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Protein

Mannan endo-1,4-beta-mannosidase

Gene

gmuG

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

Functioni

Involved in the degradation of glucomannan. Catalyzes the endo hydrolysis of beta-1,4-linked mannan, galactomannan and glucomannan.2 Publications

Catalytic activityi

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

Kineticsi

Kcat is 330 min(-1) for mannanase activity with galactomannan as substrate. Kcat is 350 min(-1) for mannanase activity with glucomannan as substrate.1 Publication

  1. KM=2.7 mg/ml for glucomannan1 Publication
  2. KM=4.5 mg/ml for galactomannan1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei131 – 1311SubstrateBy similarity
    Sitei192 – 1921Plays an important role in maintaining the position of the catalytic nucleophileBy similarity
    Active sitei193 – 1931Proton donorBy similarity
    Binding sitei198 – 1981SubstrateBy similarity
    Binding sitei268 – 2681SubstrateBy similarity
    Active sitei292 – 2921NucleophileBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation

    Enzyme and pathway databases

    BioCyciBSUB:BSU05880-MONOMER.
    BRENDAi3.2.1.78. 658.

    Protein family/group databases

    CAZyiGH26. Glycoside Hydrolase Family 26.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mannan endo-1,4-beta-mannosidase1 Publication (EC:3.2.1.781 Publication)
    Alternative name(s):
    1,4-beta-D-mannan mannanohydrolase1 Publication
    Beta-mannanase1 Publication
    Glucomannan utilization protein G1 Publication
    Gene namesi
    Name:gmuG1 Publication
    Synonyms:ydhT1 Publication
    Ordered Locus Names:BSU05880
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570 Componenti: Chromosome

    Organism-specific databases

    GenoListiBSU05880. [Micado]

    Subcellular locationi

    • Secreted 1 Publication

    GO - Cellular componenti

    Complete GO annotation...

    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

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100003293.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini38 – 349312GH26PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni324 – 3252Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 26 family.PROSITE-ProRule annotationCurated
    Contains 1 GH26 (glycosyl hydrolase family 26) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG4105D3P. Bacteria.
    COG4124. LUCA.
    HOGENOMiHOG000009206.
    InParanoidiO05512.
    KOiK01218.
    OMAiSPAIYGC.
    OrthoDBiEOG6GXTPF.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR000805. Glyco_hydro_26.
    IPR022790. Glyco_hydro_26_dom.
    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.
    PROSITEiPS51764. GH26. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O05512-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MFKKHTISLL IIFLLASAVL AKPIEAHTVS PVNPNAQQTT KTVMNWLAHL
    60 70 80 90 100
    PNRTENRVLS GAFGGYSHDT FSMAEADRIR SATGQSPAIY GCDYARGWLE
    110 120 130 140 150
    TANIEDSIDV SCNGDLMSYW KNGGIPQISL HLANPAFQSG HFKTPITNDQ
    160 170 180 190 200
    YKKILDSSTV EGKRLNAMLS KIADGLQELE NQGVPVLFRP LHEMNGEWFW
    210 220 230 240 250
    WGLTSYNQKD NERISLYKQL YKKIYHYMTD TRGLDHLIWV YSPDANRDFK
    260 270 280 290 300
    TDFYPGASYV DIVGLDAYFQ DAYSINGYDQ LTALNKPFAF TEVGPQTANG
    310 320 330 340 350
    SFDYSLFINA IKQKYPKTIY FLAWNDEWSA AVNKGASALY HDSWTLNKGE
    360
    IWNGDSLTPI VE
    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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D88802 Genomic DNA. Translation: BAA19712.1.
    AL009126 Genomic DNA. Translation: CAB12407.2.
    PIRiH69785.
    RefSeqiNP_388469.2. NC_000964.3.
    WP_003244107.1. NZ_JNCM01000031.1.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D88802 Genomic DNA. Translation: BAA19712.1.
    AL009126 Genomic DNA. Translation: CAB12407.2.
    PIRiH69785.
    RefSeqiNP_388469.2. NC_000964.3.
    WP_003244107.1. NZ_JNCM01000031.1.

    3D structure databases

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

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100003293.

    Protein family/group databases

    CAZyiGH26. Glycoside Hydrolase Family 26.

    Proteomic databases

    PaxDbiO05512.

    Protocols and materials databases

    DNASUi938034.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    GenoListiBSU05880. [Micado]

    Phylogenomic databases

    eggNOGiENOG4105D3P. Bacteria.
    COG4124. LUCA.
    HOGENOMiHOG000009206.
    InParanoidiO05512.
    KOiK01218.
    OMAiSPAIYGC.
    OrthoDBiEOG6GXTPF.

    Enzyme and pathway databases

    BioCyciBSUB:BSU05880-MONOMER.
    BRENDAi3.2.1.78. 658.

    Miscellaneous databases

    EvolutionaryTraceiO05512.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    InterProiIPR000805. Glyco_hydro_26.
    IPR022790. Glyco_hydro_26_dom.
    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.
    PROSITEiPS51764. GH26. 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(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: FUNCTION IN GLUCOMANNAN UTILIZATION, INDUCTION.
      Strain: 168.
    6. "Crystal structure of the YdhT protein from Bacillus subtilis."
      Bonanno J.B., Rutter M., Bain K.T., Iizuka M., Romero R., Smith D., Wasserman S., Sauder J.M., Burley S.K., Almo S.C.
      Submitted (FEB-2008) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.27 ANGSTROMS) OF 21-362, SUBUNIT.
    7. Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 27-362, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.

    Entry informationi

    Entry nameiMANB_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: November 11, 2015
    This is version 94 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

    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 one 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.