P69328 (AMYG_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glucoamylase
EC=3.2.1.3

Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase

Gene names

Name:

GLAA

Organism

Aspergillus niger

Taxonomic identifier

5061 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	640 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.
Sequence similarities	Belongs to the glycosyl hydrolase 15 family. Contains 1 CBM20 (carbohydrate binding type-20) domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation
Coding sequence diversity	Alternative splicing
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	glucan 1,4-alpha-glucosidase activity Inferred from electronic annotation. Source: EC starch binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform G1 (identifier: P69328-1)

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.

Isoform G2 (identifier: P69328-2)

The sequence of this isoform differs from the canonical sequence as follows:
     527-534: STSSTSCT → TTRSGMSL
     535-640: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Potential

Propeptide

19 – 24

6

PRO_0000001461

Chain

25 – 640

616

Glucoamylase

PRO_0000001462

Regions

Domain

533 – 640

108

CBM20

Sites

Active site

200

1

Proton acceptor By similarity

Active site

203

1

Proton donor By similarity

Binding site

144

1

Substrate By similarity

Amino acid modifications

Glycosylation

195

1

N-linked (GlcNAc...) By similarity

Glycosylation

419

1

N-linked (GlcNAc...) By similarity

Glycosylation

465

1

O-linked (Man)

Glycosylation

467

1

O-linked (Man)

Glycosylation

468

1

O-linked (Man)

Glycosylation

476

1

O-linked (Man)

Glycosylation

477

1

O-linked (Man)

Glycosylation

483

1

O-linked (Man)

Glycosylation

484

1

O-linked (Man)

Glycosylation

486

1

O-linked (Man)

Glycosylation

488

1

O-linked (Man)

Glycosylation

489

1

O-linked (Man)

Glycosylation

492

1

O-linked (Man)

Glycosylation

496

1

O-linked (Man)

Glycosylation

499

1

O-linked (Man)

Glycosylation

500

1

O-linked (Man)

Glycosylation

501

1

O-linked (Man)

Glycosylation

502

1

O-linked (Man)

Glycosylation

504

1

O-linked (Man)

Glycosylation

506

1

O-linked (Man)

Glycosylation

508

1

O-linked (Man)

Glycosylation

510

1

O-linked (Man)

Glycosylation

512

1

O-linked (Man)

Glycosylation

513

1

O-linked (Man)

Glycosylation

514

1

O-linked (Man)

Glycosylation

515

1

O-linked (Man)

Glycosylation

517

1

O-linked (Man)

Glycosylation

518

1

O-linked (Man)

Glycosylation

520

1

O-linked (Man)

Glycosylation

522

1

O-linked (Man)

Glycosylation

524

1

O-linked (Man)

Glycosylation

525

1

O-linked (Man)

Glycosylation

526

1

O-linked (Man)

Glycosylation

527

1

O-linked (Man)

Glycosylation

528

1

O-linked (Man)

Glycosylation

529

1

O-linked (Man)

Glycosylation

530

1

O-linked (Man)

Glycosylation

531

1

O-linked (Man)

Glycosylation

532

1

O-linked (Man)

Glycosylation

534

1

O-linked (Man)

Glycosylation

535

1

O-linked (Man)

Disulfide bond

234 ↔ 237

By similarity

Disulfide bond

246 ↔ 473

By similarity

Disulfide bond

286 ↔ 294

By similarity

Natural variations

Alternative sequence

527 – 534

8

STSSTSCT → TTRSGMSL in isoform G2.

VSP_012837

Alternative sequence

535 – 640

106

Missing in isoform G2.

VSP_012838

Secondary structure

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640

Helix Strand Turn

Details...

Helix

31 – 44

14

Turn

47 – 49

3

Beta strand

67 – 71

5

Beta strand

74 – 76

3

Helix

77 – 92

16

Helix

96 – 98

3

Helix

99 – 112

14

Turn

122 – 124

3

Helix

126 – 129

4

Beta strand

132 – 134

3

Turn

135 – 137

3

Helix

150 – 168

19

Helix

172 – 177

6

Helix

179 – 193

15

Beta strand

206 – 209

4

Helix

210 – 229

20

Helix

235 – 248

14

Helix

249 – 251

3

Beta strand

254 – 257

4

Helix

270 – 278

9

Helix

288 – 290

3

Helix

296 – 307

12

Turn

308 – 312

5

Helix

314 – 316

3

Helix

335 – 337

3

Helix

342 – 362

21

Beta strand

364 – 367

4

Turn

369 – 371

3

Helix

372 – 378

7

Beta strand

384 – 388

5

Helix

392 – 415

24

Beta strand

424 – 426

3

Turn

428 – 430

3

Beta strand

433 – 438

6

Helix

440 – 453

14

Helix

463 – 465

3

Turn

535 – 537

3

Beta strand

541 – 546

6

Beta strand

554 – 556

3

Beta strand

560 – 562

3

Beta strand

566 – 568

3

Helix

569 – 571

3

Beta strand

572 – 574

3

Beta strand

578 – 583

6

Beta strand

588 – 591

4

Beta strand

595 – 597

3

Beta strand

604 – 606

3

Beta strand

608 – 610

3

Beta strand

612 – 614

3

Beta strand

620 – 623

4

Beta strand

626 – 629

4

Beta strand

634 – 638

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform G1 [UniParc]. Last modified November 1, 1986. Version 1. Checksum: 26F58DD18AD7F702	FASTA	640	68,309
	10 20 30 40 50 60 MSFRSLLALS GLVCTGLANV ISKRATLDSW LSNEATVART AILNNIGADG AWVSGADSGI 70 80 90 100 110 120 VVASPSTDNP DYFYTWTRDS GLVLKTLVDL FRNGDTSLLS TIENYISAQA IVQGISNPSG 130 140 150 160 170 180 DLSSGAGLGE PKFNVDETAY TGSWGRPQRD GPALRATAMI GFGQWLLDNG YTSTATDIVW 190 200 210 220 230 240 PLVRNDLSYV AQYWNQTGYD LWEEVNGSSF FTIAVQHRAL VEGSAFATAV GSSCSWCDSQ 250 260 270 280 290 300 APEILCYLQS FWTGSFILAN FDSSRSGKDA NTLLGSIHTF DPEAACDDST FQPCSPRALA 310 320 330 340 350 360 NHKEVVDSFR SIYTLNDGLS DSEAVAVGRY PEDTYYNGNP WFLCTLAAAE QLYDALYQWD 370 380 390 400 410 420 KQGSLEVTDV SLDFFKALYS DAATGTYSSS SSTYSSIVDA VKTFADGFVS IVETHAASNG 430 440 450 460 470 480 SMSEQYDKSD GEQLSARDLT WSYAALLTAN NRRNSVVPAS WGETSASSVP GTCAATSAIG 490 500 510 520 530 540 TYSSVTVTSW PSIVATGGTT TTATPTGSGS VTSTSKTTAT ASKTSTSTSS TSCTTPTAVA 550 560 570 580 590 600 VTFDLTATTT YGENIYLVGS ISQLGDWETS DGIALSADKY TSSDPLWYVT VTLPAGESFE 610 620 630 640 YKFIRIESDD SVEWESDPNR EYTVPQACGT STATVTDTWR
	Isoform G2 [UniParc]. Checksum: 94D188E946D0C12E	FASTA	534	56,730
	10 20 30 40 50 60 MSFRSLLALS GLVCTGLANV ISKRATLDSW LSNEATVART AILNNIGADG AWVSGADSGI 70 80 90 100 110 120 VVASPSTDNP DYFYTWTRDS GLVLKTLVDL FRNGDTSLLS TIENYISAQA IVQGISNPSG 130 140 150 160 170 180 DLSSGAGLGE PKFNVDETAY TGSWGRPQRD GPALRATAMI GFGQWLLDNG YTSTATDIVW 190 200 210 220 230 240 PLVRNDLSYV AQYWNQTGYD LWEEVNGSSF FTIAVQHRAL VEGSAFATAV GSSCSWCDSQ 250 260 270 280 290 300 APEILCYLQS FWTGSFILAN FDSSRSGKDA NTLLGSIHTF DPEAACDDST FQPCSPRALA 310 320 330 340 350 360 NHKEVVDSFR SIYTLNDGLS DSEAVAVGRY PEDTYYNGNP WFLCTLAAAE QLYDALYQWD 370 380 390 400 410 420 KQGSLEVTDV SLDFFKALYS DAATGTYSSS SSTYSSIVDA VKTFADGFVS IVETHAASNG 430 440 450 460 470 480 SMSEQYDKSD GEQLSARDLT WSYAALLTAN NRRNSVVPAS WGETSASSVP GTCAATSAIG 490 500 510 520 530 TYSSVTVTSW PSIVATGGTT TTATPTGSGS VTSTSKTTAT ASKTSTTTRS GMSL

References

[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X00548 mRNA. Translation: CAA25219.1.
X00712 Genomic DNA. Translation: CAA25303.1.
X00712 Genomic DNA. Translation: CAA25304.1.
X56442 Genomic DNA. Translation: CAA39825.1.

PIR

ALASGR. A90986.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P69328.

SMR

P69328. Positions 25-640.

ModBase

Search...

Protein family/group databases

Allergome

914. Asp n Glucoamylase.

CAZy

CBM20. Carbohydrate-Binding Module Family 20.
GH15. Glycoside Hydrolase Family 15.

mycoCLAP

GLA15A_ASPNG.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

eggNOG

COG3387.

Enzyme and pathway databases

BRENDA

3.2.1.3. 518.

Family and domain databases

Gene3D

1.50.10.10. 1 hit.
2.60.40.10. 1 hit.

InterPro

IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR000165. Glucoamylase.
IPR008291. Glucoamylase_SBD.
IPR015902. Glyco_hydro_13.
IPR011613. Glyco_hydro_15.
IPR013783. Ig-like_fold.
[Graphical view]

PANTHER

PTHR10357. PTHR10357. 1 hit.

Pfam

PF00686. CBM_20. 1 hit.
PF00723. Glyco_hydro_15. 1 hit.
[Graphical view]

PIRSF

PIRSF001031. Glu-a-glcsd_SBD. 1 hit.

PRINTS

PR00736. GLHYDRLASE15.

SMART

SM01065. CBM_2. 1 hit.
[Graphical view]

SUPFAM

SSF49452. CBD_4. 1 hit.
SSF48208. Glyco_trans_6hp. 1 hit.

PROSITE

PS51166. CBM20. 1 hit.
PS00820. GLUCOAMYLASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P69328.

ChEMBL

CHEMBL3745.

EvolutionaryTrace

P69328.

Entry information

Entry name

AMYG_ASPNG

Accession

Primary (citable) accession number: P69328
Secondary accession number(s): P04064, Q92201, Q99179

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	November 1, 1986
Last modified:	April 3, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program