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A1DMT2 (MANBA_NEOFI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 42. 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:NFIA_054490
OrganismNeosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus) [Complete proteome]
Taxonomic identifier331117 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeNeosartorya

Protein attributes

Sequence length930 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.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   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

Signal peptide1 – 2121 Potential
Chain22 – 930909Beta-mannosidase A
PRO_0000394650

Sites

Active site4781Proton donor By similarity

Amino acid modifications

Glycosylation621N-linked (GlcNAc...) Potential
Glycosylation2461N-linked (GlcNAc...) Potential
Glycosylation2811N-linked (GlcNAc...) Potential
Glycosylation3151N-linked (GlcNAc...) Potential
Glycosylation3461N-linked (GlcNAc...) Potential
Glycosylation5361N-linked (GlcNAc...) Potential
Glycosylation6071N-linked (GlcNAc...) Potential
Glycosylation6301N-linked (GlcNAc...) Potential
Glycosylation6571N-linked (GlcNAc...) Potential
Glycosylation7371N-linked (GlcNAc...) Potential
Glycosylation7601N-linked (GlcNAc...) Potential
Glycosylation7821N-linked (GlcNAc...) Potential
Glycosylation7891N-linked (GlcNAc...) Potential
Glycosylation7971N-linked (GlcNAc...) Potential
Glycosylation8231N-linked (GlcNAc...) Potential
Glycosylation9091N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
A1DMT2 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 736EDACC02D252D3

FASTA930104,276
        10         20         30         40         50         60 
MHVKAETVLA LLTPGLPSVV GQHVVDLSGD GWTLSSTALD RTVPGHLPSQ VHLDLFEAGV 

        70         80         90        100        110        120 
INITASMILT FVGLLMPIGR IPATRLKACD LENFESTWLV FDGLDTFTTI TFCDQHVGST 

       130        140        150        160        170        180 
DNQFRQYHFD VSQILKECKQ DPVIRINFGS APSIANAIAK SPDAEEWPPG VQITNEYPNR 

       190        200        210        220        230        240 
WYIRKEQSDF GWDWGPAFAP VGPWKPSYIV QNNHAELYVL NTDLDFYRQG QINYLPPDQS 

       250        260        270        280        290        300 
QPWIVNASID ILGPVPWKPS MSIEIKDAAT GSVLSSGLLQ NVTVSGNSIT GTTTIDGDAP 

       310        320        330        340        350        360 
KLWWPSGMGE QNLYNVTVTV QNDKKKSLAK VTKRTGFRTI FLNQRNITDD QLAQGIAPGA 

       370        380        390        400        410        420 
NWHFEINGHA FYAKGSNIIP PDAFWPRVTQ ARMARLFDAV TAGNQNMLRV WASGAYLHDF 

       430        440        450        460        470        480 
IYDLADEKGI LLWSEFQFSD ALYPVNDAFL ENVAAEVVYN VRRVNHHPSL ALWAGGNEIE 

       490        500        510        520        530        540 
SLMLPMVKRA DPTGYSKYVG EYEKLYISLI LPLVYENTRS ITYSPSSTTE GYLYVNLSAP 

       550        560        570        580        590        600 
VPMAERYSNT TPGSYYGDTD YYNYDTSVSF DYNHYPVGRF ANEFGFHSMP SLQTWQQAVD 

       610        620        630        640        650        660 
PEDLHFNSSV VMLRNHHYTA GGLFTDNFKN SSKGMGEMTM GVEAYYPIPS KSDSVANFSA 

       670        680        690        700        710        720 
WCHATQLFQA DMYKSQIQFY RRGSGMPERQ LGSLYWQLED IWQAPTWAGI EYDGRWKVLH 

       730        740        750        760        770        780 
YVARDIYQPI IVSPFWNYTT GRLEVYVTSD LWEPAQGTVN LTWVDLSGKT IANNAGTPET 

       790        800        810        820        830        840 
VNFTVGALNT TNIYTTNISE LSLPDLKDSI LILSLSGEGR LPNTSSKKAF VHQNHFTPVF 

       850        860        870        880        890        900 
PKDLSLKDPK LEISYSPESR KFTVQATGGV SLYTWLDYPA GAVGYFEENA FVLLPGVQKE 

       910        920        930 
VSFAAQEGNV TDDWVRRVTV QSLWDQKVRD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027698 Genomic DNA. Translation: EAW16103.1.
RefSeqXP_001258000.1. XM_001257999.1.

3D structure databases

ProteinModelPortalA1DMT2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING36630.CADNFIAP00004919.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADNFIAT00005047; CADNFIAP00004919; CADNFIAG00005047.
GeneID4584515.
KEGGnfi:NFIA_054490.

Phylogenomic databases

eggNOGCOG3250.
HOGENOMHOG000216059.
KOK01192.
OMACHATQLF.
OrthoDBEOG78D7TH.

Enzyme and pathway databases

UniPathwayUPA00280.

Family and domain databases

Gene3D2.60.120.260. 2 hits.
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.
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.
[Graphical view]
SUPFAMSSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMANBA_NEOFI
AccessionPrimary (citable) accession number: A1DMT2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 42 of the entry and version 1 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