE YGGFRNRKVV
160 170 180 190 200
DFFVNFAEAC FTRYKDKVKY WMTFNEINNQ MDVNNPLFLW TNSGVVVGEN
210 220 230 240 250
ENAKEVMYQT AHHELVASAL AVAKGKDINP EFQIGAMVSH VPIYPFSSNP
260 270 280 290 300
EDVMLAEEEM RQRYFFPDVQ VRGYYPSYAL KEFEREGYNI TFEDGDDEIL
310 320 330 340 350
RNGTVDYLGF SYYMSTTVKS DVKNDNTGDI VNGGLPNGVE NPYITSSDWG
360 370 380 390 400
WAIDPTGLRY TLNRFYDRYQ IPLFIVENGF GAVDTLEEDG KVHDPERIQY
410 420 430 440 450
LKSHIEALKK AVTYDGVDLI GYTPWGIIDI VSFTTGEMKK RYGMIYVDRD
460 470
NEGNGSMKRY KKDSFEWYKN VIQTNGEEL
Length:479
Mass (Da):54,841
Last modified:November 1, 1995 - v1
Checksum:iFC9FA6131A14257A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19710 Genomic DNA. Translation: AAA22660.1.
D78193 Genomic DNA. Translation: BAA11270.1.
AL009126 Genomic DNA. Translation: CAB16048.1.
PIRiI39953.
RefSeqiNP_391891.1. NC_000964.3.
WP_003226994.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB16048; CAB16048; BSU40110.
GeneIDi937718.
KEGGibsu:BSU40110.
PATRICi18980092. VBIBacSub10457_4208.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19710 Genomic DNA. Translation: AAA22660.1.
D78193 Genomic DNA. Translation: BAA11270.1.
AL009126 Genomic DNA. Translation: CAB16048.1.
PIRiI39953.
RefSeqiNP_391891.1. NC_000964.3.
WP_003226994.1. NZ_JNCM01000034.1.

3D structure databases

ProteinModelPortaliP42973.
SMRiP42973. Positions 1-479.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100021631.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Proteomic databases

PaxDbiP42973.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB16048; CAB16048; BSU40110.
GeneIDi937718.
KEGGibsu:BSU40110.
PATRICi18980092. VBIBacSub10457_4208.

Organism-specific databases

GenoListiBSU40110. [Micado]

Phylogenomic databases

eggNOGiCOG2723.
HOGENOMiHOG000088631.
InParanoidiP42973.
KOiK01223.
OMAiMRGYYPA.
OrthoDBiEOG6F81PM.
PhylomeDBiP42973.

Enzyme and pathway databases

BioCyciBSUB:BSU40110-MONOMER.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
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.
PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiBGLA_BACSU
AccessioniPrimary (citable) accession number: P42973
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 22, 2015
This is version 105 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

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.