P07683 (AMYG_RHIOR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Glucoamylase 1 Short name=Gluc 1 EC=3.2.1.3 Alternative name(s): 1,4-alpha-D-glucan glucohydrolase Glucan 1,4-alpha-glucosidase Cleaved into the following 2 chains: Glucoamylase 2 Short name=Gluc 2 Glucoamylase 3 Short name=Gluc 3
Organism	Rhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
Taxonomic identifier	64495 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Fungi › Fungi incertae sedis › Early diverging fungal lineages › Mucoromycotina › Mucorales › Mucoraceae › Rhizopus

Protein attributes

Sequence length	604 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.
Miscellaneous	Rhizopus glucoamylase exists in multiple forms, Gluc 1, Gluc 2, and Gluc 3, all of which hydrolyze gelatinized starch at similar rates, but only the largest one (Gluc 1) is able to adsorb raw starch. Glucoamylase 3 may be 110-604 instead of 116-104.
Sequence similarities	Belongs to the glycosyl hydrolase 15 family. Contains 1 CBM21 (carbohydrate binding type-21) domain.

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 – 25

25

Chain

26 – 604

579

Glucoamylase 1

PRO_0000001472

Chain

116 – 604

489

Glucoamylase 3

PRO_0000001473

Chain

159 – 604

446

Glucoamylase 2

PRO_0000001474

Regions

Domain

26 – 130

105

CBM21

Region

26 – 115

90

Adsorption to raw starch

Region

116 – 604

489

Starch degradation

Sites

Active site

336

1

Proton acceptor By similarity

Active site

339

1

Proton donor By similarity

Binding site

279

1

Substrate By similarity

Amino acid modifications

Glycosylation

122

1

N-linked (GlcNAc...) Potential

Glycosylation

167

1

N-linked (GlcNAc...) Potential

Glycosylation

230

1

N-linked (GlcNAc...) Potential

Glycosylation

236

1

N-linked (GlcNAc...) Potential

Glycosylation

564

1

N-linked (GlcNAc...) Potential

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

604

Helix Strand Turn

Details...

Beta strand

30 – 44

15

Beta strand

46 – 52

7

Beta strand

55 – 57

3

Beta strand

59 – 67

9

Beta strand

78 – 80

3

Beta strand

82 – 86

5

Beta strand

93 – 99

7

Beta strand

102 – 115

14

Beta strand

117 – 120

4

Beta strand

122 – 125

4

Sequences

	Sequence		Length	Mass (Da)
	P07683 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: 78421F1AAA93ADB9	FASTA	604	65,162
	10 20 30 40 50 60 MQLFNLPLKV SFFLVLSYFS LLVSAASIPS SASVQLDSYN YDGSTFSGKI YVKNIAYSKK 70 80 90 100 110 120 VTVIYADGSD NWNNNGNTIA ASYSAPISGS NYEYWTFSAS INGIKEFYIK YEVSGKTYYD 130 140 150 160 170 180 NNNSANYQVS TSKPTTTTAT ATTTTAPSTS TTTPPSRSEP ATFPTGNSTI SSWIKKQEGI 190 200 210 220 230 240 SRFAMLRNIN PPGSATGFIA ASLSTAGPDY YYAWTRDAAL TSNVIVYEYN TTLSGNKTIL 250 260 270 280 290 300 NVLKDYVTFS VKTQSTSTVC NCLGEPKFNP DASGYTGAWG RPQNDGPAER ATTFILFADS 310 320 330 340 350 360 YLTQTKDASY VTGTLKPAIF KDLDYVVNVW SNGCFDLWEE VNGVHFYTLM VMRKGLLLGA 370 380 390 400 410 420 DFAKRNGDST RASTYSSTAS TIANKISSFW VSSNNWIQVS QSVTGGVSKK GLDVSTLLAA 430 440 450 460 470 480 NLGSVDDGFF TPGSEKILAT AVAVEDSFAS LYPINKNLPS YLGNSIGRYP EDTYNGNGNS 490 500 510 520 530 540 QGNSWFLAVT GYAELYYRAI KEWIGNGGVT VSSISLPFFK KFDSSATSGK KYTVGTSDFN 550 560 570 580 590 600 NLAQNIALAA DRFLSTVQLH AHNNGSLAEE FDRTTGLSTG ARDLTWSHAS LITASYAKAG APAA

References

[1]	"Rhizopus raw-starch-degrading glucoamylase: its cloning and expression in yeast." Ashikari T., Nakamura N., Tanaka Y., Kiuchi N., Shibano Y., Tanaka T., Amachi T., Yoshizumi H. Agric. Biol. Chem. 50:957-964(1986) [AGRICOLA] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SAM0034.
[2]	"Comparison of amino acid sequences of three glucoamylases and their structure-function relationships." Tanaka Y., Ashikari T., Nakamura N., Kiuchi N., Shibano Y., Amachi T., Yoshizumi H. Agric. Biol. Chem. 50:965-969(1986) [AGRICOLA] [Europe PMC] Cited for: HOMOLOGY, PREDICTED SECONDARY STRUCTURE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D00049 Genomic DNA. Translation: BAA00033.1.

PIR

JP0001.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DJM	NMR	-	A	26-131	[»]

ProteinModelPortal

P07683.

ModBase

Search...

Protein family/group databases

CAZy

CBM21. Carbohydrate-Binding Module Family 21.
GH15. Glycoside Hydrolase Family 15.

mycoCLAP

GLA15E_RHIOR.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.50.10.10. 1 hit.

InterPro

IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR005036. CBM_21.
IPR000165. Glucoamylase.
IPR011613. Glyco_hydro_15.
[Graphical view]

Pfam

PF03370. CBM_21. 1 hit.
PF00723. Glyco_hydro_15. 1 hit.
[Graphical view]

PRINTS

PR00736. GLHYDRLASE15.

SUPFAM

SSF48208. Glyco_trans_6hp. 1 hit.

PROSITE

PS51159. CBM21. 1 hit.
PS00820. GLUCOAMYLASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P07683.

ChEMBL

CHEMBL4449.

EvolutionaryTrace

P07683.

Entry information

Entry name

AMYG_RHIOR

Accession

Primary (citable) accession number: P07683

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	November 1, 1995
Last modified:	March 6, 2013
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program