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P69327

- AMYG_ASPAW

UniProt

P69327 - AMYG_ASPAW

Protein

Glucoamylase

Gene

GLAA

Organism
Aspergillus awamori (Black koji mold)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 62 (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 – 1441Substrate
    Active sitei200 – 2001Proton acceptor1 PublicationPROSITE-ProRule annotation
    Active sitei203 – 2031Proton donor1 PublicationPROSITE-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

    Protein family/group databases

    mycoCLAPiGLA15A_ASPAW.

    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 awamori (Black koji mold)
    Taxonomic identifieri105351 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi144 – 1441W → Y: 2% of wild-type activity. 3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Propeptidei19 – 246PRO_0000001459
    Chaini25 – 640616GlucoamylasePRO_0000001460Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi195 – 1951N-linked (GlcNAc...)CAR_000112
    Disulfide bondi234 ↔ 2371 Publication
    Disulfide bondi246 ↔ 4731 Publication
    Disulfide bondi286 ↔ 2941 Publication
    Glycosylationi419 – 4191N-linked (GlcNAc...)CAR_000113
    Glycosylationi465 – 4651O-linked (Man)By similarity
    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)
    Glycosylationi492 – 4921O-linked (Man)By similarity
    Glycosylationi496 – 4961O-linked (Man)By similarity
    Glycosylationi499 – 4991O-linked (Man)By similarity
    Glycosylationi500 – 5001O-linked (Man)By similarity
    Glycosylationi501 – 5011O-linked (Man)By similarity
    Glycosylationi502 – 5021O-linked (Man)By similarity
    Glycosylationi504 – 5041O-linked (Man)By similarity
    Glycosylationi506 – 5061O-linked (Man)By similarity
    Glycosylationi508 – 5081O-linked (Man)By similarity
    Glycosylationi510 – 5101O-linked (Man)By similarity
    Glycosylationi512 – 5121O-linked (Man)By similarity
    Glycosylationi513 – 5131O-linked (Man)By similarity
    Glycosylationi514 – 5141O-linked (Man)By similarity
    Glycosylationi515 – 5151O-linked (Man)By similarity
    Glycosylationi517 – 5171O-linked (Man)By similarity
    Glycosylationi518 – 5181O-linked (Man)By similarity
    Glycosylationi520 – 5201O-linked (Man)By similarity
    Glycosylationi522 – 5221O-linked (Man)By similarity
    Glycosylationi524 – 5241O-linked (Man)By similarity
    Glycosylationi525 – 5251O-linked (Man)By similarity
    Glycosylationi526 – 5261O-linked (Man)By similarity
    Glycosylationi527 – 5271O-linked (Man)By similarity
    Glycosylationi528 – 5281O-linked (Man)By similarity
    Glycosylationi529 – 5291O-linked (Man)By similarity
    Glycosylationi530 – 5301O-linked (Man)By similarity
    Glycosylationi531 – 5311O-linked (Man)By similarity
    Glycosylationi532 – 5321O-linked (Man)By similarity
    Glycosylationi534 – 5341O-linked (Man)By similarity
    Glycosylationi535 – 5351O-linked (Man)By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    PTM databases

    UniCarbKBiP69327.

    Interactioni

    Structurei

    Secondary structure

    1
    640
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi26 – 4419
    Turni47 – 493
    Beta strandi67 – 715
    Beta strandi74 – 763
    Helixi77 – 9216
    Helixi96 – 983
    Helixi99 – 11416
    Turni122 – 1254
    Helixi127 – 1293
    Helixi150 – 16819
    Helixi172 – 1776
    Helixi179 – 19315
    Beta strandi206 – 2094
    Helixi210 – 22920
    Helixi235 – 24814
    Helixi249 – 2513
    Beta strandi254 – 2574
    Beta strandi259 – 2624
    Helixi271 – 2777
    Turni288 – 2914
    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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AGMX-ray2.30A25-495[»]
    1DOGX-ray2.30A25-495[»]
    1GAHX-ray2.00A25-496[»]
    1GAIX-ray1.70A25-497[»]
    1GLMX-ray2.40A25-495[»]
    3GLYX-ray2.20A25-495[»]
    ProteinModelPortaliP69327.
    SMRiP69327. Positions 25-640.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP69327.

    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

    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: P69327-1) [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: P69327-2) [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. 1 PublicationVSP_012836
    Alternative sequencei535 – 640106Missing in isoform G2. 1 PublicationVSP_000262Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02465 mRNA. Translation: AAB59296.1.
    K02465 mRNA. Translation: AAB59297.1.
    PIRiA29166.
    A93066. A29776.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02465 mRNA. Translation: AAB59296.1 .
    K02465 mRNA. Translation: AAB59297.1 .
    PIRi A29166.
    A93066. A29776.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AGM X-ray 2.30 A 25-495 [» ]
    1DOG X-ray 2.30 A 25-495 [» ]
    1GAH X-ray 2.00 A 25-496 [» ]
    1GAI X-ray 1.70 A 25-497 [» ]
    1GLM X-ray 2.40 A 25-495 [» ]
    3GLY X-ray 2.20 A 25-495 [» ]
    ProteinModelPortali P69327.
    SMRi P69327. Positions 25-640.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P69327.

    Protein family/group databases

    mycoCLAPi GLA15A_ASPAW.

    PTM databases

    UniCarbKBi P69327.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P69327.

    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. "Molecular cloning and characterization of the glucoamylase gene of Aspergillus awamori."
      Nunberg J.H., Meade J.H., Cole G., Lawyer F.C., McCabe P., Schweickart V., Tal R., Wittman V.P., Flatgaard J.E., Innis M.A.
      Mol. Cell. Biol. 4:2306-2315(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS G1 AND G2).
    2. Nunberg J.H., Meade J.H., Cole G., Lawyer F.C., McCabe P., Schweickart V., Tal R., Wittman V.P., Flatgaard J.E., Innis M.A.
      Submitted (FEB-1985) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori."
      Sierks M.R., Ford C., Reilly P.J., Svensson B.
      Protein Eng. 3:193-198(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITES, MUTAGENESIS.
    4. "Site-directed mutagenesis at the active site Trp120 of Aspergillus awamori glucoamylase."
      Sierks M.R., Ford C., Reilly P.J., Svensson B.
      Protein Eng. 2:621-625(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TRP-144.
    5. "Functional roles and subsite locations of Leu177, Trp178 and Asn182 of Aspergillus awamori glucoamylase determined by site-directed mutagenesis."
      Sierks M.R., Ford C., Reilly P.J., Svensson B.
      Protein Eng. 6:75-79(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    6. "Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2.2-A resolution."
      Aleshin A., Golubev A., Firsov L.M., Honzatko R.B.
      J. Biol. Chem. 267:19291-19298(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-495, GLYCOSYLATION, DISULFIDE BONDS.
      Strain: Var. X100.
    7. "Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. X100 to 2.4-A resolution."
      Aleshin A., Firsov L.M., Honzatko R.B.
      J. Biol. Chem. 269:15631-15639(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 25-495.
      Strain: Var. X100.
    8. "Refined crystal structures of glucoamylase from Aspergillus awamori var. X100."
      Aleshin A., Hoffman C., Firsov L.M., Honzatko R.B.
      J. Mol. Biol. 238:575-591(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-495, GLYCOSYLATION.
      Strain: Var. X100.

    Entry informationi

    Entry nameiAMYG_ASPAW
    AccessioniPrimary (citable) accession number: P69327
    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 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

    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