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O05512 (MANB1_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:gmuG
Synonyms:ydhT
Ordered Locus Names:BSU05880
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Seems to be involved in the degradation of glucomannan. Ref.5

Catalytic activity

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

Subcellular location

Secreted Potential.

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. Ref.5

Sequence similarities

Belongs to the glycosyl hydrolase 26 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.4
Chain27 – 362336Mannan endo-1,4-beta-mannosidase
PRO_0000360866

Experimental info

Sequence conflict1531K → N in BAA19712. Ref.1
Sequence conflict158 – 1603STV → ATA in BAA19712. Ref.1

Secondary structure

......................................................... 362
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O05512 [UniParc].

Last modified July 7, 2009. Version 2.
Checksum: C7E1D527AA001B14

FASTA36240,892
        10         20         30         40         50         60 
MFKKHTISLL IIFLLASAVL AKPIEAHTVS PVNPNAQQTT KTVMNWLAHL PNRTENRVLS 

        70         80         90        100        110        120 
GAFGGYSHDT FSMAEADRIR SATGQSPAIY GCDYARGWLE TANIEDSIDV SCNGDLMSYW 

       130        140        150        160        170        180 
KNGGIPQISL HLANPAFQSG HFKTPITNDQ YKKILDSSTV EGKRLNAMLS KIADGLQELE 

       190        200        210        220        230        240 
NQGVPVLFRP LHEMNGEWFW WGLTSYNQKD NERISLYKQL YKKIYHYMTD TRGLDHLIWV 

       250        260        270        280        290        300 
YSPDANRDFK TDFYPGASYV DIVGLDAYFQ DAYSINGYDQ LTALNKPFAF TEVGPQTANG 

       310        320        330        340        350        360 
SFDYSLFINA IKQKYPKTIY FLAWNDEWSA AVNKGASALY HDSWTLNKGE IWNGDSLTPI 


VE 

« Hide

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] [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. 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] [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D88802 Genomic DNA. Translation: BAA19712.1.
AL009126 Genomic DNA. Translation: CAB12407.2.
PIRH69785.
RefSeqNP_388469.2. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WHKX-ray1.70A27-362[»]
3CBWX-ray1.27A/B20-362[»]
ProteinModelPortalO05512.
SMRO05512. Positions 27-362.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU05880.

Protein family/group databases

CAZyGH26. Glycoside Hydrolase Family 26.

Proteomic databases

PaxDbO05512.

Protocols and materials databases

DNASU938034.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12407; CAB12407; BSU05880.
GeneID938034.
KEGGbsu:BSU05880.
PATRIC18972792. VBIBacSub10457_0617.

Organism-specific databases

GenoListBSU05880. [Micado]

Phylogenomic databases

eggNOGCOG4124.
HOGENOMHOG000009206.
KOK01218.
OrthoDBEOG6GXTPF.
ProtClustDBCLSK886796.

Enzyme and pathway databases

BioCycBSUB:BSU05880-MONOMER.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR022790. 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]
PfamPF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
PIRSFPIRSF018168. Mannan-1_4-beta-mannosidase. 1 hit.
PRINTSPR00739. GLHYDRLASE26.
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO05512.

Entry information

Entry nameMANB1_BACSU
AccessionPrimary (citable) accession number: O05512
Secondary accession number(s): Q797D6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: July 7, 2009
Last modified: November 13, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Bacillus subtilis

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