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Protein

Glucoamylase

Gene

GLAA

Organism
Aspergillus awamori (Black koji mold)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei144Substrate1
Active sitei200Proton acceptorPROSITE-ProRule annotation1 Publication1
Active sitei203Proton donorPROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

BRENDAi3.2.1.3. 494.

Protein family/group databases

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

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)DescriptionActionsGraphical viewLength
Mutagenesisi144W → Y: 2% of wild-type activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
PropeptideiPRO_000000145919 – 246
ChainiPRO_000000146025 – 640GlucoamylaseAdd BLAST616

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
GlycosylationiCAR_000112195N-linked (GlcNAc...)1
Disulfide bondi234 ↔ 2371 Publication
Disulfide bondi246 ↔ 4731 Publication
Disulfide bondi286 ↔ 2941 Publication
GlycosylationiCAR_000113419N-linked (GlcNAc...)1
Glycosylationi465O-linked (Man)By similarity1
Glycosylationi467O-linked (Man)1
Glycosylationi468O-linked (Man)1
Glycosylationi476O-linked (Man)1
Glycosylationi477O-linked (Man)1
Glycosylationi483O-linked (Man)1
Glycosylationi484O-linked (Man)1
Glycosylationi486O-linked (Man)1
Glycosylationi488O-linked (Man)1
Glycosylationi492O-linked (Man)By similarity1
Glycosylationi496O-linked (Man)By similarity1
Glycosylationi499O-linked (Man)By similarity1
Glycosylationi500O-linked (Man)By similarity1
Glycosylationi501O-linked (Man)By similarity1
Glycosylationi502O-linked (Man)By similarity1
Glycosylationi504O-linked (Man)By similarity1
Glycosylationi506O-linked (Man)By similarity1
Glycosylationi508O-linked (Man)By similarity1
Glycosylationi510O-linked (Man)By similarity1
Glycosylationi512O-linked (Man)By similarity1
Glycosylationi513O-linked (Man)By similarity1
Glycosylationi514O-linked (Man)By similarity1
Glycosylationi515O-linked (Man)By similarity1
Glycosylationi517O-linked (Man)By similarity1
Glycosylationi518O-linked (Man)By similarity1
Glycosylationi520O-linked (Man)By similarity1
Glycosylationi522O-linked (Man)By similarity1
Glycosylationi524O-linked (Man)By similarity1
Glycosylationi525O-linked (Man)By similarity1
Glycosylationi526O-linked (Man)By similarity1
Glycosylationi527O-linked (Man)By similarity1
Glycosylationi528O-linked (Man)By similarity1
Glycosylationi529O-linked (Man)By similarity1
Glycosylationi530O-linked (Man)By similarity1
Glycosylationi531O-linked (Man)By similarity1
Glycosylationi532O-linked (Man)By similarity1
Glycosylationi534O-linked (Man)By similarity1
Glycosylationi535O-linked (Man)By similarity1

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

PTM databases

UniCarbKBiP69327.

Structurei

Secondary structure

1640
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi26 – 44Combined sources19
Turni47 – 49Combined sources3
Beta strandi67 – 71Combined sources5
Beta strandi74 – 76Combined sources3
Helixi77 – 92Combined sources16
Helixi96 – 98Combined sources3
Helixi99 – 114Combined sources16
Turni122 – 125Combined sources4
Helixi127 – 129Combined sources3
Helixi150 – 168Combined sources19
Helixi172 – 177Combined sources6
Helixi179 – 193Combined sources15
Beta strandi206 – 209Combined sources4
Helixi210 – 229Combined sources20
Helixi235 – 248Combined sources14
Helixi249 – 251Combined sources3
Beta strandi254 – 257Combined sources4
Beta strandi259 – 262Combined sources4
Helixi271 – 277Combined sources7
Turni288 – 291Combined sources4
Helixi296 – 307Combined sources12
Turni308 – 312Combined sources5
Helixi314 – 316Combined sources3
Helixi335 – 337Combined sources3
Helixi342 – 362Combined sources21
Beta strandi364 – 367Combined sources4
Turni369 – 371Combined sources3
Helixi372 – 378Combined sources7
Beta strandi384 – 388Combined sources5
Helixi392 – 415Combined sources24
Beta strandi424 – 426Combined sources3
Turni428 – 430Combined sources3
Beta strandi433 – 438Combined sources6
Helixi440 – 453Combined sources14
Helixi463 – 465Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69327.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini533 – 640CBM20PROSITE-ProRule annotationAdd BLAST108

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/PHK.
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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_012836527 – 534STSSTSCT → TTRSGMSL in isoform G2. 1 Publication8
Alternative sequenceiVSP_000262535 – 640Missing in isoform G2. 1 PublicationAdd BLAST106

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
K02465 mRNA. Translation: AAB59296.1.
K02465 mRNA. Translation: AAB59297.1.
PIRiA29166.
A93066. A29776.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

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

PTM databases

UniCarbKBiP69327.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.3. 494.

Miscellaneous databases

EvolutionaryTraceiP69327.

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/PHK.
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]
ProtoNetiSearch...

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: November 2, 2016
This is version 74 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.