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A2QYN2

- MANBB_ASPNC

UniProt

A2QYN2 - MANBB_ASPNC

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Protein
Beta-mannosidase B
Gene
mndB, An12g01850
Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 2 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. 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 activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei432 – 4321Proton donor By similarity

GO - Molecular functioni

  1. beta-mannosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. mannan catabolic process Source: InterPro
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 B (EC:3.2.1.25)
Alternative name(s):
Mannanase B
Short name:
Mannase B
Gene namesi
Name:mndB
ORF Names:An12g01850
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706: Chromosome 3L

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 844844Beta-mannosidase B
PRO_0000394655Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi723 – 7231N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00009453.

Structurei

3D structure databases

ProteinModelPortaliA2QYN2.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000186861.
KOiK01192.
OrthoDBiEOG7NSB9Q.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
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.
IPR006104. Glyco_hydro_2_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR028369. Mannanase.
[Graphical view]
PANTHERiPTHR10066:SF12. PTHR10066:SF12. 1 hit.
PfamiPF00703. Glyco_hydro_2. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
SUPFAMiSSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

A2QYN2-1 [UniParc]FASTAAdd to Basket

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MAAFAQYTLS TGWYFKDRDE LASEAWMPVP VVPSVVHQDL QANGKLKNPY    50
VGFNELDARW VNEKSWTYRK ILQKPTVLAG SRIVLAFDGL DTFAKVKLDN 100
NIILESSNMF QAYRVDVTKA LDCGDEHVLE IEFDCAMLRA QELRKQDPNH 150
NWASFNGDPA RMSVRKAQYH WGWDWGPVLM TAGIWRAVRL EVYSTRLADL 200
WTEINLDPTH KTASISAFTE LESVDLDPSY KVKFTITLHG KQIAQAEATP 250
QEGRAKVEFN IDQPCLWWPH GYGDSTLYEV SASLNADQLE LHRVTKKIGI 300
RTAEVVQRPD KHGKSFFFRI NGVDIFCGGS CWIPADNLLP NISPQRYRKW 350
IQLMVAGRQA MIRVWGGGCY EDDSFYEACD ELGVLVWQDF MFGCGNYPTW 400
PELLKSIEQE AIYNVRRLRH HPSIVVYVGN NEDYQVQEQA GLEYNYEDKN 450
PENWLKTNFP ARYIYEELLP SVVERCSPKT FYHPGSPWGD GKITSDPTVG 500
DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHLSTI EYFVENEKDK 550
YPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLETYIYL TQVVQAETMM 600
FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAYYAVA 650
RVLNPVAVGV RREHHDWSIT HAQPPKTSKY ELWVVSSLQK PASGKVELRF 700
LSVDTGREIR ERIVRENVDI VPNGTTNLIT DGLIDHTVDA EPHVLAARLW 750
VDGEIVARDV DWPQPFKYLD FADRGLEVKR VSEASDQQVF QISTEKPVKC 800
LVFEERDGVK FSDSAMDIVP GDVQTVKVTG LRADEKLKYK FLGQ 844
Length:844
Mass (Da):97,117
Last modified:March 6, 2007 - v1
Checksum:iD24AE1CB82B9CEA0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270263 Genomic DNA. Translation: CAK48467.1.
RefSeqiXP_001395271.1. XM_001395234.2.

Genome annotation databases

EnsemblFungiiCADANGAT00009634; CADANGAP00009453; CADANGAG00009634.
GeneIDi4985535.
KEGGiang:ANI_1_250104.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270263 Genomic DNA. Translation: CAK48467.1 .
RefSeqi XP_001395271.1. XM_001395234.2.

3D structure databases

ProteinModelPortali A2QYN2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5061.CADANGAP00009453.

Protein family/group databases

CAZyi GH2. Glycoside Hydrolase Family 2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANGAT00009634 ; CADANGAP00009453 ; CADANGAG00009634 .
GeneIDi 4985535.
KEGGi ang:ANI_1_250104.

Phylogenomic databases

eggNOGi COG3250.
HOGENOMi HOG000186861.
KOi K01192.
OrthoDBi EOG7NSB9Q.

Enzyme and pathway databases

UniPathwayi UPA00280 .

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProi IPR008979. 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 ]
PANTHERi PTHR10066:SF12. PTHR10066:SF12. 1 hit.
Pfami PF00703. Glyco_hydro_2. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view ]
SUPFAMi SSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

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 nameiMANBB_ASPNC
AccessioniPrimary (citable) accession number: A2QYN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: March 6, 2007
Last modified: May 14, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete 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

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