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Reviewed, UniProtKB/Swiss-Prot O05508 (GMUD_BACSU)

Last modified November 3, 2009. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    6-phospho-beta-glucosidase gmuD
    EC=3.2.1.86
Alternative name(s):
    Aryl-phospho-beta-D-glucosidase bglD
    Glucomannan utilization protein D
Gene names
Name: gmuD
Synonyms: bglD, ydhP
Ordered Locus Names: BSU05840
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Phospho-beta-D-glucosidase that seems to be involved in the degradation of glucomannan. Is also capable of hydrolyzing aryl-phospho-beta-D-glucosides, although very weakly, and plays only a minor role, if any, in the degradation of these substrates in vivo. Ref.3 Ref.4

Catalytic activity

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

Developmental stage

Expressed at only a very low level in exponential-phase cells and germinating spores, but is expressed at a higher levels upon entry into the stationary phase of growth. Ref.3

Induction

Up-regulated by konjac glucomannan and by cellobiose and mannobiose, the possible degradation products of glucomannan. Repressed by glucose via the carbon catabolite repression system. Also repressed by gmuR. Is not induced by aryl-beta-D-glucosides such as arbutin or salicin. Ref.3 Ref.4

Sequence similarities

Belongs to the glycosyl hydrolase 1 family.

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Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpolysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function6-phospho-beta-glucosidase activity

Inferred from electronic annotation. Source: EC

cation binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4654656-phospho-beta-glucosidase gmuD
PRO_0000371418

Sites

Active site1701Proton donor Potential
Active site3681Nucleophile By similarity

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Sequences

Sequence LengthMass (Da)Tools
O05508-1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 9DD069BF2151D590

FASTA46554,334
        10         20         30         40         50         60 
MAHTEQYRFP KDFWWGSSAS ATQMEGAADR DGKGQNIWDY WFEKEPHRFF DHVGPADTSQ 

        70         80         90        100        110        120 
FYDNYKEDIR LMKELGHNSF RMSISWSRLI PNGTGEINDK AADFYNNVID ELIANGIEPF 

       130        140        150        160        170        180 
VNLFHFDMPM ALQKIGGWVN RETVDAYENY ARTCFRLFGG RVKKWFTHNE PIVPVEGGYL 

       190        200        210        220        230        240 
YDFHYPNKVD FKEAVQVGFH TMLSSARAIQ AYREMKQDGK IGIILNLTPS YPRSSHPADV 

       250        260        270        280        290        300 
KAGEIADAFF NRSFLDPSVK GEFPKELVDI LKHEGFMPDY NAEDLDIIKK NTVDLLGVNY 

       310        320        330        340        350        360 
YQPRRVKAKE HLPNPDAPFL PDRYFDPYVM PGRKMNPHRG WEIYEKGVYD ILINLKENYG 

       370        380        390        400        410        420 
NIECFISENG MGVEGEERFR DEQGIIQDDY RIEFIKEHLK WIHRAIQEGS NVKGYHLWTF 

       430        440        450        460 
MDNWSWTNAY KNRYGFVSVN LEKDGERTVK KSGKWFKEVA EHSGF

« Hide

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References

« Hide 'large scale' references
[1]"Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the Bacillus subtilis chromosome."
Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y., Ogasawara N.
Microbiology 143:1861-1866(1997) [PubMed: 9202461] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / JH642.
[2]"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: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"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.
[4]"Glucomannan utilization operon of Bacillus subtilis."
Sadaie Y., Nakadate H., Fukui R., Yee L.M., Asai K.
FEMS Microbiol. Lett. 279:103-109(2008) [PubMed: 18177310] [Abstract]
Cited for: INDUCTION BY GLUCOMANNAN, FUNCTION IN GLUCOMANNAN UTILIZATION.
Strain: 168.

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Cross-references

Sequence databases

D88802 Genomic DNA. Translation: BAA19708.1.
AL009126 Genomic DNA. Translation: CAB12403.1.
PIRD69785.
RefSeqNP_388465.1.

3D structure databases

HSSPHSSP built from PDB template 1PBG based on UniProtKB P11546.
ModBaseSearch...

Genome annotation databases

GeneID939872.
GenomeReviewsGene locus BSU05840 in contig AL009126_GR.
KEGGbsu:BSU05840.
NMPDRfig|224308.1.peg.584.

Organism-specific databases

SubtiListBG12193. gmuD. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMO05508.
OMAHTAFRTS.

Enzyme and pathway databases

BioCycBSUB224308:BSU0584-MON.

Family and domain databases

InterProIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHERPTHR10353. Glyco_hydro_1. 1 hit.
PfamPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSPR00131. GLHYDRLASE1.
PROSITEPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameGMUD_BACSU
AccessionPrimary (citable) accession number: O05508
Secondary accession number(s): Q797D9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: July 1, 1997
Last modified: November 3, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents