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Protein

6-phospho-beta-glucosidase GmuD

Gene

gmuD

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

Functioni

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.2 Publications

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 sitei170 – 1701Proton donorSequence Analysis
Active sitei368 – 3681NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

  1. 6-phospho-beta-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

BioCyciBSUB:BSU05840-MONOMER.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:gmuD
Synonyms:bglD, ydhP
Ordered Locus Names:BSU05840
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU05840. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4654656-phospho-beta-glucosidase GmuDPRO_0000371418Add
BLAST

Proteomic databases

PaxDbiO05508.

Expressioni

Developmental stagei

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.1 Publication

Inductioni

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.2 Publications

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU05840.

Structurei

3D structure databases

ProteinModelPortaliO05508.
SMRiO05508. Positions 6-465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family.Curated

Phylogenomic databases

eggNOGiCOG2723.
HOGENOMiHOG000088632.
InParanoidiO05508.
KOiK01223.
OMAiDVAIGWF.
OrthoDBiEOG60658J.
PhylomeDBiO05508.

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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O05508-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHTEQYRFP KDFWWGSSAS ATQMEGAADR DGKGQNIWDY WFEKEPHRFF
60 70 80 90 100
DHVGPADTSQ FYDNYKEDIR LMKELGHNSF RMSISWSRLI PNGTGEINDK
110 120 130 140 150
AADFYNNVID ELIANGIEPF VNLFHFDMPM ALQKIGGWVN RETVDAYENY
160 170 180 190 200
ARTCFRLFGG RVKKWFTHNE PIVPVEGGYL YDFHYPNKVD FKEAVQVGFH
210 220 230 240 250
TMLSSARAIQ AYREMKQDGK IGIILNLTPS YPRSSHPADV KAGEIADAFF
260 270 280 290 300
NRSFLDPSVK GEFPKELVDI LKHEGFMPDY NAEDLDIIKK NTVDLLGVNY
310 320 330 340 350
YQPRRVKAKE HLPNPDAPFL PDRYFDPYVM PGRKMNPHRG WEIYEKGVYD
360 370 380 390 400
ILINLKENYG NIECFISENG MGVEGEERFR DEQGIIQDDY RIEFIKEHLK
410 420 430 440 450
WIHRAIQEGS NVKGYHLWTF MDNWSWTNAY KNRYGFVSVN LEKDGERTVK
460
KSGKWFKEVA EHSGF
Length:465
Mass (Da):54,334
Last modified:July 1, 1997 - v1
Checksum:i9DD069BF2151D590
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88802 Genomic DNA. Translation: BAA19708.1.
AL009126 Genomic DNA. Translation: CAB12403.1.
PIRiD69785.
RefSeqiNP_388465.1. NC_000964.3.
WP_003243625.1. NZ_JNCM01000031.1.

Genome annotation databases

EnsemblBacteriaiCAB12403; CAB12403; BSU05840.
GeneIDi939872.
KEGGibsu:BSU05840.
PATRICi18972784. VBIBacSub10457_0613.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88802 Genomic DNA. Translation: BAA19708.1.
AL009126 Genomic DNA. Translation: CAB12403.1.
PIRiD69785.
RefSeqiNP_388465.1. NC_000964.3.
WP_003243625.1. NZ_JNCM01000031.1.

3D structure databases

ProteinModelPortaliO05508.
SMRiO05508. Positions 6-465.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU05840.

Protein family/group databases

CAZyiGH1. Glycoside Hydrolase Family 1.

Proteomic databases

PaxDbiO05508.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12403; CAB12403; BSU05840.
GeneIDi939872.
KEGGibsu:BSU05840.
PATRICi18972784. VBIBacSub10457_0613.

Organism-specific databases

GenoListiBSU05840. [Micado]

Phylogenomic databases

eggNOGiCOG2723.
HOGENOMiHOG000088632.
InParanoidiO05508.
KOiK01223.
OMAiDVAIGWF.
OrthoDBiEOG60658J.
PhylomeDBiO05508.

Enzyme and pathway databases

BioCyciBSUB:BSU05840-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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1996) [PubMed] [Europe PMC] [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.
    , 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(1996) [PubMed] [Europe PMC] [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(2003) [PubMed] [Europe PMC] [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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY GLUCOMANNAN, FUNCTION IN GLUCOMANNAN UTILIZATION.
    Strain: 168.

Entry informationi

Entry nameiGMUD_BACSU
AccessioniPrimary (citable) accession number: O05508
Secondary accession number(s): Q797D9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: July 1, 1997
Last modified: January 7, 2015
This is version 90 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.