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Protein

Beta-mannosidase B

Gene

mndB

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed-Annotation score: 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).By similarity

Miscellaneous

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

Catalytic activityi

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

Pathwayi: 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)DescriptionActionsGraphical viewLength
Active sitei432Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate 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
Proteomesi
  • UP000006706 Componenti: Chromosome 3L

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003946551 – 844Beta-mannosidase BAdd BLAST844

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi723N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00009453.

Structurei

3D structure databases

ProteinModelPortaliA2QYN2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000186861.
KOiK01192.
OrthoDBiEOG092C0CWO.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
2.60.40.10. 3 hits.
InterProiView protein in InterPro
IPR008979. Galactose-bd-like.
IPR006102. Glyco_hydro_2_Ig-like.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
PfamiView protein in Pfam
PF00703. Glyco_hydro_2. 1 hit.
SUPFAMiSSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

A2QYN2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAFAQYTLS TGWYFKDRDE LASEAWMPVP VVPSVVHQDL QANGKLKNPY
60 70 80 90 100
VGFNELDARW VNEKSWTYRK ILQKPTVLAG SRIVLAFDGL DTFAKVKLDN
110 120 130 140 150
NIILESSNMF QAYRVDVTKA LDCGDEHVLE IEFDCAMLRA QELRKQDPNH
160 170 180 190 200
NWASFNGDPA RMSVRKAQYH WGWDWGPVLM TAGIWRAVRL EVYSTRLADL
210 220 230 240 250
WTEINLDPTH KTASISAFTE LESVDLDPSY KVKFTITLHG KQIAQAEATP
260 270 280 290 300
QEGRAKVEFN IDQPCLWWPH GYGDSTLYEV SASLNADQLE LHRVTKKIGI
310 320 330 340 350
RTAEVVQRPD KHGKSFFFRI NGVDIFCGGS CWIPADNLLP NISPQRYRKW
360 370 380 390 400
IQLMVAGRQA MIRVWGGGCY EDDSFYEACD ELGVLVWQDF MFGCGNYPTW
410 420 430 440 450
PELLKSIEQE AIYNVRRLRH HPSIVVYVGN NEDYQVQEQA GLEYNYEDKN
460 470 480 490 500
PENWLKTNFP ARYIYEELLP SVVERCSPKT FYHPGSPWGD GKITSDPTVG
510 520 530 540 550
DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHLSTI EYFVENEKDK
560 570 580 590 600
YPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLETYIYL TQVVQAETMM
610 620 630 640 650
FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAYYAVA
660 670 680 690 700
RVLNPVAVGV RREHHDWSIT HAQPPKTSKY ELWVVSSLQK PASGKVELRF
710 720 730 740 750
LSVDTGREIR ERIVRENVDI VPNGTTNLIT DGLIDHTVDA EPHVLAARLW
760 770 780 790 800
VDGEIVARDV DWPQPFKYLD FADRGLEVKR VSEASDQQVF QISTEKPVKC
810 820 830 840
LVFEERDGVK FSDSAMDIVP GDVQTVKVTG LRADEKLKYK FLGQ
Length:844
Mass (Da):97,117
Last modified:March 6, 2007 - v1
Checksum:iD24AE1CB82B9CEA0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM270263 Genomic DNA. Translation: CAK48467.1.
RefSeqiXP_001395271.1. XM_001395234.2.

Genome annotation databases

EnsemblFungiiCAK48467; CAK48467; An12g01850.
GeneIDi4985535.
KEGGiang:ANI_1_250104.

Similar proteinsi

Entry informationi

Entry nameiMANBB_ASPNC
AccessioniPrimary (citable) accession number: A2QYN2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: March 6, 2007
Last modified: September 27, 2017
This is version 60 of the entry and version 1 of the sequence. See 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