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Protein

Alpha-glucosidase

Gene

aglA

Organism
Aspergillus niger
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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)DescriptionActionsGraphical viewLength
Active sitei490Nucleophile1
Active sitei493By similarity1
Active sitei660Proton donorBy similarity1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.20. 518.

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.
mycoCLAPiAGL31A_ASPNG.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-glucosidase (EC:3.2.1.20)
Alternative name(s):
Maltase
Gene namesi
Name:aglA
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3435.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 251 PublicationAdd BLAST25
ChainiPRO_000001857626 – 985Alpha-glucosidaseAdd BLAST960

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi36O-linked (Man)1 Publication1
Glycosylationi124N-linked (GlcNAc...)1 Publication1
Glycosylationi143N-linked (GlcNAc...)1 Publication1
Glycosylationi218N-linked (GlcNAc...)1 Publication1
Glycosylationi347N-linked (GlcNAc...)1 Publication1
Glycosylationi422N-linked (GlcNAc...)1 Publication1
Glycosylationi506N-linked (GlcNAc...)1 Publication1
Glycosylationi534N-linked (GlcNAc...)1 Publication1
Glycosylationi537N-linked (GlcNAc...)1
Glycosylationi545O-linked (Man)1 Publication1
Glycosylationi550O-linked (Man)1 Publication1
Glycosylationi559O-linked (Man)1 Publication1
Glycosylationi560O-linked (Man)1 Publication1
Glycosylationi561O-linked (Man)1 Publication1
Glycosylationi562O-linked (Man)1 Publication1
Glycosylationi571O-linked (Man)1 Publication1
Glycosylationi601N-linked (GlcNAc...)1 Publication1
Glycosylationi623N-linked (GlcNAc...)1 Publication1
Glycosylationi835N-linked (GlcNAc...)1 Publication1
Glycosylationi881N-linked (GlcNAc...)1 Publication1
Glycosylationi895O-linked (Man)1 Publication1
Glycosylationi899N-linked (GlcNAc...)1 Publication1
Glycosylationi957N-linked (GlcNAc...)1 Publication1
Glycosylationi970N-linked (GlcNAc...)1 Publication1

Post-translational modificationi

The O-linked saccharide is not identified, but is probably mannose.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP56526.

PTM databases

UniCarbKBiP56526.

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00004308.

Chemistry databases

BindingDBiP56526.

Structurei

3D structure databases

ProteinModelPortaliP56526.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 31 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1065. Eukaryota.
COG1501. LUCA.

Family and domain databases

InterProiIPR031727. Gal_mutarotase_N.
IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR030458. Glyco_hydro_31_AS.
IPR030459. Glyco_hydro_31_CS.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01055. Glyco_hydro_31. 1 hit.
PF16863. NtCtMGAM_N. 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.

P56526-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKLTHLLAR AWLVPLAYGA SQSLLSTTAP SQPQFTIPAS ADVGAQLIAN
60 70 80 90 100
IDDPQAADAQ SVCPGYKASK VQHNSRGFTA SLQLAGRPCN VYGTDVESLT
110 120 130 140 150
LSVEYQDSDR LNIQILPTHV DSTNASWYFL SENLVPRPKA SLNASVSQSD
160 170 180 190 200
LFVSWSNEPS FNFKVIRKAT GDALFSTEGT VLVYENQFIE FVTALPEEYN
210 220 230 240 250
LYGLGEHITQ FRLQRNANLT IYPSDDGTPI DQNLYGQHPF YLDTRYYKGD
260 270 280 290 300
RQNGSYIPVK SSEADASQDY ISLSHGVFLR NSHGLEILLR SQKLIWRTLG
310 320 330 340 350
GGIDLTFYSG PAPADVTRQY LTSTVGLPAM QQYNTLGFHQ CRWGYNNWSD
360 370 380 390 400
LADVVANFEK FEIPLEYIWT DIDYMHGYRN FDNDQHRFSY SEGDEFLSKL
410 420 430 440 450
HESGRYYVPI VDAALYIPNP ENASDAYATY DRGAADDVFL KNPDGSLYIG
460 470 480 490 500
AVWPGYTVFP DWHHPKAVDF WANELVIWSK KVAFDGVWYD MSEVSSFCVG
510 520 530 540 550
SCGTGNLTLN PAHPSFLLPG EPGDIIYDYP EAFNITNATE AASASAGASS
560 570 580 590 600
QAAATATTTS TSVSYLRTTP TPGVRNVEHP PYVINHDQEG HDLSVHAVSP
610 620 630 640 650
NATHVDGVEE YDVHGLYGHQ GLNATYQGLL EVWSHKRRPF IIGRSTFAGS
660 670 680 690 700
GKWAGHWGGD NYSKWWSMYY SISQALSFSL FGIPMFGADT CGFNGNSDEE
710 720 730 740 750
LCNRWMQLSA FFPFYRNHNE LSTIPQEPYR WASVIEATKS AMRIRYAILP
760 770 780 790 800
YFYTLFDLAH TTGSTVMRAL SWEFPNDPTL AAVETQFMVG PAIMVVPVLE
810 820 830 840 850
PLVNTVKGVF PGVGHGEVWY DWYTQAAVDA KPGVNTTISA PLGHIPVYVR
860 870 880 890 900
GGNILPMQEP ALTTREARQT PWALLAALGS NGTASGQLYL DDGESIYPNA
910 920 930 940 950
TLHVDFTASR SSLRSSAQGR WKERNPLANV TVLGVNKEPS AVTLNGQAVF
960 970 980
PGSVTYNSTS QVLFVGGLQN LTKGGAWAEN WVLEW
Length:985
Mass (Da):108,913
Last modified:July 15, 1998 - v1
Checksum:i9A18772AEB2E0927
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti27 – 28TT → LL in strain: GN-8. 2
Natural varianti42D → A in strain: GN-8. 1
Natural varianti929N → M in strain: GN-8. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45356 Genomic DNA. Translation: BAA23616.1.
PIRiJC1199.
JC1200.
JC5561.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45356 Genomic DNA. Translation: BAA23616.1.
PIRiJC1199.
JC1200.
JC5561.

3D structure databases

ProteinModelPortaliP56526.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5061.CADANGAP00004308.

Chemistry databases

BindingDBiP56526.
ChEMBLiCHEMBL3435.

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.
mycoCLAPiAGL31A_ASPNG.

PTM databases

UniCarbKBiP56526.

Proteomic databases

PaxDbiP56526.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1065. Eukaryota.
COG1501. LUCA.

Enzyme and pathway databases

BRENDAi3.2.1.20. 518.

Family and domain databases

InterProiIPR031727. Gal_mutarotase_N.
IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR030458. Glyco_hydro_31_AS.
IPR030459. Glyco_hydro_31_CS.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01055. Glyco_hydro_31. 1 hit.
PF16863. NtCtMGAM_N. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiAGLU_ASPNG
AccessioniPrimary (citable) accession number: P56526
Secondary accession number(s): O13451
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: November 30, 2016
This is version 74 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

Direct protein sequencing

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.