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P16699 (MANB_BACMA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 A and B

EC=3.2.1.78
Alternative name(s):
Beta-mannanase
Endo-1,4-mannanase
OrganismBacillus mannanilyticus (strain DSM 16130 / JCM 10596 / AM-001)
Taxonomic identifier1418 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 26 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processsubstituted mannan metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functioncellulase activity

Inferred from electronic annotation. Source: InterPro

mannan endo-1,4-beta-mannosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626
Chain27 – 513487Mannan endo-1,4-beta-mannosidase A
PRO_0000012169
Chain27 – 365339Mannan endo-1,4-beta-mannosidase B
PRO_0000012170

Sequences

Sequence LengthMass (Da)Tools
P16699 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 88D105F622CDB5A8

FASTA51358,430
        10         20         30         40         50         60 
MKVYKKVAFV MAFIMFFSVL PTISMSSEAN GAALSNPNAN QTTKNVYSWL ANLPNKSNKR 

        70         80         90        100        110        120 
VVSGHFGGYS DSTLAWIKQC ARELTGKMPG ILSCDYKNWQ TRLYVADQIS YGCNQELINF 

       130        140        150        160        170        180 
WNQGGLVTIS VHMPNPGFHS GENYKTILPT SQFQNLTNHR TTEGRRWKDM LDKMADGLDE 

       190        200        210        220        230        240 
LQNNGVTVLF RPLHEMNGEW FWWGAEGYNQ FDQTRANAYI SAWRDMYQYF THERKLNNLI 

       250        260        270        280        290        300 
WVYSPDVYRD HVTSYYPGAN YVDIVALDSY HPDPHSLTDQ YNRMIALDKP FAFAEIGPPE 

       310        320        330        340        350        360 
SMAGSFDYSN YIQAIKQKYP RTVYFLAWND KWSPHNNRGA WDLFNDSWVV NRGEIDYGQS 

       370        380        390        400        410        420 
NPATVLYDFE NNTLSWSGCE FTDGGPWTSN EWSANGTQSL KADVVLGNNS YHLQKTVNRN 

       430        440        450        460        470        480 
LSSFKNLEIK VSHSSWGNVG SGMTARVFVK TGSAWRWNAG EFCQFAGKRT TALSIDLTKV 

       490        500        510 
SNLHDVREIG VEYKAPANSN GKTAIYLDHV TVR 

« Hide

References

[1]"Two Bacillus beta-mannanases having different COOH termini are produced in Escherichia coli carrying pMAH5."
Akino T., Kato C., Horikoshi K.
Appl. Environ. Microbiol. 55:3178-3183(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31797 Genomic DNA. Translation: AAA22586.1.
PIRA37219.

3D structure databases

ProteinModelPortalP16699.
SMRP16699. Positions 33-363.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM59. Carbohydrate-Binding Module Family 59.
GH26. Glycoside Hydrolase Family 26.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR022790. EndoGluc_H/Glyco_hydro_26.
IPR008979. Galactose-bd-like.
IPR000805. Glyco_hydro_26.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02156. Glyco_hydro_26. 1 hit.
[Graphical view]
PRINTSPR00739. GLHYDRLASE26.
SUPFAMSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMANB_BACMA
AccessionPrimary (citable) accession number: P16699
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: December 11, 2013
This is version 62 of the entry and version 1 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries