Beta-mannosidase precursor - Aspergillus niger

Contribute

Read comments (?) or add your own

Q9UUZ3 (MANBA_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 60. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

to top of page

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

to top of page

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Beta-mannosidase
EC=3.2.1.25

Alternative name(s):
Mannanase
Short name=Mannase

Gene names

Name:

mndA

Organism

Aspergillus niger

Taxonomic identifier

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	931 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of all N-linked glycoprotein oligosaccharides. Involved in the degradation of mannan and galactomannan. Ref.1 UniProtKB O00462 Ref.2
Catalytic activity	Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides. Ref.1 Ref.2
Pathway	Glycan metabolism; N-glycan degradation. UniProtKB O00462
Subunit structure	Homodimer. Ref.2
Subcellular location	Secreted Ref.2.
Post-translational modification	N-glycosylated.
Sequence similarities	Belongs to the glycosyl hydrolase 2 family. UniProtKB O00462
Biophysicochemical properties	pH dependence: Optimum pH is 2.5-5.0. Ref.2 Temperature dependence: Optimum temperature is 70 degrees Celsius. Ref.2

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	carbohydrate catabolic process Inferred from direct assay Ref.2 Ref.1. Source: UniProtKB
Cellular_component	extracellular region Non-traceable author statement Ref.2. Source: UniProtKB
Molecular_function	beta-mannosidase activity Inferred from direct assay Ref.2 Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

21

Potential

Chain

910

Beta-mannosidase

PRO_0000012168

Sites

Active site

1

Proton donor By similarity UniProtKB P08236

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q9UUZ3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: D296E185EA3BF430
Show »

931

104,390

        10         20         30         40         50         60 
MRHSIGLAAA LLAPTLPVAL GQHIRDLSSE KWTLSSRALN RTVPAQFPSQ VHLDLLRAGV 

        70         80         90        100        110        120 
IGEYHGLNDF NLRWIAAANW TYTSQPIKGL LDNYGSTWLV FDGLDTFATI SILWTANRIH 

       130        140        150        160        170        180 
GQSVSPVSGS MYLPALEACQ RRILIRKVSF RGGVTAEVNT CYLHIEWPDD VQLTYEYPNR 

       190        200        210        220        230        240 
WFMRKEQSDF GWDWGPAFAP AGPWKPAYIV QLDKKESVYV LNTDLDIYRK NQINYLPPDQ 

       250        260        270        280        290        300 
SQPWVVNASI DILGPLPAKP TMSIEVRDTH SGTILTSRTL NNVSVAGNAI TGVTVLDGLN 

       310        320        330        340        350        360 
PKLWWPQSSV IRTSTMFLSL SKVEGTRPWP VWTNGRASAP FFLNQRNITE VQRAQGIAPG 

       370        380        390        400        410        420 
ANWHFEVNGH EFYAKGSNLI PPDSFWTRVT EERISRLFDA VVVGNQNMLR VWSSGAYLHD 

       430        440        450        460        470        480 
YIYDLADEKG ILLWSEFEFS DALYPSDDAF LENVAAEIVY NVRRVNHHPS LALWAGGNEI 

       490        500        510        520        530        540 
ESLMLPRVKD AAPSSYSYYV GEYEKMYISL FLPLVYENTR SISYSPSSTT EGYLYIDLSA 

       550        560        570        580        590        600 
PVPMAERYDN TTSGSYYGDT DHYDYDTSVA FDYGSYPVGR FANEFGFHSM PSLQTWQQAV 

       610        620        630        640        650        660 
DTEDLYFNSS VVMLRNHHDP AGGLMTDNYA NSATGMGEMT MGVISYYPIP SKSDHISNFS 

       670        680        690        700        710        720 
AWCHATQLFQ ADMYKSQIQF YRRGSGMPER QLGSLYWQLE DIWQAPSWAG IEYGGRWKVL 

       730        740        750        760        770        780 
HHVMRDIYQP VIVSPFWNYT TGSLDVYVTS DLWSPAAGTV DLTWLDLSGR PIAGNAGTPK 

       790        800        810        820        830        840 
SVPFTVGGLN STRIYGTNVS SLGLPDTKDA VLILSLSAHG RLPNSDRTTN LTHENYATLS 

       850        860        870        880        890        900 
WPKDLKIVDP GLKLGYSSKK TTVTVEATSG VSLYTWLDYP EGVVGYFEEN AFVLAPGEKK 

       910        920        930 
EIGFTVLDDT TNGAWVRNIT VQSLWDQKVR G

References

[1]

"Cloning and characterization of Aspergillus niger genes encoding an alpha-galactosidase and a beta-mannosidase involved in galactomannan degradation."
Ademark P., de Vries R.P., Haegglund P., Staalbrand H., Visser J.
Eur. J. Biochem. 268:2982-2990(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY.
Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

[2]

"Hydrolytic properties of a beta-mannosidase purified from Aspergillus niger."
Ademark P., Lundqvist J., Haegglund P., Tenkanen M., Torto N., Tjerneld F., Staalbrand H.
J. Biotechnol. 75:281-289(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 490-504, CHARACTERIZATION.
Strain: ATCC 46890.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ251874 Genomic DNA. Translation: CAB63902.1.
3D structure databases
ProteinModelPortal	Q9UUZ3.
ModBase	Search...
Protein family/group databases
CAZy	GH2. Glycoside Hydrolase Family 2.
mycoCLAP	MND2A_ASPNG.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-17577.
UniPathway	UPA00280.
Family and domain databases
Gene3D	3.20.20.80. 2 hits.
InterPro	IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...
Other
ChEMBL	CHEMBL5417.

Entry information

Entry name

MANBA_ASPNG

Accession

Primary (citable) accession number: Q9UUZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 2002
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of page

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents