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Protein

Beta-mannosidase A

Gene

mndA

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
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. Involved in the degradation of polymeric mannan and galactomannan (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 sitei474 – 4741Proton 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 A (EC:3.2.1.25)
Alternative name(s):
Mannanase A
Short name:
Mannase A
Gene namesi
Name:mndA
ORF Names:AFUA_6G08840
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiFungiDB:Afu6g08840.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 926905Beta-mannosidase APRO_0000394646Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi40 – 401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi277 – 2771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi311 – 3111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi342 – 3421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi532 – 5321N-linked (GlcNAc...)Sequence Analysis
Glycosylationi603 – 6031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi626 – 6261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi653 – 6531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi733 – 7331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi756 – 7561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi785 – 7851N-linked (GlcNAc...)Sequence Analysis
Glycosylationi793 – 7931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi819 – 8191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi905 – 9051N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi5085.CADAFUAP00001844.

Structurei

3D structure databases

ProteinModelPortaliQ4WMS9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000216059.
InParanoidiQ4WMS9.
KOiK01192.
OMAiCHATQLF.
OrthoDBiEOG78D7TH.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
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.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00703. Glyco_hydro_2. 1 hit.
[Graphical view]
SUPFAMiSSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q4WMS9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHVKAETVLA LLTPAPPSVV GQHVVDLSGD GWTLSSTALN RTVPGHLPSQ
60 70 80 90 100
VHLDLFEAGV IDIMASMILT FVGLRMPIGR IPATRLKAYF ESTWLVFDGL
110 120 130 140 150
DTFATITFCD QHVGSTDNQF RQHHFDVSQI LKECKQDPVL RINFGSAPNI
160 170 180 190 200
ANTIAKSPDA EEWPPGVQIT NEYPNRWYIR KEQSDFGWDW GPAFAPVGPW
210 220 230 240 250
KPSYIVQNGH AELYVLNTDI DIYRQGQINY LPPDQSQPWI VNASIDFLGP
260 270 280 290 300
VPCKPSMSIE IKDAATGSVL SSGLLQNVTV SGKSITGTTT IDGDAPKLWW
310 320 330 340 350
PSGMGKQNLY NVTITVQNDM KKSLAKVTKR TGFRTIFLNQ RNITDDQLAQ
360 370 380 390 400
GIAPGANWHF EINGYEFYTK GSNIIPPDAF WPRVTQARMA RLFDAVTAGN
410 420 430 440 450
QNMLRVWASG AYLHDFIYDL ADEKGILLWS EFQFSDALYP VNDAFLENVA
460 470 480 490 500
AEVVYNVRRV NHHPSLALWA GGNEIESLML PMARRADPTG YSKYIGEYEK
510 520 530 540 550
LYISLILPLV YENTRSITYS PSSTTEGYLY VNLSAPVPMA ERYSNTTPGS
560 570 580 590 600
YYGDTDYYNY DTSVSFDYNH YPVGRFANEF GFHSMPSLQT WQQAVDPEDL
610 620 630 640 650
QFNSSVVVLR NHHYTAGGLF TDNFKNSSKG MGEMTMGVEA YYPIPSKSDS
660 670 680 690 700
VANFSAWCHA TQLFQADLYK SQIQFYRRGS GMPERQLGSL YWQLEDIWQA
710 720 730 740 750
PTWAGIEYDG RWKVLHYVAR DIYQPIIVSP FWNYTTGRLE VYVTSDLWEP
760 770 780 790 800
AQGTVNLTWV DLSGKSIANN AGTPETVSFT VGALNTTNIY TTNISELSLP
810 820 830 840 850
DLKDSILILS LSGEGRLPNA SSKKAFVHQN HFTPVFPKDL SLKDPKLEVS
860 870 880 890 900
YSPESRKFTV QATGGVSLYT WLDYPAGAVG YFEANAFVLL PGVPKEVSFV
910 920
AQEGNVTDDW LQRVTVQSLW DQKVRD
Length:926
Mass (Da):103,736
Last modified:July 5, 2005 - v1
Checksum:i77968D62D87000E6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000006 Genomic DNA. Translation: EAL88735.1.
RefSeqiXP_750773.1. XM_745680.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00001844; CADAFUAP00001844; CADAFUAG00001844.
GeneIDi3508060.
KEGGiafm:AFUA_6G08840.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000006 Genomic DNA. Translation: EAL88735.1.
RefSeqiXP_750773.1. XM_745680.1.

3D structure databases

ProteinModelPortaliQ4WMS9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5085.CADAFUAP00001844.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00001844; CADAFUAP00001844; CADAFUAG00001844.
GeneIDi3508060.
KEGGiafm:AFUA_6G08840.

Organism-specific databases

EuPathDBiFungiDB:Afu6g08840.

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000216059.
InParanoidiQ4WMS9.
KOiK01192.
OMAiCHATQLF.
OrthoDBiEOG78D7TH.

Enzyme and pathway databases

UniPathwayiUPA00280.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
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.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00703. Glyco_hydro_2. 1 hit.
[Graphical view]
SUPFAMiSSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiMANBA_ASPFU
AccessioniPrimary (citable) accession number: Q4WMS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: July 5, 2005
Last modified: April 29, 2015
This is version 66 of the entry and version 1 of the sequence. [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

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.