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O74168

- MANBA_ASPAC

UniProt

O74168 - MANBA_ASPAC

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Protein
Beta-mannosidase A
Gene
mndA, manB
Organism
Aspergillus aculeatus
Status
Reviewed - 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.

Pathwayi

Sites

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

GO - Molecular functioni

  1. beta-mannosidase activity Source: UniProtKB-EC
Complete GO annotation...

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 – 2323 Reviewed prediction
Add
BLAST
Chaini24 – 937914Beta-mannosidase A
PRO_0000394642Add
BLAST

Amino acid modifications

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

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Homodimer By similarity.

Structurei

3D structure databases

ProteinModelPortaliO74168.

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

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MRALPTTATT LLGVLFFPSA SRSQYVRDLG TEQWTLSSAT LNRTVPAQFP    50
SQVHMDLLRE GIIDEPYNDL NDFNLRWIAD ANWTYTSGKI EGLGEDYEST 100
WLVFDGLDTF ASISFCGQFV GATDNQFRQY MFDVSSILKA CPEEPTLGIQ 150
FGSAPNIVDA IAQDPSSPTW PEGVQITYEY PNRWFMRKEQ SDFGWDWGPA 200
FAPAGPWKPG YVVQLKQAAP VYVRNTDLDI YRLGQINYLP PDQTQPWVVN 250
ASLDYLGSLP ENPSMAIEVK DLQSGEILAS RPLTNITVTE GSVTGVTVLE 300
GVDPKLWWPQ GLGDQNLYNV TISVTDGGNQ SVAEVTKRTG FRTIFLNQRN 350
ITDAQLAQGI APGANWHFEV NGHEFYAKGS NLIPPDCFWT RVTEDTMTRL 400
FDAVVAGNQN MLRVWSSGAY LHDYIYDLAD EKGILLCSEF QFSDALYPTD 450
DAFLENVAAE VVYNVRRVNH HPSLALWAGG NEIESLMLLL VEAADPESYP 500
FYVGEYEKMY ISLFLPLVYE NTRSISYSPS STTEGYLDID LSAPVPMAER 550
YSNTTEGEYY GDTDHYNYDA SIAFDYGTYP VGRFANEFGF HSMPSLQTWQ 600
QALTDPADLT FNSSVVMLRN HHYPAGGLMT DNYHNTVARH GRNDPGRAGL 650
LPDAQHSVRP RGQLQRLVPR DPALPGGPLQ VTNPVLPAGQ RAARTPARVP 700
VLAARGHLAG ALVGGDRVRR PLEGPHYVAR DIYKPVIVSP FWNYTTGALD 750
IYVTSDLWTA AAGSVTLTWR DLSGKPIASN GGLPTKPLPF HVGALNSTRL 800
YRMNMKQQPL PRHEDAILAL ELTATGSLPN TDEEVTFTHE QWFTPAFPKD 850
LDLVNLRVRV EYDAPLGKFA VEATAGVALY TWLEHPEGVV GYFEENSFVV 900
VPGQKKVVGF VVQADETDGE WVHDVTVRSL WDLNEGE 937
Length:937
Mass (Da):104,216
Last modified:November 1, 1998 - v1
Checksum:i0F6200BEB03D704B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB015509 Genomic DNA. Translation: BAA29029.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB015509 Genomic DNA. Translation: BAA29029.1 .

3D structure databases

ProteinModelPortali O74168.
ModBasei Search...

Protein family/group databases

CAZyi GH2. Glycoside Hydrolase Family 2.
mycoCLAPi MND2B_ASPAC.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00280 .

Family and domain databases

Gene3Di 2.60.120.260. 2 hits.
2.60.40.320. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR008979. 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 ]
Pfami PF00703. Glyco_hydro_2. 1 hit.
[Graphical view ]
SUPFAMi SSF49303. SSF49303. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

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: June 11, 2014
This is version 70 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

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