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P56526

- AGLU_ASPNG

UniProt

P56526 - AGLU_ASPNG

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Protein

Alpha-glucosidase

Gene

aglA

Organism
Aspergillus niger
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei490 – 4901Nucleophile
Active sitei493 – 4931By similarity
Active sitei660 – 6601Proton donorBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 PublicationAdd
BLAST
Chaini26 – 985960Alpha-glucosidasePRO_0000018576Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi36 – 361O-linked (Man)1 Publication
Glycosylationi124 – 1241N-linked (GlcNAc...)1 Publication
Glycosylationi143 – 1431N-linked (GlcNAc...)1 Publication
Glycosylationi218 – 2181N-linked (GlcNAc...)1 Publication
Glycosylationi347 – 3471N-linked (GlcNAc...)1 Publication
Glycosylationi422 – 4221N-linked (GlcNAc...)1 Publication
Glycosylationi506 – 5061N-linked (GlcNAc...)1 Publication
Glycosylationi534 – 5341N-linked (GlcNAc...)1 Publication
Glycosylationi537 – 5371N-linked (GlcNAc...)
Glycosylationi545 – 5451O-linked (Man)1 Publication
Glycosylationi550 – 5501O-linked (Man)1 Publication
Glycosylationi559 – 5591O-linked (Man)1 Publication
Glycosylationi560 – 5601O-linked (Man)1 Publication
Glycosylationi561 – 5611O-linked (Man)1 Publication
Glycosylationi562 – 5621O-linked (Man)1 Publication
Glycosylationi571 – 5711O-linked (Man)1 Publication
Glycosylationi601 – 6011N-linked (GlcNAc...)1 Publication
Glycosylationi623 – 6231N-linked (GlcNAc...)1 Publication
Glycosylationi835 – 8351N-linked (GlcNAc...)1 Publication
Glycosylationi881 – 8811N-linked (GlcNAc...)1 Publication
Glycosylationi895 – 8951O-linked (Man)1 Publication
Glycosylationi899 – 8991N-linked (GlcNAc...)1 Publication
Glycosylationi957 – 9571N-linked (GlcNAc...)1 Publication
Glycosylationi970 – 9701N-linked (GlcNAc...)1 Publication

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein

PTM databases

UniCarbKBiP56526.

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00004308.

Structurei

3D structure databases

ProteinModelPortaliP56526.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 31 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1501.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti27 – 282TT → LL in strain: GN-8.
Natural varianti42 – 421D → A in strain: GN-8.
Natural varianti929 – 9291N → M in strain: GN-8.

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 .
PIRi JC1199.
JC1200.
JC5561.

3D structure databases

ProteinModelPortali P56526.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5061.CADANGAP00004308.

Chemistry

BindingDBi P56526.
ChEMBLi CHEMBL3435.

Protein family/group databases

CAZyi GH31. Glycoside Hydrolase Family 31.
mycoCLAPi AGL31A_ASPNG.

PTM databases

UniCarbKBi P56526.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG1501.

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

  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.

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 26, 2014
This is version 69 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

External Data

Dasty 3