Reviewed, UniProtKB/Swiss-Prot P40740 (BGLH_BACSU)

Names and origin

Protein names

Recommended 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

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	469 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 process	Carbohydrate metabolism
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	6-phospho-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
	Chain	1 – 469	469	Aryl-phospho-beta-D-glucosidase bglH		PRO_0000063873
Sites
	Active site	175	1	Proton donor Potential
	Active site	368	1	Nucleophile By similarity
Experimental info
	Sequence conflict	402	1	A → R in CAA84287. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P40740-1 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 4C0CA25F964C1CC1	FASTA	469	53,289
	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

References

	« Hide 'large scale' referencesShow '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: 7883710] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg.
[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: 7704263] [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. , 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: 9384377] [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: 14652714] [Abstract] Cited for: FUNCTION AS AN ARYL-PHOSPHO-BETA-D-GLUCOSIDASE, DEVELOPMENTAL STAGE, INDUCTION. Strain: 168 / PS832.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z34526 Genomic DNA. Translation: CAA84287.1. D31856 Genomic DNA. Translation: BAA06653.1. D29985 Genomic DNA. Translation: BAA06257.1. AL009126 Genomic DNA. Translation: CAB15962.2.
PIR	H69593.
RefSeq	NP_391805.2.
3D structure databases
HSSP	HSSP built from PDB template 1PBG based on UniProtKB P11546.
ModBase	Search...
Protein family/group databases
CAZy	GH1. Glycoside Hydrolase Family 1.
Genome annotation databases
GeneID	937512.
GenomeReviews	Gene locus BSU39260 in contig AL009126_GR.
KEGG	bsu:BSU39260.
NMPDR	fig|224308.1.peg.3931.
Organism-specific databases
SubtiList	BG10935. bglH. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P40740.
OMA	ANPVNQL.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU3922-MON.
BRENDA	3.2.1.21. 150.
Family and domain databases
InterPro	IPR001360. Glyco_hydro_1. IPR018120. Glyco_hydro_1_AS. IPR013781. Glyco_hydro_sg_catalytic. [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.
PROSITE	PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit. PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BGLH_BACSU

Accession

Primary (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:	November 3, 2009
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)