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P69328

- AMYG_ASPNG

UniProt

P69328 - AMYG_ASPNG

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Protein

Glucoamylase

Gene

GLAA

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei144 – 1441SubstrateBy similarity
Active sitei200 – 2001Proton acceptorPROSITE-ProRule annotation
Active sitei203 – 2031Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

  1. glucan 1,4-alpha-glucosidase activity Source: UniProtKB-EC
  2. starch binding Source: InterPro

GO - Biological processi

  1. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

BRENDAi3.2.1.3. 518.

Protein family/group databases

CAZyiCBM20. Carbohydrate-Binding Module Family 20.
GH15. Glycoside Hydrolase Family 15.
mycoCLAPiGLA15A_ASPNG.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucoamylase (EC:3.2.1.3)
Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase
Gene namesi
Name:GLAA
OrganismiAspergillus niger
Taxonomic identifieri5061 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Pathology & Biotechi

Protein family/group databases

Allergomei914. Asp n Glucoamylase.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Propeptidei19 – 2461 PublicationPRO_0000001461
Chaini25 – 640616GlucoamylasePRO_0000001462Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi195 – 1951N-linked (GlcNAc...)By similarity
Disulfide bondi234 ↔ 237By similarity
Disulfide bondi246 ↔ 473By similarity
Disulfide bondi286 ↔ 294By similarity
Glycosylationi419 – 4191N-linked (GlcNAc...)By similarity
Glycosylationi465 – 4651O-linked (Man)1 Publication
Glycosylationi467 – 4671O-linked (Man)1 Publication
Glycosylationi468 – 4681O-linked (Man)1 Publication
Glycosylationi476 – 4761O-linked (Man)1 Publication
Glycosylationi477 – 4771O-linked (Man)1 Publication
Glycosylationi483 – 4831O-linked (Man)1 Publication
Glycosylationi484 – 4841O-linked (Man)1 Publication
Glycosylationi486 – 4861O-linked (Man)1 Publication
Glycosylationi488 – 4881O-linked (Man)1 Publication
Glycosylationi489 – 4891O-linked (Man)1 Publication
Glycosylationi492 – 4921O-linked (Man)1 Publication
Glycosylationi496 – 4961O-linked (Man)1 Publication
Glycosylationi499 – 4991O-linked (Man)1 Publication
Glycosylationi500 – 5001O-linked (Man)1 Publication
Glycosylationi501 – 5011O-linked (Man)1 Publication
Glycosylationi502 – 5021O-linked (Man)1 Publication
Glycosylationi504 – 5041O-linked (Man)1 Publication
Glycosylationi506 – 5061O-linked (Man)1 Publication
Glycosylationi508 – 5081O-linked (Man)1 Publication
Glycosylationi510 – 5101O-linked (Man)1 Publication
Glycosylationi512 – 5121O-linked (Man)1 Publication
Glycosylationi513 – 5131O-linked (Man)1 Publication
Glycosylationi514 – 5141O-linked (Man)1 Publication
Glycosylationi515 – 5151O-linked (Man)1 Publication
Glycosylationi517 – 5171O-linked (Man)1 Publication
Glycosylationi518 – 5181O-linked (Man)1 Publication
Glycosylationi520 – 5201O-linked (Man)1 Publication
Glycosylationi522 – 5221O-linked (Man)1 Publication
Glycosylationi524 – 5241O-linked (Man)1 Publication
Glycosylationi525 – 5251O-linked (Man)1 Publication
Glycosylationi526 – 5261O-linked (Man)1 Publication
Glycosylationi527 – 5271O-linked (Man)1 Publication
Glycosylationi528 – 5281O-linked (Man)1 Publication
Glycosylationi529 – 5291O-linked (Man)1 Publication
Glycosylationi530 – 5301O-linked (Man)1 Publication
Glycosylationi531 – 5311O-linked (Man)1 Publication
Glycosylationi532 – 5321O-linked (Man)1 Publication
Glycosylationi534 – 5341O-linked (Man)1 Publication
Glycosylationi535 – 5351O-linked (Man)1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Interactioni

Structurei

Secondary structure

1
640
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 4414
Turni47 – 493
Beta strandi67 – 715
Beta strandi74 – 763
Helixi77 – 9216
Helixi96 – 983
Helixi99 – 11214
Turni122 – 1243
Helixi126 – 1294
Beta strandi132 – 1343
Turni135 – 1373
Helixi150 – 16819
Helixi172 – 1776
Helixi179 – 19315
Beta strandi206 – 2094
Helixi210 – 22920
Helixi235 – 24814
Helixi249 – 2513
Beta strandi254 – 2574
Helixi270 – 2789
Helixi288 – 2903
Helixi296 – 30712
Turni308 – 3125
Helixi314 – 3163
Helixi335 – 3373
Helixi342 – 36221
Beta strandi364 – 3674
Turni369 – 3713
Helixi372 – 3787
Beta strandi384 – 3885
Helixi392 – 41524
Beta strandi424 – 4263
Turni428 – 4303
Beta strandi433 – 4386
Helixi440 – 45314
Helixi463 – 4653
Turni535 – 5373
Beta strandi541 – 5466
Beta strandi554 – 5563
Beta strandi560 – 5623
Beta strandi566 – 5683
Helixi569 – 5713
Beta strandi572 – 5743
Beta strandi578 – 5836
Beta strandi588 – 5914
Beta strandi595 – 5973
Beta strandi604 – 6063
Beta strandi608 – 6103
Beta strandi612 – 6143
Beta strandi620 – 6234
Beta strandi626 – 6294
Beta strandi634 – 6385

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AC0NMR-A533-640[»]
1ACZNMR-A533-640[»]
1KULNMR-A533-640[»]
1KUMNMR-A533-640[»]
3EQAX-ray1.90A25-494[»]
ProteinModelPortaliP69328.
SMRiP69328. Positions 25-640.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69328.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini533 – 640108CBM20PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 15 family.Curated
Contains 1 CBM20 (carbohydrate binding type-20) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3387.

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
2.60.40.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR000165. Glucoamylase.
IPR008291. Glucoamylase_SBD.
IPR011613. Glyco_hydro_15.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00686. CBM_20. 1 hit.
PF00723. Glyco_hydro_15. 1 hit.
[Graphical view]
PIRSFiPIRSF001031. Glu-a-glcsd_SBD. 1 hit.
PRINTSiPR00736. GLHYDRLASE15.
SMARTiSM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF49452. SSF49452. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
PS00820. GLUCOAMYLASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform G1 (identifier: P69328) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSFRSLLALS GLVCTGLANV ISKRATLDSW LSNEATVART AILNNIGADG
60 70 80 90 100
AWVSGADSGI VVASPSTDNP DYFYTWTRDS GLVLKTLVDL FRNGDTSLLS
110 120 130 140 150
TIENYISAQA IVQGISNPSG DLSSGAGLGE PKFNVDETAY TGSWGRPQRD
160 170 180 190 200
GPALRATAMI GFGQWLLDNG YTSTATDIVW PLVRNDLSYV AQYWNQTGYD
210 220 230 240 250
LWEEVNGSSF FTIAVQHRAL VEGSAFATAV GSSCSWCDSQ APEILCYLQS
260 270 280 290 300
FWTGSFILAN FDSSRSGKDA NTLLGSIHTF DPEAACDDST FQPCSPRALA
310 320 330 340 350
NHKEVVDSFR SIYTLNDGLS DSEAVAVGRY PEDTYYNGNP WFLCTLAAAE
360 370 380 390 400
QLYDALYQWD KQGSLEVTDV SLDFFKALYS DAATGTYSSS SSTYSSIVDA
410 420 430 440 450
VKTFADGFVS IVETHAASNG SMSEQYDKSD GEQLSARDLT WSYAALLTAN
460 470 480 490 500
NRRNSVVPAS WGETSASSVP GTCAATSAIG TYSSVTVTSW PSIVATGGTT
510 520 530 540 550
TTATPTGSGS VTSTSKTTAT ASKTSTSTSS TSCTTPTAVA VTFDLTATTT
560 570 580 590 600
YGENIYLVGS ISQLGDWETS DGIALSADKY TSSDPLWYVT VTLPAGESFE
610 620 630 640
YKFIRIESDD SVEWESDPNR EYTVPQACGT STATVTDTWR
Length:640
Mass (Da):68,309
Last modified:November 1, 1986 - v1
Checksum:i26F58DD18AD7F702
GO
Isoform G2 (identifier: P69328-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     527-534: STSSTSCT → TTRSGMSL
     535-640: Missing.

Show »
Length:534
Mass (Da):56,730
Checksum:i94D188E946D0C12E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei527 – 5348STSSTSCT → TTRSGMSL in isoform G2. CuratedVSP_012837
Alternative sequencei535 – 640106Missing in isoform G2. CuratedVSP_012838Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00548 mRNA. Translation: CAA25219.1.
X00712 Genomic DNA. Translation: CAA25303.1.
X00712 Genomic DNA. Translation: CAA25304.1.
X56442 Genomic DNA. Translation: CAA39825.1.
PIRiA90986. ALASGR.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00548 mRNA. Translation: CAA25219.1 .
X00712 Genomic DNA. Translation: CAA25303.1 .
X00712 Genomic DNA. Translation: CAA25304.1 .
X56442 Genomic DNA. Translation: CAA39825.1 .
PIRi A90986. ALASGR.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AC0 NMR - A 533-640 [» ]
1ACZ NMR - A 533-640 [» ]
1KUL NMR - A 533-640 [» ]
1KUM NMR - A 533-640 [» ]
3EQA X-ray 1.90 A 25-494 [» ]
ProteinModelPortali P69328.
SMRi P69328. Positions 25-640.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P69328.
ChEMBLi CHEMBL3745.

Protein family/group databases

Allergomei 914. Asp n Glucoamylase.
CAZyi CBM20. Carbohydrate-Binding Module Family 20.
GH15. Glycoside Hydrolase Family 15.
mycoCLAPi GLA15A_ASPNG.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG3387.

Enzyme and pathway databases

BRENDAi 3.2.1.3. 518.

Miscellaneous databases

EvolutionaryTracei P69328.

Family and domain databases

Gene3Di 1.50.10.10. 1 hit.
2.60.40.10. 1 hit.
InterProi IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR000165. Glucoamylase.
IPR008291. Glucoamylase_SBD.
IPR011613. Glyco_hydro_15.
IPR013783. Ig-like_fold.
[Graphical view ]
Pfami PF00686. CBM_20. 1 hit.
PF00723. Glyco_hydro_15. 1 hit.
[Graphical view ]
PIRSFi PIRSF001031. Glu-a-glcsd_SBD. 1 hit.
PRINTSi PR00736. GLHYDRLASE15.
SMARTi SM01065. CBM_2. 1 hit.
[Graphical view ]
SUPFAMi SSF48208. SSF48208. 1 hit.
SSF49452. SSF49452. 1 hit.
PROSITEi PS51166. CBM20. 1 hit.
PS00820. GLUCOAMYLASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Two different types of intervening sequences in the glucoamylase gene from Aspergillus niger."
    Boel E., Hansen M.T., Hjort I., Hoegh I., Fiil N.P.
    EMBO J. 3:1581-1585(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS G1 AND G2).
  2. "Glucoamylases G1 and G2 from Aspergillus niger are synthesized from two different but closely related mRNAs."
    Boel E., Hjort I., Svensson B., Norris F., Norris K.E., Fiil N.P.
    EMBO J. 3:1097-1102(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS G1 AND G2).
  3. "Characterization of a glucoamylase G2 from Aspergillus niger."
    Svensson B., Larsen K., Gunnarsson A.
    Eur. J. Biochem. 154:497-502(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-640, COMPARISON OF FORMS G1 AND G2.
  4. "The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger."
    Svensson B., Larsen K., Svendsen I., Boel E.
    Carlsberg Res. Commun. 48:529-544(1983)
    Cited for: PROTEIN SEQUENCE OF 25-640 (ISOFORM G1), GLYCOSYLATION.
  5. "Regulation of the glaA gene of Aspergillus niger."
    Fowler T., Berka R.M., Ward M.
    Curr. Genet. 18:537-545(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 1-11.
    Strain: ATCC 10864 / NRRL 330 / CBS 122.49 / IFO 6661.
  6. "O-glycosylation in Aspergillus glucoamylase. Conformation and role in binding."
    Williamson G., Belshaw N.J., Williamson M.P.
    Biochem. J. 282:423-428(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CONFORMATION OF O-GLYCOSYLATED REGION.
  7. "Production, purification and characterization of the catalytic domain of glucoamylase from Aspergillus niger."
    Stoffer B., Frandsen T.P., Busk P.K., Schneider P., Svendsen I., Svensson B.
    Biochem. J. 292:197-202(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF CATALYTIC DOMAIN.
  8. "Solution structure of the granular starch binding domain of glucoamylase from Aspergillus niger by nuclear magnetic resonance spectroscopy."
    Sorimachi K., Jacks A.J., le Gal-Coeffet M.-F., Williamson G., Archer D.B., Williamson M.P.
    J. Mol. Biol. 259:970-987(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 533-640.
  9. "Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin."
    Sorimachi K., le Gal-Coeffet M.-F., Williamson G., Archer D.B., Williamson M.P.
    Structure 5:647-661(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 533-640.

Entry informationi

Entry nameiAMYG_ASPNG
AccessioniPrimary (citable) accession number: P69328
Secondary accession number(s): P04064, Q92201, Q99179
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: October 1, 2014
This is version 63 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

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3