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P69327

- AMYG_ASPAW

UniProt

P69327 - AMYG_ASPAW

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Protein

Glucoamylase

Gene

GLAA

Organism
Aspergillus awamori (Black koji mold)
Status
Reviewed - Annotation score: 5 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
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
Complete GO annotation...

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. 1 Publication

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

        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: 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 29, 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

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