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Q0CCA0 (MANBB_ASPTN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Beta-mannosidase B

EC=3.2.1.25
Alternative name(s):
Mannanase B
Short name=Mannase B
Gene names
Name:mndB
ORF Names:ATEG_08684
OrganismAspergillus terreus (strain NIH 2624 / FGSC A1156) [Complete proteome]
Taxonomic identifier341663 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length843 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of beta-mannosidic oligosaccharides of various complexity and length. Prefers manobiose over mannotriose and has no activity against polymeric mannan. Is also severly restricetd by galactosyl substitutions at the +1 subsite By similarity.

Catalytic activity

Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.

Pathway

Glycan metabolism; N-glycan degradation.

Miscellaneous

In contrast to clade A beta-mannosidases, which are likely secreted, clade B proteins appear to be intracellular By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 2 family. Beta-mannosidase B subfamily.

Sequence caution

The sequence EAU30816.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processmannan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-mannosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 843843Beta-mannosidase B
PRO_0000394657

Sites

Active site4301Proton donor By similarity

Amino acid modifications

Glycosylation7211N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q0CCA0 [UniParc].

Last modified June 15, 2010. Version 2.
Checksum: EE4DB1B4648C2506

FASTA84396,245
        10         20         30         40         50         60 
MASFFQQSLA TGWSFKDAED NSAEAWMPVA QVPSVVHQDL IANNKLQDPY VGFRELDARW 

        70         80         90        100        110        120 
VNEKSWTYRT VFQKPAVPAG SSVILAFDGL DTFAKVKLNG NVILESNNMF LAHRIDVTKA 

       130        140        150        160        170        180 
LGADGDHVLE IDFDCAMLRA RELRAKDPQH KWVGFNGDPA RMGVRKAQYH WGWDWGPVLM 

       190        200        210        220        230        240 
TAGIWRDVRL EVYTARVADL WTETDLAVDH HAAQISAFAQ VEGAISSSKV NFILSLHGQE 

       250        260        270        280        290        300 
VARAVAEPQD QVAKVAFDVQ QPSLWWPNGY GDPTLYEISA TLDQDGATVH QISKKIGIRT 

       310        320        330        340        350        360 
AEVVQRPDKH GKSFFFRING VDIFCGGSCW IPADNLLPSI SAERYRKWIE LMVHGRQVMI 

       370        380        390        400        410        420 
RVWGGGCYED DSFYQACDEL GVMVWQDFMF GCGNYPTWPE MLESVEKEAI YNVRRLRHHP 

       430        440        450        460        470        480 
SIVVYVGNNE DYQVQEQQGL TYNFEDKDPQ NWLKSDFPAR YIYEKILPEV VQRYSPSTFY 

       490        500        510        520        530        540 
HPGSPWGDGK ITSDPTVGDM HQWNVWHGTQ EKYQIFDTLG GRFNSEFGME AFPHMSTIEY 

       550        560        570        580        590        600 
FVENEKDKYP QSHVLDFHNK ADGHERRIAT YLVENLRTAT DLETYIYLTQ VVQAETMMFG 

       610        620        630        640        650        660 
YRGWRRQWGD ERHCGGALLW QLNDCWPTIS WAIVDYFLRP KPAFYAVARV LNPIAVGVRR 

       670        680        690        700        710        720 
EHHDWSVTHA QPPKKSKFEL WVASNLQKET RGMVELKFLS VDTGREIRER IVREDVIIVP 

       730        740        750        760        770        780 
NGTTDIIVDG VIDHQEYAEP HVLAARLWVD GKIVARDVDW PQPFKYLDLS GRGLEVKTVS 

       790        800        810        820        830        840 
TSDDQQTLLI SAQKPVKCLV FEERDGVRVS DSAMDIVPGD EQTVTITGLK ADAPPLKYKY 


LGQ 

« Hide

References

« Hide 'large scale' references
[1]"Annotation of the Aspergillus terreus NIH2624 genome."
Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M., Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K. expand/collapse author list , Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J., Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W., Nierman W.C., Milne T., Madden K.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NIH 2624 / FGSC A1156.
[2]"Phylogenetic analysis and substrate specificity of GH2 beta-mannosidases from Aspergillus species."
Reddy S.K., Rosengren A., Klaubauf S., Kulkarni T., Karlsson E.N., de Vries R.P., Stalbrand H.
FEBS Lett. 587:3444-3449(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE MODEL REVISION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476606 Genomic DNA. Translation: EAU30816.1. Sequence problems.
RefSeqXP_001217270.1. XM_001217269.1.

3D structure databases

ProteinModelPortalQ0CCA0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING33178.CADATEAP00006706.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4323103.

Phylogenomic databases

eggNOGCOG3250.
HOGENOMHOG000186861.
OrthoDBEOG7NSB9Q.

Enzyme and pathway databases

UniPathwayUPA00280.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProIPR008979. Galactose-bd-like.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR028369. Mannanase.
[Graphical view]
PANTHERPTHR10066:SF12. PTHR10066:SF12. 1 hit.
PfamPF00703. Glyco_hydro_2. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
SUPFAMSSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMANBB_ASPTN
AccessionPrimary (citable) accession number: Q0CCA0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: March 19, 2014
This is version 44 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries