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Protein

Beta-mannosidase B

Gene

mndB

Organism
Aspergillus terreus (strain NIH 2624 / FGSC A1156)
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. 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

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei430 – 4301Proton donorBy 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.

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:ATEG_08684
OrganismiAspergillus terreus (strain NIH 2624 / FGSC A1156)
Taxonomic identifieri341663 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000007963: Unassembled WGS sequence

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 843843Beta-mannosidase BPRO_0000394657Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi721 – 7211N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi33178.CADATEAP00006706.

Structurei

3D structure databases

ProteinModelPortaliQ0CCA0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000186861.
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.

Q0CCA0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASFFQQSLA TGWSFKDAED NSAEAWMPVA QVPSVVHQDL IANNKLQDPY
60 70 80 90 100
VGFRELDARW VNEKSWTYRT VFQKPAVPAG SSVILAFDGL DTFAKVKLNG
110 120 130 140 150
NVILESNNMF LAHRIDVTKA LGADGDHVLE IDFDCAMLRA RELRAKDPQH
160 170 180 190 200
KWVGFNGDPA RMGVRKAQYH WGWDWGPVLM TAGIWRDVRL EVYTARVADL
210 220 230 240 250
WTETDLAVDH HAAQISAFAQ VEGAISSSKV NFILSLHGQE VARAVAEPQD
260 270 280 290 300
QVAKVAFDVQ QPSLWWPNGY GDPTLYEISA TLDQDGATVH QISKKIGIRT
310 320 330 340 350
AEVVQRPDKH GKSFFFRING VDIFCGGSCW IPADNLLPSI SAERYRKWIE
360 370 380 390 400
LMVHGRQVMI RVWGGGCYED DSFYQACDEL GVMVWQDFMF GCGNYPTWPE
410 420 430 440 450
MLESVEKEAI YNVRRLRHHP SIVVYVGNNE DYQVQEQQGL TYNFEDKDPQ
460 470 480 490 500
NWLKSDFPAR YIYEKILPEV VQRYSPSTFY HPGSPWGDGK ITSDPTVGDM
510 520 530 540 550
HQWNVWHGTQ EKYQIFDTLG GRFNSEFGME AFPHMSTIEY FVENEKDKYP
560 570 580 590 600
QSHVLDFHNK ADGHERRIAT YLVENLRTAT DLETYIYLTQ VVQAETMMFG
610 620 630 640 650
YRGWRRQWGD ERHCGGALLW QLNDCWPTIS WAIVDYFLRP KPAFYAVARV
660 670 680 690 700
LNPIAVGVRR EHHDWSVTHA QPPKKSKFEL WVASNLQKET RGMVELKFLS
710 720 730 740 750
VDTGREIRER IVREDVIIVP NGTTDIIVDG VIDHQEYAEP HVLAARLWVD
760 770 780 790 800
GKIVARDVDW PQPFKYLDLS GRGLEVKTVS TSDDQQTLLI SAQKPVKCLV
810 820 830 840
FEERDGVRVS DSAMDIVPGD EQTVTITGLK ADAPPLKYKY LGQ
Length:843
Mass (Da):96,245
Last modified:June 15, 2010 - v2
Checksum:iEE4DB1B4648C2506
GO

Sequence cautioni

The sequence EAU30816.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476606 Genomic DNA. Translation: EAU30816.1. Sequence problems.
RefSeqiXP_001217270.1. XM_001217269.1.

Genome annotation databases

GeneIDi4323103.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH476606 Genomic DNA. Translation: EAU30816.1. Sequence problems.
RefSeqiXP_001217270.1. XM_001217269.1.

3D structure databases

ProteinModelPortaliQ0CCA0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi33178.CADATEAP00006706.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi4323103.

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000186861.
OrthoDBiEOG7NSB9Q.

Enzyme and pathway databases

UniPathwayiUPA00280.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiMANBB_ASPTN
AccessioniPrimary (citable) accession number: Q0CCA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: January 7, 2015
This is version 47 of the entry and version 2 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, 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.