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O05512

- MANB1_BACSU

UniProt

O05512 - MANB1_BACSU

Protein

Mannan endo-1,4-beta-mannosidase

Gene

gmuG

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 2 (07 Jul 2009)
      Previous versions | rss
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    Functioni

    Seems to be involved in the degradation of glucomannan.1 Publication

    Catalytic activityi

    Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.

    GO - Molecular functioni

    1. cellulase activity Source: InterPro
    2. mannan endo-1,4-beta-mannosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. polysaccharide catabolic process Source: UniProtKB-KW
    2. substituted mannan metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation

    Enzyme and pathway databases

    BioCyciBSUB:BSU05880-MONOMER.

    Protein family/group databases

    CAZyiGH26. Glycoside Hydrolase Family 26.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mannan endo-1,4-beta-mannosidase (EC:3.2.1.78)
    Alternative name(s):
    1,4-beta-D-mannan mannanohydrolase
    Beta-mannanase
    Glucomannan utilization protein G
    Gene namesi
    Name:gmuG
    Synonyms:ydhT
    Ordered Locus Names:BSU05880
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU05880. [Micado]

    Subcellular locationi

    Secreted Curated

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 26261 PublicationAdd
    BLAST
    Chaini27 – 362336Mannan endo-1,4-beta-mannosidasePRO_0000360866Add
    BLAST

    Proteomic databases

    PaxDbiO05512.

    Expressioni

    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.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU05880.

    Structurei

    Secondary structure

    1
    362
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi38 – 4912
    Helixi50 – 523
    Beta strandi53 – 564
    Beta strandi61 – 666
    Turni67 – 704
    Helixi74 – 8310
    Beta strandi88 – 969
    Helixi104 – 1074
    Helixi113 – 1219
    Beta strandi125 – 1317
    Beta strandi137 – 1393
    Helixi148 – 1558
    Helixi160 – 18021
    Turni181 – 1833
    Beta strandi186 – 1894
    Beta strandi196 – 1994
    Helixi211 – 22919
    Beta strandi236 – 2416
    Turni250 – 2534
    Turni257 – 2593
    Beta strandi261 – 27010
    Helixi272 – 2743
    Helixi278 – 2825
    Beta strandi288 – 29710
    Helixi304 – 31411
    Beta strandi318 – 3236
    Helixi326 – 3283
    Helixi330 – 3323
    Helixi336 – 3416
    Beta strandi351 – 3533

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WHKX-ray1.70A27-362[»]
    3CBWX-ray1.27A/B21-362[»]
    ProteinModelPortaliO05512.
    SMRiO05512. Positions 27-362.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO05512.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 26 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4124.
    HOGENOMiHOG000009206.
    KOiK01218.
    OrthoDBiEOG6GXTPF.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR022790. EndoGluc_H/Glyco_hydro_26.
    IPR000805. Glyco_hydro_26.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR016714. Mannan-1_4-b-mannosidase.
    [Graphical view]
    PfamiPF02156. Glyco_hydro_26. 1 hit.
    [Graphical view]
    PIRSFiPIRSF018168. Mannan-1_4-beta-mannosidase. 1 hit.
    PRINTSiPR00739. GLHYDRLASE26.
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O05512-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFKKHTISLL IIFLLASAVL AKPIEAHTVS PVNPNAQQTT KTVMNWLAHL    50
    PNRTENRVLS GAFGGYSHDT FSMAEADRIR SATGQSPAIY GCDYARGWLE 100
    TANIEDSIDV SCNGDLMSYW KNGGIPQISL HLANPAFQSG HFKTPITNDQ 150
    YKKILDSSTV EGKRLNAMLS KIADGLQELE NQGVPVLFRP LHEMNGEWFW 200
    WGLTSYNQKD NERISLYKQL YKKIYHYMTD TRGLDHLIWV YSPDANRDFK 250
    TDFYPGASYV DIVGLDAYFQ DAYSINGYDQ LTALNKPFAF TEVGPQTANG 300
    SFDYSLFINA IKQKYPKTIY FLAWNDEWSA AVNKGASALY HDSWTLNKGE 350
    IWNGDSLTPI VE 362
    Length:362
    Mass (Da):40,892
    Last modified:July 7, 2009 - v2
    Checksum:iC7E1D527AA001B14
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti153 – 1531K → N in BAA19712. (PubMed:9202461)Curated
    Sequence conflicti158 – 1603STV → ATA in BAA19712. (PubMed:9202461)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D88802 Genomic DNA. Translation: BAA19712.1.
    AL009126 Genomic DNA. Translation: CAB12407.2.
    PIRiH69785.
    RefSeqiNP_388469.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB12407; CAB12407; BSU05880.
    GeneIDi938034.
    KEGGibsu:BSU05880.
    PATRICi18972792. VBIBacSub10457_0617.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D88802 Genomic DNA. Translation: BAA19712.1 .
    AL009126 Genomic DNA. Translation: CAB12407.2 .
    PIRi H69785.
    RefSeqi NP_388469.2. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WHK X-ray 1.70 A 27-362 [» ]
    3CBW X-ray 1.27 A/B 21-362 [» ]
    ProteinModelPortali O05512.
    SMRi O05512. Positions 27-362.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU05880.

    Protein family/group databases

    CAZyi GH26. Glycoside Hydrolase Family 26.

    Proteomic databases

    PaxDbi O05512.

    Protocols and materials databases

    DNASUi 938034.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB12407 ; CAB12407 ; BSU05880 .
    GeneIDi 938034.
    KEGGi bsu:BSU05880.
    PATRICi 18972792. VBIBacSub10457_0617.

    Organism-specific databases

    GenoListi BSU05880. [Micado ]

    Phylogenomic databases

    eggNOGi COG4124.
    HOGENOMi HOG000009206.
    KOi K01218.
    OrthoDBi EOG6GXTPF.

    Enzyme and pathway databases

    BioCyci BSUB:BSU05880-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei O05512.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR022790. EndoGluc_H/Glyco_hydro_26.
    IPR000805. Glyco_hydro_26.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR016714. Mannan-1_4-b-mannosidase.
    [Graphical view ]
    Pfami PF02156. Glyco_hydro_26. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF018168. Mannan-1_4-beta-mannosidase. 1 hit.
    PRINTSi PR00739. GLHYDRLASE26.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    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. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 153; 158 AND 160.
    4. "Proteome analysis of Bacillus subtilis extracellular proteins: a two-dimensional protein electrophoretic study."
      Hirose I., Sano K., Shioda I., Kumano M., Nakamura K., Yamane K.
      Microbiology 146:65-75(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-37.
      Strain: 168.
    5. "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, FUNCTION IN GLUCOMANNAN UTILIZATION.
      Strain: 168.

    Entry informationi

    Entry nameiMANB1_BACSU
    AccessioniPrimary (citable) accession number: O05512
    Secondary accession number(s): Q797D6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 20, 2009
    Last sequence update: July 7, 2009
    Last modified: October 1, 2014
    This is version 85 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3