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Q4WAH4 (MANBB_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-mannosidase B

EC=3.2.1.25
Alternative name(s):
Mannanase B
Short name=Mannase B
Gene names
Name:mndB
ORF Names:AFUA_7G01320
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length845 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 activity

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

Pathway

Glycan metabolism; N-glycan degradation.

Miscellaneous

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

Sequence similarities

Belongs to the glycosyl hydrolase 2 family. Beta-mannosidase B subfamily.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmannan catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionbeta-mannosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 845845Beta-mannosidase B
PRO_0000394654

Sites

Active site4321Proton donor By similarity

Amino acid modifications

Glycosylation2521N-linked (GlcNAc...) Potential
Glycosylation7171N-linked (GlcNAc...) Potential
Glycosylation7231N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q4WAH4 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: B6EA86796A8C33DE

FASTA84596,998
        10         20         30         40         50         60 
MSKLQQFPLS KGWSFRDNEA TSEDAWMPVP VVPSVVHQDL QANNKLKDPY IGFNELEARW 

        70         80         90        100        110        120 
VNEKSWTYKT VFQKPAAPAG SCIVLAFDGL DTFAKVKLDG NVILENDNMF LARRVDVTKA 

       130        140        150        160        170        180 
LEAEGDHVLE IDFDCAFLRA KELRKQDPRH NWASFNGDPS RLSVRKAQYH WGWDWGPVLM 

       190        200        210        220        230        240 
TAGIWREVRL EVYSARVADL WTEVQLASDH QSAQVTAFVE VESVHSGSHR ACFTLSLHGQ 

       250        260        270        280        290        300 
EITREEIGVT ENGTAKATFD VKEPSLWWPH GYGDATLYEV SVSLVKEQEE LHRVSKKFGI 

       310        320        330        340        350        360 
RTAEVIQRPD KHGKSFFFRV NGVDIFCGGS CWIPADNLLP SITAERYRKW IELMVHGRQV 

       370        380        390        400        410        420 
MIRVWGGGIY EDNSFYDACD ELGVLVWQDF MFGCGNYPTW PNLLESIRKE SVYNVRRLRH 

       430        440        450        460        470        480 
HPSIVIWVGN NEDYQVQEQA GLTYNYEDKD PENWLKTDFP ARYIYEKLLP EVVQEYSPGT 

       490        500        510        520        530        540 
FYHPGSPWGD GKTTSDPTVG DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHMSTI 

       550        560        570        580        590        600 
DYFVENEADK YPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLETHIYL TQVVQAETMM 

       610        620        630        640        650        660 
FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAFYAVA RVLNPIAVGV 

       670        680        690        700        710        720 
RREHHDWSVT HAQPPKTSKF ELWVASSRQQ EIQGTVELRF LSVNTGLEVR ERIVHENVSI 

       730        740        750        760        770        780 
VPNGTTNLIV DGLIDHTVHS EPHVLAARIW VDGQLVARDV DWPQPFKYLD LSDRGLEVKK 

       790        800        810        820        830        840 
ISESEDEQTL LISTKKPVKC LVFEEREGVR ISDSAMDIVP GDDQRVTIKG LKPGDAPLKY 


KFLGQ 

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000015 Genomic DNA. Translation: EAL84762.1.
RefSeqXP_746800.1. XM_741707.1.

3D structure databases

ProteinModelPortalQ4WAH4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00001205.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00001205; CADAFUAP00001205; CADAFUAG00001205.
GeneID3504183.
KEGGafm:AFUA_7G01320.

Phylogenomic databases

eggNOGCOG3250.
HOGENOMHOG000186861.
KOK01192.
OMASWGLGYY.
OrthoDBEOG7NSB9Q.

Enzyme and pathway databases

UniPathwayUPA00280.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProIPR008979. 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]
PANTHERPTHR10066:SF12. PTHR10066:SF12. 1 hit.
PfamPF00703. Glyco_hydro_2. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
SUPFAMSSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMANBB_ASPFU
AccessionPrimary (citable) accession number: Q4WAH4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: July 5, 2005
Last modified: May 14, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries