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P69328

- AMYG_ASPNG

UniProt

P69328 - AMYG_ASPNG

Protein

Glucoamylase

Gene

GLAA

Organism
Aspergillus niger
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 63 (01 Oct 2014)
      Sequence version 1 (01 Nov 1986)
      Previous versions | rss
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    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

    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: P69328-1) [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. 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