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Protein

Beta-mannosidase B

Gene

mndB

Organism
Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
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

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 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.

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:AFLA_117830
OrganismiAspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167)
Taxonomic identifieri332952 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000001875 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:AFLA_117830.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 844844Beta-mannosidase BPRO_0000394653Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5059.CADAFLAP00012355.

Structurei

3D structure databases

ProteinModelPortaliB8NW36.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000186861.
KOiK01192.
OMAiYVEFNEH.
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.

B8NW36-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAFSQYPLS TGWSFKDSDD QSPEAWMPVP VVPSVAHQDL QANQKLKNPY
60 70 80 90 100
IGFNELDARW VNDKSWTYRT VFQKPAVAAG SSIILAFDGL DTFATVKLDG
110 120 130 140 150
SVILQSDNMF LAHRVDVTKA LEAEGDHVLE IDFDCAMRRA RELREKDTKH
160 170 180 190 200
NWASFNGDPA RMAVRKAQYH WGWDWGPLLS TAGIWREVRL EVYSAKISDL
210 220 230 240 250
WTEVELASDH QTARVSAFTE VDAADSVDSY KASFLLSLHG KEVAREVATL
260 270 280 290 300
KDKVAKVTFD VTQPSLWWPN GYGDPALYEI SVSLEKEDCE IHSVSKKIGI
310 320 330 340 350
RTAELIQQPD RHGKSFFFRI NGVDVFCGGS CWIPADNLLP SITAERYRKW
360 370 380 390 400
IELMVAGRQV MIRVWGGGCY EDDSFYQACD ELGVLVWQDF MFGCGNYPTW
410 420 430 440 450
PELLESIEKE ANYNVRRLRH HPSIVVYVGN NEDYQVQESA GLVYDYEDKN
460 470 480 490 500
PENWLKTDFP ARYIYEKLLP SVVEKLSPKT VYHPGSPWGD GKITSDPTVG
510 520 530 540 550
DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHMSTI EYFVENEADK
560 570 580 590 600
YPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLETYVYL TQVVQAETMM
610 620 630 640 650
FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAFYAVA
660 670 680 690 700
RVLKPIAVGV RREHHDWSVT HAQPPKTSKY ELWIASSLQK ETVGTIELRF
710 720 730 740 750
LSVNTGLDVR APILRDNVKI VPNGTTNILE GVINHKAQPE PHVLAARLWV
760 770 780 790 800
DGEVTARDVD WPQPFKYLDL SDRGLEVNKV SESGNEQKLL ITAKKPVKCL
810 820 830 840
VFEERDGIRV SDSAMDIVPG DGQTVTVTGL KAGDAPLKYK YLGQ
Length:844
Mass (Da):96,003
Last modified:March 3, 2009 - v1
Checksum:iCB0DFBDDBC8C0ADF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EQ963485 Genomic DNA. Translation: EED45554.1.
RefSeqiXP_002384490.1. XM_002384449.1.

Genome annotation databases

EnsemblFungiiCADAFLAT00012355; CADAFLAP00012355; CADAFLAG00012355.
GeneIDi7921506.
KEGGiafv:AFLA_117830.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EQ963485 Genomic DNA. Translation: EED45554.1.
RefSeqiXP_002384490.1. XM_002384449.1.

3D structure databases

ProteinModelPortaliB8NW36.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5059.CADAFLAP00012355.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFLAT00012355; CADAFLAP00012355; CADAFLAG00012355.
GeneIDi7921506.
KEGGiafv:AFLA_117830.

Organism-specific databases

EuPathDBiFungiDB:AFLA_117830.

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000186861.
KOiK01192.
OMAiYVEFNEH.
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

  1. "Genome sequence of Aspergillus flavus strain NRRL 3357."
    Payne W.G.A., Dean R.A., Nierman W.C., Amedeo P., Caler E.G.A., Fedorova N.D., Maiti R., Joardar V., Inman J., Galinsky K.J., Yu J., Bhatnagar D., Cleveland T.E.
    Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167.

Entry informationi

Entry nameiMANBB_ASPFN
AccessioniPrimary (citable) accession number: B8NW36
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: March 3, 2009
Last modified: April 29, 2015
This is version 38 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, 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.