Probable beta-mannosidase A precursor - Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)

Contribute

Read comments (?) or add your own

Q2UN00 (MANBA_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 42. 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:
Probable beta-mannosidase A
EC=3.2.1.25

Alternative name(s):
Mannanase A
Short name=Mannase A

Gene names

Name:	mndA
ORF Names:	AO090001000556

Organism

Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]

Taxonomic identifier

Taxonomic lineage

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

Protein attributes

Sequence length	914 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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 By similarity.
Catalytic activity	Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.
Pathway	Glycan metabolism; N-glycan degradation.
Subunit structure	Homodimer By similarity.
Subcellular location	Secreted By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 2 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	beta-mannosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

20

Potential

Chain

894

Probable beta-mannosidase A

PRO_0000394647

Sites

Active site

1

Proton donor By similarity

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

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q2UN00 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: F56D1E1EFAC63821
Show »

914

102,870

        10         20         30         40         50         60 
MRFTATAAAL VASSIPATLG QHVRDLSNEK WTLSSDALNH TVPGNLPSHA HLDLLKAGVI 

        70         80         90        100        110        120 
DDPYHGLNDF NLRWIPESNW TYTTDKIKDL MPIEFCGKYV ASTNNQYRQY SFDVSQILEG 

       130        140        150        160        170        180 
CNEDPILKID FGSAPNIVNA IAEDRNSPVW PDGIQQTYEY PNRWFMRKEQ SDFGWDWGPA 

       190        200        210        220        230        240 
FAPAGPWKPA YIVQLPKAQN IHVLNTDLDI YRKGQINHLP PDQSQPWVVN ASIDFVGSLP 

       250        260        270        280        290        300 
PNPSMSIEFK DTKSGEILTS KRIGNVTVSG NSVTGVTVLG GVTPKLWWPL GLGDQNLYNI 

       310        320        330        340        350        360 
TVTVTGHQNQ TLAHVTKRTG FRTIFLNQRN ITDAQLAQGI APGANWHFEV NGHEFYAKGS 

       370        380        390        400        410        420 
NIIPPDAFWP RVTEARMARL FDAVVAGNQN MLRVWSSGIY LHDFIYDLAD ERGILLWSEF 

       430        440        450        460        470        480 
EFSDALYPVD DAFLDNIAAE VVYNVRRVNH HPSLALWAGG NEIESLMLPT VERKAPEEYA 

       490        500        510        520        530        540 
KYVGEYEKLY ISLILPLVYQ NTRSITYSPS STTEGYLDVD LSAPVPMVER YHNTTPGSYY 

       550        560        570        580        590        600 
GDTDFYNYDS SVSFNSHVYP VGRFANEFGY HSMPSLQTWQ QAVDPEDLHF NSTTVMLRNH 

       610        620        630        640        650        660 
HYPAGGTFTD NFHNTSLGMG EMTIAVQRYY PIPNKLDSVA NFSAWCHATQ LFQADMYKSE 

       670        680        690        700        710        720 
IQFYRRGSGM PERQLGSLYW QLEDIWQAPS WAGIEYGGRW KVLHYVSRDI YQPIIVSPFW 

       730        740        750        760        770        780 
NYTTGDLDLY VTSDLWESAK GKVNLTWLDL SGTPLPHNAG TPGSVPFNVG ALNTTKIYST 

       790        800        810        820        830        840 
NIKNLTLPNP KDAILVLSLS GEGHLPNSDK KTTFTHQNHF TPVFPKDLAL VDPGLELSYN 

       850        860        870        880        890        900 
TKSKTFTVEA KSGVSLYTWL DYPADVVGYF DENAFVLLPG QKKEIGFTVQ EDNTDGKWVQ 

       910 
GVTVQSLWNQ TLEK

References

[1]

"Genome sequencing and analysis of Aspergillus oryzae."
Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.

expand/collapse author list

Kikuchi H.
Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP007154 Genomic DNA. Translation: BAE57065.1.
3D structure databases
ProteinModelPortal	Q2UN00.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAORAT00000510; CADAORAP00000499; CADAORAG00000510.
Phylogenomic databases
eggNOG	COG3250.
HOGENOM	HOG000216059.
OrthoDB	EOG47DDQ6.
Enzyme and pathway databases
UniPathway	UPA00280.
Family and domain databases
Gene3D	2.60.40.320. 1 hit. 3.20.20.80. 2 hits.
InterPro	IPR013812. Glyco_hydro_2/20_Ig-like. IPR006102. Glyco_hydro_2_Ig-like. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF00703. Glyco_hydro_2. 1 hit. [Graphical view]
SUPFAM	SSF49303. Glyco_hydro_2Ig. 2 hits. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00719. GLYCOSYL_HYDROL_F2_1. False negative. PS00608. GLYCOSYL_HYDROL_F2_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MANBA_ASPOR

Accession

Primary (citable) accession number: Q2UN00

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 15, 2010
Last sequence update:	January 24, 2006
Last modified:	May 1, 2013
This is version 42 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