P36914 (AMYG_ASPOR) 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
Synonyms:	gluB
ORF Names:	AO090010000746

Organism

Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]

Taxonomic identifier

510516 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	612 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	By similarity
	Propeptide	20 – 25	6	By similarity		PRO_0000001465
	Chain	26 – 612	587	Glucoamylase		PRO_0000001466
Regions
	Domain	506 – 612	107	CBM20
Sites
	Active site	202	1	Proton acceptor By similarity
	Active site	205	1	Proton donor By similarity
	Binding site	146	1	Substrate By similarity
Amino acid modifications
	Glycosylation	39	1	N-linked (GlcNAc...) Potential
	Disulfide bond	236 ↔ 239		By similarity
	Disulfide bond	248 ↔ 475		By similarity
	Disulfide bond	288 ↔ 296		By similarity
Experimental info
	Sequence conflict	172	1	G → S in BAA00841. Ref.1
	Sequence conflict	172	1	G → S in BAA01540. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P36914 [UniParc]. Last modified May 2, 2006. Version 2. Checksum: 7C36E1B0A341CEDA	FASTA	612	65,457
	10 20 30 40 50 60 MVSFSSCLRA LALGSSVLAV QPVLRQATGL DTWLSTEANF SRQAILNNIG ADGQSAQGAS 70 80 90 100 110 120 PGVVIASPSK SDPDYFYTWT RDSGLVMKTL VDLFRGGDAD LLPIIEEFIS SQARIQGISN 130 140 150 160 170 180 PSGALSSGGL GEPKFNVDET AFTGAWGRPQ RDGPALRATA MISFGEWLVE NGHTSIATDL 190 200 210 220 230 240 VWPVVRNDLS YVAQYWSQSG FDLWEEVQGT SFFTVAVSHR ALVEGSSFAK TVGSSCPYCD 250 260 270 280 290 300 SQAPQVRCYL QSFWTGSYIQ ANFGGGRSGK DINTVLGSIH TFDPQATCDD ATFQPCSARA 310 320 330 340 350 360 LANHKVVTDS FRSIYAINSG RAENQAVAVG RYPEDSYYNG NPWFLTTLAA AEQLYDALYQ 370 380 390 400 410 420 WDKIGSLAIT DVSLPFFKAL YSSAATGTYA SSTTVYKDIV SAVKAYADGY VQIVQTYAAS 430 440 450 460 470 480 TGSMAEQYTK TDGSQTSARD LTWSYAALLT ANNRRNAVVP APWGETAATS IPSACSTTSA 490 500 510 520 530 540 SGTYSSVVIT SWPTISGYPG APDSPCQVPT TVSVTFAVKA TTVYGESIKI VGSISQLGSW 550 560 570 580 590 600 NPSSATALNA DSYTTDNPLW TGTINLPAGQ SFEYKFIRVQ NGAVTWESDP NRKYTVPSTC 610 GVKSAVQSDV WR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The glucoamylase cDNA from Aspergillus oryzae: its cloning, nucleotide sequence, and expression in Saccharomyces cerevisiae." Hata Y., Kitamoto K., Gomi K., Kumagai C., Tamura G., Hara S. Agric. Biol. Chem. 55:941-949(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Nucleotide sequence and expression of the glucoamylase-encoding gene (glaA) from Aspergillus oryzae." Hata Y., Tsuchiya K., Kitamoto K., Gomi K., Kumagai C., Tamura G., Hara S. Gene 108:145-150(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.
[3]	Ma L., Chen D., Chen X., Wang H. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H. Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D01035 mRNA. Translation: BAA00841.1. D10698 Genomic DNA. Translation: BAA01540.1. DQ211971 mRNA. Translation: ABA62323.1. AP007175 Genomic DNA. Translation: BAE66563.1.
PIR	JQ1346.
RefSeq	XP_001827696.1. XM_001827644.2.
3D structure databases
ProteinModelPortal	P36914.
SMR	P36914. Positions 30-612.
ModBase	Search...
Protein-protein interaction databases
STRING	5062.CADAORAP00004691.
Protein family/group databases
CAZy	CBM20. Carbohydrate-Binding Module Family 20. GH15. Glycoside Hydrolase Family 15.
mycoCLAP	GLA15A_ASPOR.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAORAT00004778; CADAORAP00004691; CADAORAG00004778.
GeneID	5999830.
KEGG	aor:AOR_1_1262024.
Phylogenomic databases
eggNOG	COG3387.
HOGENOM	HOG000182646.
KO	K01178.
OrthoDB	EOG4FFH90.
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...

Entry information

Entry name

AMYG_ASPOR

Accession

Primary (citable) accession number: P36914
Secondary accession number(s): Q3HLW7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	May 2, 2006
Last modified:	May 1, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program