Alpha-glucosidase precursor - Aspergillus niger

Preferred order of sections

Names and origin

Protein names

Recommended name:
Alpha-glucosidase
EC=3.2.1.20

Alternative name(s):
Maltase

Gene names

Name:

aglA

Organism

Aspergillus niger

Taxonomic identifier

5061 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	985 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	Hydrolyzes malto-oligosaccharides, but has a low activity toward soluble starch.
Catalytic activity	Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.
Post-translational modification	The O-linked saccharide is not identified, but is probably mannose.
Sequence similarities	Belongs to the glycosyl hydrolase 31 family.

Ontologies

Keywords
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	carbohydrate binding Inferred from electronic annotation. Source: InterPro maltose alpha-glucosidase 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

1 – 25

25

Ref.2

Chain

26 – 985

960

Alpha-glucosidase

PRO_0000018576

Sites

Active site

490

1

Nucleophile

Active site

493

1

By similarity

Active site

660

1

Proton donor By similarity

Amino acid modifications

Glycosylation

36

1

O-linked (Man) Probable

Glycosylation

124

1

N-linked (GlcNAc...) Ref.2

Glycosylation

143

1

N-linked (GlcNAc...) Ref.2

Glycosylation

218

1

N-linked (GlcNAc...) Ref.2

Glycosylation

347

1

N-linked (GlcNAc...) Ref.2

Glycosylation

422

1

N-linked (GlcNAc...) Ref.2

Glycosylation

506

1

N-linked (GlcNAc...) Ref.2

Glycosylation

534

1

N-linked (GlcNAc...) Ref.2

Glycosylation

537

1

N-linked (GlcNAc...)

Glycosylation

545

1

O-linked (Man) Probable

Glycosylation

550

1

O-linked (Man) Probable

Glycosylation

559

1

O-linked (Man) Probable

Glycosylation

560

1

O-linked (Man) Probable

Glycosylation

561

1

O-linked (Man) Probable

Glycosylation

562

1

O-linked (Man) Probable

Glycosylation

571

1

O-linked (Man) Probable

Glycosylation

601

1

N-linked (GlcNAc...) Ref.2

Glycosylation

623

1

N-linked (GlcNAc...) Ref.2

Glycosylation

835

1

N-linked (GlcNAc...) Ref.2

Glycosylation

881

1

N-linked (GlcNAc...) Ref.2

Glycosylation

895

1

O-linked (Man) Probable

Glycosylation

899

1

N-linked (GlcNAc...) Ref.2

Glycosylation

957

1

N-linked (GlcNAc...) Ref.2

Glycosylation

970

1

N-linked (GlcNAc...) Ref.2

Natural variations

Natural variant

27 – 28

2

TT → LL in strain: GN-8.

Natural variant

42

1

D → A in strain: GN-8.

Natural variant

929

1

N → M in strain: GN-8.

Sequences

Sequence

Length

Mass (Da)

Tools

P56526 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: 9A18772AEB2E0927
Show »

FASTA

985

108,913

        10         20         30         40         50         60 
MVKLTHLLAR AWLVPLAYGA SQSLLSTTAP SQPQFTIPAS ADVGAQLIAN IDDPQAADAQ 

        70         80         90        100        110        120 
SVCPGYKASK VQHNSRGFTA SLQLAGRPCN VYGTDVESLT LSVEYQDSDR LNIQILPTHV 

       130        140        150        160        170        180 
DSTNASWYFL SENLVPRPKA SLNASVSQSD LFVSWSNEPS FNFKVIRKAT GDALFSTEGT 

       190        200        210        220        230        240 
VLVYENQFIE FVTALPEEYN LYGLGEHITQ FRLQRNANLT IYPSDDGTPI DQNLYGQHPF 

       250        260        270        280        290        300 
YLDTRYYKGD RQNGSYIPVK SSEADASQDY ISLSHGVFLR NSHGLEILLR SQKLIWRTLG 

       310        320        330        340        350        360 
GGIDLTFYSG PAPADVTRQY LTSTVGLPAM QQYNTLGFHQ CRWGYNNWSD LADVVANFEK 

       370        380        390        400        410        420 
FEIPLEYIWT DIDYMHGYRN FDNDQHRFSY SEGDEFLSKL HESGRYYVPI VDAALYIPNP 

       430        440        450        460        470        480 
ENASDAYATY DRGAADDVFL KNPDGSLYIG AVWPGYTVFP DWHHPKAVDF WANELVIWSK 

       490        500        510        520        530        540 
KVAFDGVWYD MSEVSSFCVG SCGTGNLTLN PAHPSFLLPG EPGDIIYDYP EAFNITNATE 

       550        560        570        580        590        600 
AASASAGASS QAAATATTTS TSVSYLRTTP TPGVRNVEHP PYVINHDQEG HDLSVHAVSP 

       610        620        630        640        650        660 
NATHVDGVEE YDVHGLYGHQ GLNATYQGLL EVWSHKRRPF IIGRSTFAGS GKWAGHWGGD 

       670        680        690        700        710        720 
NYSKWWSMYY SISQALSFSL FGIPMFGADT CGFNGNSDEE LCNRWMQLSA FFPFYRNHNE 

       730        740        750        760        770        780 
LSTIPQEPYR WASVIEATKS AMRIRYAILP YFYTLFDLAH TTGSTVMRAL SWEFPNDPTL 

       790        800        810        820        830        840 
AAVETQFMVG PAIMVVPVLE PLVNTVKGVF PGVGHGEVWY DWYTQAAVDA KPGVNTTISA 

       850        860        870        880        890        900 
PLGHIPVYVR GGNILPMQEP ALTTREARQT PWALLAALGS NGTASGQLYL DDGESIYPNA 

       910        920        930        940        950        960 
TLHVDFTASR SSLRSSAQGR WKERNPLANV TVLGVNKEPS AVTLNGQAVF PGSVTYNSTS 

       970        980 
QVLFVGGLQN LTKGGAWAEN WVLEW

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References

[1]

"Cloning and sequencing of an alpha-glucosidase gene from Aspergillus niger and its expression in A. nidulans."
Nakamura A., Nishimura I., Yokoyama A., Lee D.-G., Hidaka M., Masaki H., Kimura A., Chiba S., Uozumi T.
J. Biotechnol. 53:75-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: GN-3.

[2]

"Complete amino acid sequence of crystalline alpha-glucosidase from Aspergillus niger."
Kimura A., Takata M., Sakai O., Matsui H., Takai N., Takayanagi T., Nishimua I., Uozumi T., Chiba S.
Biosci. Biotechnol. Biochem. 56:1368-1370(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-252 AND 267-985, GLYCOSYLATION AT THR-36; ASN-124; ASN-143; ASN-218; ASN-347; ASN-422; ASN-506; ASN-534; SER-545; SER-550; THR-559; SER-560; THR-561; SER-562; THR-571; ASN-601; ASN-623; ASN-835; ASN-881; SER-895; ASN-899; ASN-957 AND ASN-970.
Strain: GN-8.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D45356 Genomic DNA. Translation: BAA23616.1.
PIR	JC1199. JC1200. JC5561.
3D structure databases
ProteinModelPortal	P56526.
ModBase	Search...
Protein-protein interaction databases
STRING	5061.CADANGAP00004308.
Protein family/group databases
CAZy	GH31. Glycoside Hydrolase Family 31.
mycoCLAP	AGL31A_ASPNG.
PTM databases
GlycoSuiteDB	P56526.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG1501.
Family and domain databases
InterPro	IPR011013. Gal_mutarotase_SF_dom. IPR000322. Glyco_hydro_31. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
PANTHER	PTHR22762. PTHR22762. 1 hit.
Pfam	PF01055. Glyco_hydro_31. 1 hit. [Graphical view]
SUPFAM	SSF74650. Gal_mut_like. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00129. GLYCOSYL_HYDROL_F31_1. 1 hit. PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL3435.

Entry information

Entry name

AGLU_ASPNG

Accession

Primary (citable) accession number: P56526
Secondary accession number(s): O13451

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 15, 1998
Last modified:	April 3, 2013
This is version 61 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

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Protocols and materials databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents