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Protein

Beta-mannosidase A

Gene

mndA

Organism
Aspergillus aculeatus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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. Releases the terminal mannose residue from mannotriose and is somewaht less active on other mannooligosaccharides.1 Publication

Catalytic activityi

Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.1 Publication

pH dependencei

Optimum pH is 2.0. Stable from pH 4 to pH 7.1 Publication

Temperature dependencei

Optimum temperature is 70 degrees Celsius.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei482 – 4821Proton donorBy similarity

GO - Molecular functioni

  1. beta-mannosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

UniPathwayiUPA00280.

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.
mycoCLAPiMND2B_ASPAC.

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
Synonyms:manB
OrganismiAspergillus aculeatus
Taxonomic identifieri5053 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

Secreted 2 Publications

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 937914Beta-mannosidase APRO_0000394642Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi82 – 821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi285 – 2851N-linked (GlcNAc...)Sequence Analysis
Glycosylationi319 – 3191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi329 – 3291N-linked (GlcNAc...)Sequence Analysis
Glycosylationi350 – 3501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi553 – 5531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi612 – 6121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi743 – 7431N-linked (GlcNAc...)Sequence Analysis
Glycosylationi796 – 7961N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO74168.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.320. 1 hit.
3.20.20.80. 1 hit.
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. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O74168-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRALPTTATT LLGVLFFPSA SRSQYVRDLG TEQWTLSSAT LNRTVPAQFP
60 70 80 90 100
SQVHMDLLRE GIIDEPYNDL NDFNLRWIAD ANWTYTSGKI EGLGEDYEST
110 120 130 140 150
WLVFDGLDTF ASISFCGQFV GATDNQFRQY MFDVSSILKA CPEEPTLGIQ
160 170 180 190 200
FGSAPNIVDA IAQDPSSPTW PEGVQITYEY PNRWFMRKEQ SDFGWDWGPA
210 220 230 240 250
FAPAGPWKPG YVVQLKQAAP VYVRNTDLDI YRLGQINYLP PDQTQPWVVN
260 270 280 290 300
ASLDYLGSLP ENPSMAIEVK DLQSGEILAS RPLTNITVTE GSVTGVTVLE
310 320 330 340 350
GVDPKLWWPQ GLGDQNLYNV TISVTDGGNQ SVAEVTKRTG FRTIFLNQRN
360 370 380 390 400
ITDAQLAQGI APGANWHFEV NGHEFYAKGS NLIPPDCFWT RVTEDTMTRL
410 420 430 440 450
FDAVVAGNQN MLRVWSSGAY LHDYIYDLAD EKGILLCSEF QFSDALYPTD
460 470 480 490 500
DAFLENVAAE VVYNVRRVNH HPSLALWAGG NEIESLMLLL VEAADPESYP
510 520 530 540 550
FYVGEYEKMY ISLFLPLVYE NTRSISYSPS STTEGYLDID LSAPVPMAER
560 570 580 590 600
YSNTTEGEYY GDTDHYNYDA SIAFDYGTYP VGRFANEFGF HSMPSLQTWQ
610 620 630 640 650
QALTDPADLT FNSSVVMLRN HHYPAGGLMT DNYHNTVARH GRNDPGRAGL
660 670 680 690 700
LPDAQHSVRP RGQLQRLVPR DPALPGGPLQ VTNPVLPAGQ RAARTPARVP
710 720 730 740 750
VLAARGHLAG ALVGGDRVRR PLEGPHYVAR DIYKPVIVSP FWNYTTGALD
760 770 780 790 800
IYVTSDLWTA AAGSVTLTWR DLSGKPIASN GGLPTKPLPF HVGALNSTRL
810 820 830 840 850
YRMNMKQQPL PRHEDAILAL ELTATGSLPN TDEEVTFTHE QWFTPAFPKD
860 870 880 890 900
LDLVNLRVRV EYDAPLGKFA VEATAGVALY TWLEHPEGVV GYFEENSFVV
910 920 930
VPGQKKVVGF VVQADETDGE WVHDVTVRSL WDLNEGE
Length:937
Mass (Da):104,216
Last modified:November 1, 1998 - v1
Checksum:i0F6200BEB03D704B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015509 Genomic DNA. Translation: BAA29029.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015509 Genomic DNA. Translation: BAA29029.1.

3D structure databases

ProteinModelPortaliO74168.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.
mycoCLAPiMND2B_ASPAC.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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. 1 hit.
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. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequencing of beta-mannosidase gene from Aspergillus aculeatus no. F-50."
    Takada G., Kawaguchi T., Kaga T., Sumitani J., Arai M.
    Biosci. Biotechnol. Biochem. 63:206-209(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 55-71; 186-189; 265-274; 411-424 AND 805-819, GLYCOSYLATION, SUBCELLULAR LOCATION.
    Strain: F-50.
  2. "Purification and properties of a beta-mannosidase from Aspergillus aculeatus."
    Arai M., Fujimoto H., Ooi T., Ogura S., Murao S.
    J. Appl. Glycosci. 42:49-51(1995)
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
    Strain: F-50.

Entry informationi

Entry nameiMANBA_ASPAC
AccessioniPrimary (citable) accession number: O74168
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: November 1, 1998
Last modified: January 7, 2015
This is version 73 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

Direct protein sequencing

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.