Alpha-glucosidase precursor - Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)

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Q12558 (AGLU_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 71. History...

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

Documents (2) |

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:
Alpha-glucosidase
Short name=AGL
EC=3.2.1.20

Alternative name(s):
Maltase

Gene names

Name:	agdA
ORF Names:	AO090003001209

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	985 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
Induction	By maltose.
Sequence similarities	Belongs to the glycosyl hydrolase 31 family.

Ontologies

Keywords
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome
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

25

By similarity

Chain

960

Alpha-glucosidase

PRO_0000018577

Sites

Active site

1

Nucleophile By similarity

Active site

1

By similarity

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

Glycosylation

1

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q12558 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 3E9EAE0A0E38209E
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985

108,704

        10         20         30         40         50         60 
MAGLKSFLAS SWLLPVACGA SQSIVPSTSA TAAYSQFTIP ASADVGANLV ANIDDPQAVN 

        70         80         90        100        110        120 
AQSVCPGYKA SDVKHSSQGF TASLELAGDP CNVYGTDVDS LTLTVEYQAK DRLNIQIVPT 

       130        140        150        160        170        180 
YFDASNASWY ILSEELVPRP KASQNASVPQ SDFVVSWSNE PSFNFKVIRK ATGDVLFNTK 

       190        200        210        220        230        240 
GSTLVYENQF IEFVTLLPEE YNLYGLGERM NQLRLLENAN LTLYAADIAD PIDDNIYGHH 

       250        260        270        280        290        300 
AFYLDTRYYK VGGQNKSHTI VKSSEAEPSQ EYVSYSHGVF LRNAHGQEIL LRDQKLIWRT 

       310        320        330        340        350        360 
LGGSVDLTFY SGPTQAEVTK QYQLSTVGLP AMQQYNTLGF HQCRWGYNNW SEFEDVLANF 

       370        380        390        400        410        420 
ERFEIPLEYL WADIDYMHGY RNFDNDQHRF SYEEGEKFLN KLHAGGRRWV PIVDGALYIP 

       430        440        450        460        470        480 
NPENASDAYE TYDRGAKDDV FIKNPDGSLY IGAVWPGYTV YPDWHHPKAS DFWANELVTW 

       490        500        510        520        530        540 
WNKLHYDGVW YDMAEVSSFC VGSCGTGNLS MNPAHPPFAL PGEPGNVVYD YPEGFNITNA 

       550        560        570        580        590        600 
TEAASASAGA ASQSAAASST TTSAPYLRTT PTPGVRNVDH PPYVINHVQP GHDLSVHAIS 

       610        620        630        640        650        660 
PNSTHSDGVQ EYDVHSLYGH QGINATYHGL LKVWENKRPF IIARSTFSGS GKWAGHWGGD 

       670        680        690        700        710        720 
NFSKWGSMFF SISQALQFSL FGIPMFGVDT CGFNGNTDEE LCNRWMQLSA FFPFYRNHNV 

       730        740        750        760        770        780 
LSAIPQEPYR WASVIDATKA AMNIRYAILP YFYTLFHLAH TTGSTVMRAL AWEFPNDPSL 

       790        800        810        820        830        840 
AAVGTQFLVG PSVMVIPVLE PQVDTVQGVF PGVGHGEVWY DWYSQTAVDA KPGVNTTISA 

       850        860        870        880        890        900 
PLGHIPVFVR GGSILPMQEV ALTTRDARKT PWSLLASLSS NGTASGQLYL DDGESVYPED 

       910        920        930        940        950        960 
TLSVDFLASR STLRASARGT WKEANPLANV TVLGVTEKPS SVTLNGETLS SDSVKYNATS 

       970        980 
HVLHVGGLQK HTADGAWAKD WVLKW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and expression of alpha-glucosidase-encoding gene (agdA) from Aspergillus oryzae." Minetoki T., Gomi K., Kitamoto K., Kumagai C., Tamura G. Biosci. Biotechnol. Biochem. 59:1516-1521(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.
[2]	"Molecular cloning and characterization of a transcriptional activator gene, amyR, involved in the amylolytic gene expression in Aspergillus oryzae." Gomi K., Akeno T., Minetoki T., Ozeki K., Kumagai C., Okazaki N., Iimura Y. Biosci. Biotechnol. Biochem. 64:816-827(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.
[3]	"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. 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	D45179 Genomic DNA. Translation: BAA08125.1. AB021876 Genomic DNA. Translation: BAA95702.1. AP007155 Genomic DNA. Translation: BAE58289.1.
PIR	JC4217.
RefSeq	XP_001820291.1. XM_001820239.2.
3D structure databases
ProteinModelPortal	Q12558.
ModBase	Search...
Protein-protein interaction databases
STRING	5062.CADAORAP00001723.
Protein family/group databases
CAZy	GH31. Glycoside Hydrolase Family 31.
mycoCLAP	AGL31A_ASPOR.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAORAT00001748; CADAORAP00001723; CADAORAG00001748.
GeneID	5992274.
KEGG	aor:AOR_1_2146154.
Phylogenomic databases
eggNOG	COG1501.
HOGENOM	HOG000041175.
KO	K01187.
OrthoDB	EOG4J40R4.
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...

Entry information

Entry name

AGLU_ASPOR

Accession

Primary (citable) accession number: Q12558
Secondary accession number(s): Q7LWA9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 71 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

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