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Q12558

- AGLU_ASPOR

UniProt

Q12558 - AGLU_ASPOR

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Protein

Alpha-glucosidase

Gene

agdA

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Hydrolyzes malto-oligosaccharides, but has a low activity toward soluble starch.

Catalytic activityi

Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei492 – 4921NucleophilePROSITE-ProRule annotation
Active sitei495 – 4951By similarity
Active sitei660 – 6601Proton donorBy similarity

GO - Molecular functioni

  1. alpha-1,4-glucosidase activity Source: ASPGD
  2. carbohydrate binding Source: InterPro
  3. glucosyltransferase activity Source: ASPGD
  4. maltose alpha-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular polysaccharide metabolic process Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.
mycoCLAPiAGL31A_ASPOR.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-glucosidase (EC:3.2.1.20)
Short name:
AGL
Alternative name(s):
Maltase
Gene namesi
Name:agdA
ORF Names:AO090003001209
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564: Chromosome 2

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525By similarityAdd
BLAST
Chaini26 – 985960Alpha-glucosidasePRO_0000018577Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi220 – 2201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi255 – 2551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi349 – 3491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi424 – 4241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi508 – 5081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi536 – 5361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi539 – 5391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi602 – 6021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi624 – 6241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi661 – 6611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi835 – 8351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi881 – 8811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi929 – 9291N-linked (GlcNAc...)Sequence Analysis
Glycosylationi957 – 9571N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Expressioni

Inductioni

By maltose.

Interactioni

Protein-protein interaction databases

STRINGi5062.CADAORAP00001723.

Structurei

3D structure databases

ProteinModelPortaliQ12558.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 31 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1501.
HOGENOMiHOG000041175.
KOiK01187.
OMAiYDYPEGF.
OrthoDBiEOG77T1CZ.

Family and domain databases

InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 2 hits.
PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q12558-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGLKSFLAS SWLLPVACGA SQSIVPSTSA TAAYSQFTIP ASADVGANLV
60 70 80 90 100
ANIDDPQAVN AQSVCPGYKA SDVKHSSQGF TASLELAGDP CNVYGTDVDS
110 120 130 140 150
LTLTVEYQAK DRLNIQIVPT YFDASNASWY ILSEELVPRP KASQNASVPQ
160 170 180 190 200
SDFVVSWSNE PSFNFKVIRK ATGDVLFNTK GSTLVYENQF IEFVTLLPEE
210 220 230 240 250
YNLYGLGERM NQLRLLENAN LTLYAADIAD PIDDNIYGHH AFYLDTRYYK
260 270 280 290 300
VGGQNKSHTI VKSSEAEPSQ EYVSYSHGVF LRNAHGQEIL LRDQKLIWRT
310 320 330 340 350
LGGSVDLTFY SGPTQAEVTK QYQLSTVGLP AMQQYNTLGF HQCRWGYNNW
360 370 380 390 400
SEFEDVLANF ERFEIPLEYL WADIDYMHGY RNFDNDQHRF SYEEGEKFLN
410 420 430 440 450
KLHAGGRRWV PIVDGALYIP NPENASDAYE TYDRGAKDDV FIKNPDGSLY
460 470 480 490 500
IGAVWPGYTV YPDWHHPKAS DFWANELVTW WNKLHYDGVW YDMAEVSSFC
510 520 530 540 550
VGSCGTGNLS MNPAHPPFAL PGEPGNVVYD YPEGFNITNA TEAASASAGA
560 570 580 590 600
ASQSAAASST TTSAPYLRTT PTPGVRNVDH PPYVINHVQP GHDLSVHAIS
610 620 630 640 650
PNSTHSDGVQ EYDVHSLYGH QGINATYHGL LKVWENKRPF IIARSTFSGS
660 670 680 690 700
GKWAGHWGGD NFSKWGSMFF SISQALQFSL FGIPMFGVDT CGFNGNTDEE
710 720 730 740 750
LCNRWMQLSA FFPFYRNHNV LSAIPQEPYR WASVIDATKA AMNIRYAILP
760 770 780 790 800
YFYTLFHLAH TTGSTVMRAL AWEFPNDPSL AAVGTQFLVG PSVMVIPVLE
810 820 830 840 850
PQVDTVQGVF PGVGHGEVWY DWYSQTAVDA KPGVNTTISA PLGHIPVFVR
860 870 880 890 900
GGSILPMQEV ALTTRDARKT PWSLLASLSS NGTASGQLYL DDGESVYPED
910 920 930 940 950
TLSVDFLASR STLRASARGT WKEANPLANV TVLGVTEKPS SVTLNGETLS
960 970 980
SDSVKYNATS HVLHVGGLQK HTADGAWAKD WVLKW
Length:985
Mass (Da):108,704
Last modified:November 1, 1996 - v1
Checksum:i3E9EAE0A0E38209E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45179 Genomic DNA. Translation: BAA08125.1.
AB021876 Genomic DNA. Translation: BAA95702.1.
AP007155 Genomic DNA. Translation: BAE58289.1.
PIRiJC4217.
RefSeqiXP_001820291.1. XM_001820239.2.

Genome annotation databases

EnsemblFungiiCADAORAT00001748; CADAORAP00001723; CADAORAG00001748.
GeneIDi5992274.
KEGGiaor:AOR_1_2146154.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45179 Genomic DNA. Translation: BAA08125.1 .
AB021876 Genomic DNA. Translation: BAA95702.1 .
AP007155 Genomic DNA. Translation: BAE58289.1 .
PIRi JC4217.
RefSeqi XP_001820291.1. XM_001820239.2.

3D structure databases

ProteinModelPortali Q12558.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5062.CADAORAP00001723.

Protein family/group databases

CAZyi GH31. Glycoside Hydrolase Family 31.
mycoCLAPi AGL31A_ASPOR.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAORAT00001748 ; CADAORAP00001723 ; CADAORAG00001748 .
GeneIDi 5992274.
KEGGi aor:AOR_1_2146154.

Phylogenomic databases

eggNOGi COG1501.
HOGENOMi HOG000041175.
KOi K01187.
OMAi YDYPEGF.
OrthoDBi EOG77T1CZ.

Family and domain databases

InterProi IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF01055. Glyco_hydro_31. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 2 hits.
PROSITEi PS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry nameiAGLU_ASPOR
AccessioniPrimary (citable) accession number: Q12558
Secondary accession number(s): Q7LWA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3