Mannan endo-1,4-beta-mannosidase precursor

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot O05512 (MANB1_BACSU)

Last modified February 9, 2010. Version 54. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Mannan endo-1,4-beta-mannosidase
    EC=3.2.1.78
Alternative name(s):
    Beta-mannanase
    1,4-beta-D-mannan mannanohydrolase
    Glucomannan utilization protein G

Gene names

Name:	gmuG
Synonyms:	ydhT
Ordered Locus Names:	BSU05880

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Hide | Top

Protein attributes

Sequence length	362 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

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.

Hide | Top

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW substituted mannan metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro mannan endo-1,4-beta-mannosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

Ref.4

Chain

27 – 362

336

Mannan endo-1,4-beta-mannosidase

PRO_0000360866

Experimental info

Sequence conflict

153

K → N in BAA19712. Ref.1

Sequence conflict

158 – 160

STV → ATA in BAA19712. Ref.1

Secondary structure

362

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

O05512-1 [UniParc].

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

FASTA

362

40,892

        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

Hide | Top

References

	« Hide 'large scale' referencesShow '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: 9202461] [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. Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [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: 19383706] [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: 10658653] [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: 18177310] [Abstract] Cited for: INDUCTION, FUNCTION IN GLUCOMANNAN UTILIZATION. Strain: 168.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D88802 Genomic DNA. Translation: BAA19712.1.
AL009126 Genomic DNA. Translation: CAB12407.2.

PIR

H69785.

RefSeq

NP_388469.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2WHK	X-ray	1.70	A	27-362	[»]
3CBW	X-ray	1.27	A/B	20-362	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH26. Glycoside Hydrolase Family 26.

Genome annotation databases

GeneID

938034.

GenomeReviews

Gene locus BSU05880 in contig AL009126_GR.

KEGG

bsu:BSU05880.

NMPDR

fig|224308.1.peg.588.

Organism-specific databases

SubtiList

BG12197. gmuG. [Micado]

CMR

Search...

Phylogenomic databases

HOGENOM

HBG338461.

Enzyme and pathway databases

BioCyc

SUBTI:BSU05880-MONOMER.

Family and domain databases

InterPro

IPR000805. Glyco_hydro_26.
IPR017853. Glyco_hydro_catalytic_core.
IPR013781. Glyco_hydro_sg_catalytic.
IPR016714. Mannan-1_4-b-mannosidase.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

PIRSF

PIRSF018168. Mannan-1_4-beta-mannosidase. 1 hit.

PRINTS

PR00739. GLHYDRLASE26.

ProtoNet

Search...

Hide | Top

Entry information

Entry name

MANB1_BACSU

Accession

Primary (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:	February 9, 2010
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top