Reviewed, UniProtKB/Swiss-Prot P08017 (AMYG_SACFI)

Names and origin

Protein names

Recommended name:
    Glucoamylase GLU1
    EC=3.2.1.3
Alternative name(s):
    Glucan 1,4-alpha-glucosidase
    1,4-alpha-D-glucan glucohydrolase

Gene names

Name:

GLU1

Organism

Saccharomycopsis fibuligera (Yeast)

Taxonomic identifier

4944 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycopsidaceae › Saccharomycopsis

Protein attributes

Sequence length	519 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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	3D-structure
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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

27

Chain

28 – 519

492

Glucoamylase GLU1

PRO_0000001475

Sites

Active site

234

1

Proton acceptor By similarity

Active site

237

1

Proton donor By similarity

Binding site

166

1

Substrate By similarity

Amino acid modifications

Glycosylation

115

1

N-linked (GlcNAc...) Potential

Glycosylation

127

1

N-linked (GlcNAc...) Potential

Glycosylation

205

1

N-linked (GlcNAc...) Potential

Secondary structure

1

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519

Helix Strand Turn

Details...

Helix

45 – 62

18

Beta strand

69 – 71

3

Beta strand

85 – 89

5

Beta strand

92 – 94

3

Helix

95 – 111

17

Turn

112 – 114

3

Helix

116 – 133

18

Helix

145 – 151

7

Helix

173 – 191

19

Helix

209 – 215

7

Helix

217 – 227

11

Helix

244 – 263

20

Helix

267 – 285

19

Turn

287 – 289

3

Turn

294 – 297

4

Helix

303 – 307

5

Helix

317 – 325

9

Helix

341 – 357

17

Helix

359 – 361

3

Beta strand

380 – 385

6

Helix

390 – 410

21

Beta strand

414 – 417

4

Helix

418 – 420

3

Helix

421 – 427

7

Helix

431 – 433

3

Helix

438 – 440

3

Beta strand

441 – 446

6

Helix

451 – 474

24

Beta strand

483 – 485

3

Turn

487 – 489

3

Beta strand

492 – 495

4

Helix

499 – 516

18

Sequences

	Sequence		Length	Mass (Da)
	P08017-1 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: BE73035AD1B77652	FASTA	519	57,539
	10 20 30 40 50 60 MKFGVLFSVF AAIVSALPLQ EGPLNKRAYP SFEAYSNYKV DRTDLETFLD KQKEVSLYYL 70 80 90 100 110 120 LQNIAYPEGQ FNNGVPGTVI ASPSTSNPDY YYQWTRDSAI TFLTVLSELE DNNFNTTLAK 130 140 150 160 170 180 AVEYYINTSY NLQRTSNPSG SFDDENHKGL GEPKFNTDGS AYTGAWGRPQ NDGPALRAYA 190 200 210 220 230 240 ISRYLNDVNS LNEGKLVLTD SGDINFSSTE DIYKNIIKPD LEYVIGYWDS TGFDLWEENQ 250 260 270 280 290 300 GRHFFTSLVQ QKALAYAVDI AKSFDDGDFA NTLSSTASTL ESYLSGSDGG FVNTDVNHIV 310 320 330 340 350 360 ENPDLLQQNS RQGLDSATYI GPLLTHDIGE SSSTPFDVDN EYVLQSYYLL LEDNKDRYSV 370 380 390 400 410 420 NSAYSAGAAI GRYPEDVYNG DGSSEGNPWF LATAYAAQVP YKLAYDAKSA SNDITINKIN 430 440 450 460 470 480 YDFFNKYIVD LSTINSAYQS SDSVTIKSGS DEFNTVADNL VTFGDSFLQV ILDHINDDGS 490 500 510 LNEQLNRYTG YSTGAYSLTW SSGALLEAIR LRNKVKALA

References

[1]	"Nucleotide sequence of the glucoamylase gene GLU1 in the yeast Saccharomycopsis fibuligera." Itoh T., Ohtsuki I., Yamashita I., Fukui S. J. Bacteriol. 169:4171-4176(1987) [PubMed: 3114236] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Structure of glucoamylase from Saccharomycopsis fibuligera at 1.7-A resolution." Sevcik J., Solovicova A., Hostinova E., Gasperik J., Wilson K.S., Dauter Z. Acta Crystallogr. D 54:854-866(1998) [PubMed: 9757101] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L25641 mRNA. Translation: AAA83997.1.
M17355 Genomic DNA. Translation: AAA34649.1.

PIR

A54549.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AYX	X-ray	1.70	A	28-519	[»]
2F6D	X-ray	1.60	A	28-519	[»]
2FBA	X-ray	1.10	A	28-519	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH15. Glycoside Hydrolase Family 15.

Family and domain databases

InterPro

IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR000165. Glyco_hydro_15.
IPR011613. Glyco_hydro_15_rel.
[Graphical view]

Gene3D

G3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit.

Pfam

PF00723. Glyco_hydro_15. 1 hit.
[Graphical view]

PRINTS

PR00736. GLHYDRLASE15.

PROSITE

PS00820. GLUCOAMYLASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

AMYG_SACFI

Accession

Primary (citable) accession number: P08017

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	November 24, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)