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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 – 1441Substrate By similarity
Active sitei200 – 2001Proton acceptor By similarity
Active sitei203 – 2031Proton donor By similarity

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 – 1818 Reviewed prediction
Add
BLAST
Propeptidei19 – 246
PRO_0000001461
Chaini25 – 640616Glucoamylase
PRO_0000001462Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Interactioni

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP69328.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini533 – 640108CBM20
Add
BLAST

Sequence similaritiesi

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: P69328-1) [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

MSFRSLLALS GLVCTGLANV ISKRATLDSW LSNEATVART AILNNIGADG    50
AWVSGADSGI VVASPSTDNP DYFYTWTRDS GLVLKTLVDL FRNGDTSLLS 100
TIENYISAQA IVQGISNPSG DLSSGAGLGE PKFNVDETAY TGSWGRPQRD 150
GPALRATAMI GFGQWLLDNG YTSTATDIVW PLVRNDLSYV AQYWNQTGYD 200
LWEEVNGSSF FTIAVQHRAL VEGSAFATAV GSSCSWCDSQ APEILCYLQS 250
FWTGSFILAN FDSSRSGKDA NTLLGSIHTF DPEAACDDST FQPCSPRALA 300
NHKEVVDSFR SIYTLNDGLS DSEAVAVGRY PEDTYYNGNP WFLCTLAAAE 350
QLYDALYQWD KQGSLEVTDV SLDFFKALYS DAATGTYSSS SSTYSSIVDA 400
VKTFADGFVS IVETHAASNG SMSEQYDKSD GEQLSARDLT WSYAALLTAN 450
NRRNSVVPAS WGETSASSVP GTCAATSAIG TYSSVTVTSW PSIVATGGTT 500
TTATPTGSGS VTSTSKTTAT ASKTSTSTSS TSCTTPTAVA VTFDLTATTT 550
YGENIYLVGS ISQLGDWETS DGIALSADKY TSSDPLWYVT VTLPAGESFE 600
YKFIRIESDD SVEWESDPNR EYTVPQACGT STATVTDTWR 640
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.
VSP_012837
Alternative sequencei535 – 640106Missing in isoform G2.
VSP_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: June 11, 2014
This is version 62 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

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