Probable beta-mannosidase A precursor - Aspergillus niger (strain CBS 513.88 / FGSC A1513)

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A2QWU9 (MANBA_ASPNC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 38. History...

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

Documents (3) |

Third-party data

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

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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:	An11g06540

Organism

Aspergillus niger (strain CBS 513.88 / FGSC A1513) [Complete proteome]

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	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

21

Potential

Chain

910

Probable beta-mannosidase A

PRO_5000220610

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

A2QWU9 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: C3D32E4763723612
Show »

931

104,026

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

        70         80         90        100        110        120 
IGEYHGLNDF NLRWIAAANW TYTSQPIKGL LDNYDSTWLV FDGLDTFATI SFCGQQIAST 

       130        140        150        160        170        180 
DNQFRQYAFD VSTALGSCKG DPVLSINFGS APNIVDAIAQ DSNSQKWPDD VQLTYEYPNR 

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

       250        260        270        280        290        300 
SQPWVVNASI DILGPLPTKP TMSIEVRDTH SGTILTSRTL NNVSVAGNAI TGVTVLDGLT 

       310        320        330        340        350        360 
PKLWWPQGLG DQNLYNVSIT VQSRGNQTVA SVNKRTGFRT IFLNQRNITE AQRAQGIAPG 

       370        380        390        400        410        420 
ANWHFEVNGH EFYAKGSNLI PPDSFWTRVT EEKMSRLFDA 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 MGVVSYYPIP 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 GLKIGHSSKK TTVTVEATSG VSLYTWLDYP EGVVGYFEEN AFVLAPGEKK 

       910        920        930 
EISFTVLEDT TDGAWVRNIT VQSLWDQKVR G

References

[1]

"Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.

expand/collapse author list

Stam H.
Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CBS 513.88 / FGSC A1513.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM270241 Genomic DNA. Translation: CAK96951.1.
3D structure databases
ProteinModelPortal	A2QWU9.
ModBase	Search...
Protein family/group databases
CAZy	GH2. Glycoside Hydrolase Family 2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANGAT00008982; CADANGAP00008814; CADANGAG00008982.
Phylogenomic databases
eggNOG	COG3250.
HOGENOM	HOG000216059.
OrthoDB	EOG47DDQ6.
Enzyme and pathway databases
UniPathway	UPA00280.
Family and domain databases
Gene3D	2.60.120.260. 2 hits. 2.60.40.320. 1 hit. 3.20.20.80. 2 hits.
InterPro	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]
Pfam	PF00703. Glyco_hydro_2. 1 hit. [Graphical view]
SUPFAM	SSF49785. Gal_bind_like. 1 hit. 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_ASPNC

Accession

Primary (citable) accession number: A2QWU9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 15, 2010
Last sequence update:	March 6, 2007
Last modified:	May 29, 2013
This is version 38 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

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