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O05508

- GMUD_BACSU

UniProt

O05508 - GMUD_BACSU

Protein

6-phospho-beta-glucosidase GmuD

Gene

gmuD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    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

    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: 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.
    KOiK01223.
    OMAiWIPLNEP.
    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

    MAHTEQYRFP KDFWWGSSAS ATQMEGAADR DGKGQNIWDY WFEKEPHRFF    50
    DHVGPADTSQ FYDNYKEDIR LMKELGHNSF RMSISWSRLI PNGTGEINDK 100
    AADFYNNVID ELIANGIEPF VNLFHFDMPM ALQKIGGWVN RETVDAYENY 150
    ARTCFRLFGG RVKKWFTHNE PIVPVEGGYL YDFHYPNKVD FKEAVQVGFH 200
    TMLSSARAIQ AYREMKQDGK IGIILNLTPS YPRSSHPADV KAGEIADAFF 250
    NRSFLDPSVK GEFPKELVDI LKHEGFMPDY NAEDLDIIKK NTVDLLGVNY 300
    YQPRRVKAKE HLPNPDAPFL PDRYFDPYVM PGRKMNPHRG WEIYEKGVYD 350
    ILINLKENYG NIECFISENG MGVEGEERFR DEQGIIQDDY RIEFIKEHLK 400
    WIHRAIQEGS NVKGYHLWTF MDNWSWTNAY KNRYGFVSVN LEKDGERTVK 450
    KSGKWFKEVA EHSGF 465
    Length:465
    Mass (Da):54,334
    Last modified:July 1, 1997 - v1
    Checksum:i9DD069BF2151D590
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_CM000487.1.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D88802 Genomic DNA. Translation: BAA19708.1 .
    AL009126 Genomic DNA. Translation: CAB12403.1 .
    PIRi D69785.
    RefSeqi NP_388465.1. NC_000964.3.
    WP_003243625.1. NZ_CM000487.1.

    3D structure databases

    ProteinModelPortali O05508.
    SMRi O05508. Positions 6-465.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU05840.

    Protein family/group databases

    CAZyi GH1. Glycoside Hydrolase Family 1.

    Proteomic databases

    PaxDbi O05508.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB12403 ; CAB12403 ; BSU05840 .
    GeneIDi 939872.
    KEGGi bsu:BSU05840.
    PATRICi 18972784. VBIBacSub10457_0613.

    Organism-specific databases

    GenoListi BSU05840. [Micado ]

    Phylogenomic databases

    eggNOGi COG2723.
    HOGENOMi HOG000088632.
    KOi K01223.
    OMAi WIPLNEP.
    OrthoDBi EOG60658J.
    PhylomeDBi O05508.

    Enzyme and pathway databases

    BioCyci BSUB:BSU05840-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR001360. Glyco_hydro_1.
    IPR018120. Glyco_hydro_1_AS.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10353. PTHR10353. 1 hit.
    Pfami PF00232. Glyco_hydro_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00131. GLHYDRLASE1.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [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(1997) [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(2004) [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(2008) [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: October 1, 2014
    This is version 88 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