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Protein

Beta-mannosidase A

Gene

mndA

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

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

Pathway: N-glycan degradation

This protein is involved in the pathway N-glycan degradation, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway N-glycan degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei479 – 4791Proton donorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

UniPathwayiUPA00280.

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-mannosidase A (EC:3.2.1.25)
Alternative name(s):
Mannanase A
Short name:
Mannase A
Gene namesi
Name:mndA
ORF Names:An11g06540
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706 Componenti: Chromosome 7R

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 931910Beta-mannosidase APRO_5000220610Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi40 – 401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi247 – 2471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi282 – 2821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi326 – 3261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi550 – 5501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi608 – 6081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi658 – 6581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi738 – 7381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi790 – 7901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi798 – 7981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi830 – 8301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi918 – 9181N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi5061.CADANGAP00008814.

Structurei

3D structure databases

ProteinModelPortaliA2QWU9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000216059.
OrthoDBiEOG78D7TH.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR008979. 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.
[Graphical view]
PfamiPF00703. Glyco_hydro_2. 1 hit.
[Graphical view]
SUPFAMiSSF49303. SSF49303. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A2QWU9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRHSIGLAAA LLAPTLPVAL GQYIRDLSTE KWTLSSRALN RTVPAQFPSQ
60 70 80 90 100
VHLDLLRAGV IGEYHGLNDF NLRWIAAANW TYTSQPIKGL LDNYDSTWLV
110 120 130 140 150
FDGLDTFATI SFCGQQIAST DNQFRQYAFD VSTALGSCKG DPVLSINFGS
160 170 180 190 200
APNIVDAIAQ DSNSQKWPDD VQLTYEYPNR WFMRKEQSDF GWDWGPAFAP
210 220 230 240 250
AGPWKPAYIV QLDKKESVYV LNTDLDIYRK GQINYLPPDQ SQPWVVNASI
260 270 280 290 300
DILGPLPTKP TMSIEVRDTH SGTILTSRTL NNVSVAGNAI TGVTVLDGLT
310 320 330 340 350
PKLWWPQGLG DQNLYNVSIT VQSRGNQTVA SVNKRTGFRT IFLNQRNITE
360 370 380 390 400
AQRAQGIAPG ANWHFEVNGH EFYAKGSNLI PPDSFWTRVT EEKMSRLFDA
410 420 430 440 450
VVVGNQNMLR VWSSGAYLHD YIYDLADEKG ILLWSEFEFS DALYPSDDAF
460 470 480 490 500
LENVAAEIVY NVRRVNHHPS LALWAGGNEI ESLMLPRVKD AAPSSYSYYV
510 520 530 540 550
GEYEKMYISL FLPLVYENTR SISYSPSSTT EGYLYIDLSA PVPMAERYDN
560 570 580 590 600
TTSGSYYGDT DHYDYDTSVA FDYGSYPVGR FANEFGFHSM PSLQTWQQAV
610 620 630 640 650
DTEDLYFNSS VVMLRNHHDP AGGLMTDNYA NSATGMGEMT MGVVSYYPIP
660 670 680 690 700
SKSDHISNFS AWCHATQLFQ ADMYKSQIQF YRRGSGMPER QLGSLYWQLE
710 720 730 740 750
DIWQAPSWAG IEYGGRWKVL HHVMRDIYQP VIVSPFWNYT TGSLDVYVTS
760 770 780 790 800
DLWSPAAGTV DLTWLDLSGR PIAGNAGTPK SVPFTVGGLN STRIYGTNVS
810 820 830 840 850
SLGLPDTKDA VLILSLSAHG RLPNSDRTTN LTHENYATLS WPKDLKIVDP
860 870 880 890 900
GLKIGHSSKK TTVTVEATSG VSLYTWLDYP EGVVGYFEEN AFVLAPGEKK
910 920 930
EISFTVLEDT TDGAWVRNIT VQSLWDQKVR G
Length:931
Mass (Da):104,026
Last modified:March 6, 2007 - v1
Checksum:iC3D32E4763723612
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270241 Genomic DNA. Translation: CAK96951.1.

Genome annotation databases

EnsemblFungiiCADANGAT00008982; CADANGAP00008814; CADANGAG00008982.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270241 Genomic DNA. Translation: CAK96951.1.

3D structure databases

ProteinModelPortaliA2QWU9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00008814.

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANGAT00008982; CADANGAP00008814; CADANGAG00008982.

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000216059.
OrthoDBiEOG78D7TH.

Enzyme and pathway databases

UniPathwayiUPA00280.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR008979. 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.
[Graphical view]
PfamiPF00703. Glyco_hydro_2. 1 hit.
[Graphical view]
SUPFAMiSSF49303. SSF49303. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513.

Entry informationi

Entry nameiMANBA_ASPNC
AccessioniPrimary (citable) accession number: A2QWU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: March 6, 2007
Last modified: January 7, 2015
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.