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Q0CI48 (MANBA_ASPTN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 43. 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 A

EC=3.2.1.25
Alternative name(s):
Mannanase A
Short name=Mannase A
Gene names
Name:mndA
ORF Names:ATEG_06636
OrganismAspergillus terreus (strain NIH 2624 / FGSC A1156) [Complete proteome]
Taxonomic identifier341663 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length932 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Involved in the degradation of polymeric mannan and galactomannan By similarity.

Catalytic activity

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

Pathway

Glycan metabolism; N-glycan degradation.

Subunit structure

Homodimer By similarity.

Subcellular location

Secreted By similarity.

Sequence similarities

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

Sequence caution

The sequence EAU33180.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   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

Signal peptide1 – 1919 Potential
Chain20 – 932913Beta-mannosidase A
PRO_0000394648

Sites

Active site4801Proton donor By similarity

Amino acid modifications

Glycosylation411N-linked (GlcNAc...) Potential
Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation2491N-linked (GlcNAc...) Potential
Glycosylation2611N-linked (GlcNAc...) Potential
Glycosylation2841N-linked (GlcNAc...) Potential
Glycosylation2891N-linked (GlcNAc...) Potential
Glycosylation3181N-linked (GlcNAc...) Potential
Glycosylation3481N-linked (GlcNAc...) Potential
Glycosylation5381N-linked (GlcNAc...) Potential
Glycosylation5511N-linked (GlcNAc...) Potential
Glycosylation6091N-linked (GlcNAc...) Potential
Glycosylation6241N-linked (GlcNAc...) Potential
Glycosylation6321N-linked (GlcNAc...) Potential
Glycosylation6591N-linked (GlcNAc...) Potential
Glycosylation7391N-linked (GlcNAc...) Potential
Glycosylation7911N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q0CI48 [UniParc].

Last modified March 19, 2014. Version 2.
Checksum: 2B1436F3E4E53D88

FASTA932105,189
        10         20         30         40         50         60 
MRVPAQATIA VLASAVSSPL NDPQIYDLGK LGWTLSSPAL NRTVPGHLPS QVHLDLLRAG 

        70         80         90        100        110        120 
VIDDPYHDLN DFNLRWIADA NWTYTSDPIR GLGNNTHSTW LVFEGLDTFA TIKYCDKQIA 

       130        140        150        160        170        180 
STNNQFRQYA FDISEAVKDC TADPVLSLNF GSAPKIVDQI AADPASPQWP FGIQQSYEYP 

       190        200        210        220        230        240 
NRWFMRKEQS DFGWDWGPAF APAGPWKPAY LVQLSSEQNV HVLNTDLDIY RQGQINYLPP 

       250        260        270        280        290        300 
DQTQPWVLNA SIDFFGSLPS NSSMSIAISE TNSGAELTTQ SLRNITILNG SITGVAVLKD 

       310        320        330        340        350        360 
ASPKLWWPYG LGEQNLYNVT ITVSDGVRSL ARVTKRTGFR TIFLNQRNIT DTEIAQGVAP 

       370        380        390        400        410        420 
GAHWNFEVNG HEFYAKGSNL IPPDAFWARV TTTKMARLFD SVVAANQNML RVWSSGAYLP 

       430        440        450        460        470        480 
DFMYDLADER GVLLWSEFEF SDAMYPVDKA FLDNVAAEVV YNVRRVNHHP SLALWAGGNE 

       490        500        510        520        530        540 
IESLILPTIE RSYPDQYAKY VGDYETLYIN LILPLVYENT HSITYSPSST TEGYLDVNLS 

       550        560        570        580        590        600 
AKIVMAERYQ NLTEGHYYGD TDYYNYDTSV AFDFSQYPVG RFANEFGFHS MPSLQSWQQA 

       610        620        630        640        650        660 
VDPEDLHFNS SVIMLRNHHY PAGNLSTHNF HNTSMGMGET TMGVMNYYPV PDKTDPIANF 

       670        680        690        700        710        720 
SAWCHATQLF QADFYKSQIQ FYRRGSGMPE RQLGSLYWQL EDIWQAPSWA GIEYDGRWKV 

       730        740        750        760        770        780 
LHYVARDIYQ PVIVSPFWNS TTRRLDVYVT SDLWEPVSGT VDLAWMDLSG KPIAQNARTP 

       790        800        810        820        830        840 
KTAAFVVGAL NTTKIYSMNI NERALPDPKN SVLILSVQAE GHLPNSNKKS TLTHQGHFTP 

       850        860        870        880        890        900 
VFPKDLMLVD PHLELRYNAK TLTFTVQAKA GVSLYTWLDY PAGVVGYFED NGFVLVPGQK 

       910        920        930 
RDIRFVMQED KTDGNWVQDV TVRSLWDQTT KT 

« 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
CH476602 Genomic DNA. Translation: EAU33180.1. Sequence problems.
RefSeqXP_001215814.1. XM_001215814.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING33178.CADATEAP00009356.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADATEAT00009356; CADATEAP00009356; CADATEAG00009356.
GeneID4321960.

Phylogenomic databases

eggNOGCOG3250.
HOGENOMHOG000216059.
OMACHATQLF.
OrthoDBEOG78D7TH.

Enzyme and pathway databases

UniPathwayUPA00280.

Family and domain databases

InterProIPR006102. Glyco_hydro_2_Ig-like.
[Graphical view]
PfamPF00703. Glyco_hydro_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMANBA_ASPTN
AccessionPrimary (citable) accession number: Q0CI48
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: March 19, 2014
Last modified: July 9, 2014
This is version 43 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