P0C1B3 (AMYA1_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-amylase A type-1/2
EC=3.2.1.1

Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Taka-amylase A
Short name=TAA

Gene names

Name:	amy1
Synonyms:	amyI, Taa-G1
ORF Names:	AO090023000944
AND
Name:	amy2
Synonyms:	amyII, Taa-G2
ORF Names:	AO090120000196

Organism

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

Taxonomic identifier

510516 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	499 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	Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.
Cofactor	Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations.
Subunit structure	Monomer.
Biotechnological use	Used in the brewing industry to increase the fermentability of beer worts (including those made from unmalted cereals), in the starch industry to make high maltose and high DE syrups (starch saccharification), in the alcohol industry to reduce fermentation time, in the cereal food industry for flour supplementation and improvement of chilled and frozen dough, and in the forestry industry for low-temperature modification of starch. Sold under the name Fungamyl by Novozymes.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	alpha-amylase activity Inferred from electronic annotation. Source: EC calcium ion 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 – 21

21

Ref.5

Chain

22 – 499

478

Alpha-amylase A type-1/2

PRO_0000001349

Regions

Region

230 – 231

2

Substrate binding

Sites

Active site

227

1

Nucleophile

Active site

251

1

Proton donor

Metal binding

142

1

Calcium 1

Metal binding

183

1

Calcium 1; via carbonyl oxygen

Metal binding

196

1

Calcium 1

Metal binding

227

1

Calcium 2

Metal binding

231

1

Calcium 1; via carbonyl oxygen

Metal binding

251

1

Calcium 2

Binding site

56

1

Substrate

Binding site

104

1

Substrate

Binding site

143

1

Substrate

Binding site

225

1

Substrate

Binding site

255

1

Substrate; via amide nitrogen

Binding site

317

1

Substrate

Binding site

365

1

Substrate

Site

318

1

Transition state stabilizer

Amino acid modifications

Glycosylation

218

1

N-linked (GlcNAc...) Ref.11

CAR_000125

Disulfide bond

51 ↔ 59

Ref.11

Disulfide bond

171 ↔ 185

Ref.11

Disulfide bond

261 ↔ 304

Ref.11

Disulfide bond

461 ↔ 496

Ref.11

Experimental info

Sequence conflict

93 – 94

2

TT → DC AA sequence Ref.5

Sequence conflict

101

1

H → T AA sequence Ref.5

Sequence conflict

106

1

Q → T AA sequence Ref.5

Sequence conflict

184

1

D → Y in BAA00336. Ref.3

Sequence conflict

195

1

P → L in BAA00336. Ref.3

Sequence conflict

255

1

G → V in BAA00336. Ref.3

Sequence conflict

345

1

I → L AA sequence Ref.5

Sequence conflict

406 – 409

4

WPIY → PYI AA sequence Ref.5

Sequence conflict

443 – 444

2

Missing AA sequence Ref.7

Sequence conflict

448

1

G → Q AA sequence Ref.7

Sequence conflict

448

1

G → S AA sequence Ref.5

Sequence conflict

458

1

V → VGTTV AA sequence Ref.7

Sequence conflict

465 – 466

2

Missing AA sequence Ref.7

Sequence conflict

469 – 471

3

DGN → BGB AA sequence Ref.7

Sequence conflict

497

1

S → SD AA sequence Ref.5

Secondary structure

1

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499

Helix Strand Turn

Details...

Helix

24 – 27

4

Beta strand

32 – 35

4

Helix

37 – 40

4

Helix

53 – 55

3

Helix

63 – 68

6

Helix

70 – 74

5

Turn

75 – 77

3

Beta strand

80 – 83

4

Beta strand

87 – 89

3

Beta strand

104 – 111

8

Helix

118 – 130

13

Beta strand

134 – 139

6

Beta strand

146 – 148

3

Helix

150 – 152

3

Helix

155 – 157

3

Beta strand

158 – 160

3

Helix

164 – 166

3

Helix

179 – 184

6

Beta strand

185 – 188

4

Beta strand

190 – 194

5

Helix

202 – 219

18

Beta strand

223 – 226

4

Helix

229 – 231

3

Helix

234 – 236

3

Helix

237 – 244

8

Beta strand

246 – 250

5

Helix

257 – 260

4

Helix

261 – 265

5

Beta strand

267 – 271

5

Helix

273 – 283

11

Helix

290 – 303

14

Helix

307 – 309

3

Beta strand

310 – 312

3

Helix

322 – 324

3

Helix

329 – 341

13

Beta strand

342 – 349

8

Helix

352 – 354

3

Turn

361 – 364

4

Helix

368 – 371

4

Helix

378 – 396

19

Turn

398 – 402

5

Beta strand

406 – 411

6

Beta strand

414 – 421

8

Beta strand

426 – 431

6

Beta strand

440 – 444

5

Beta strand

454 – 457

4

Turn

458 – 461

4

Beta strand

462 – 465

4

Beta strand

472 – 476

5

Beta strand

482 – 486

5

Helix

487 – 490

4

Sequences

	Sequence		Length	Mass (Da)
	P0C1B3 [UniParc]. Last modified May 2, 2006. Version 1. Checksum: E407AE50DD071B52	FASTA	499	54,810
	10 20 30 40 50 60 MMVAWWSLFL YGLQVAAPAL AATPADWRSQ SIYFLLTDRF ARTDGSTTAT CNTADQKYCG 70 80 90 100 110 120 GTWQGIIDKL DYIQGMGFTA IWITPVTAQL PQTTAYGDAY HGYWQQDIYS LNENYGTADD 130 140 150 160 170 180 LKALSSALHE RGMYLMVDVV ANHMGYDGAG SSVDYSVFKP FSSQDYFHPF CFIQNYEDQT 190 200 210 220 230 240 QVEDCWLGDN TVSLPDLDTT KDVVKNEWYD WVGSLVSNYS IDGLRIDTVK HVQKDFWPGY 250 260 270 280 290 300 NKAAGVYCIG EVLDGDPAYT CPYQNVMDGV LNYPIYYPLL NAFKSTSGSM DDLYNMINTV 310 320 330 340 350 360 KSDCPDSTLL GTFVENHDNP RFASYTNDIA LAKNVAAFII LNDGIPIIYA GQEQHYAGGN 370 380 390 400 410 420 DPANREATWL SGYPTDSELY KLIASANAIR NYAISKDTGF VTYKNWPIYK DDTTIAMRKG 430 440 450 460 470 480 TDGSQIVTIL SNKGASGDSY TLSLSGAGYT AGQQLTEVIG CTTVTVGSDG NVPVPMAGGL 490 PRVLYPTEKL AGSKICSSS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Three alpha-amylase genes of Aspergillus oryzae exhibit identical intron-exon organization." Wirsel S., Lachmund A., Wildhardt G., Ruttkowski E. Mol. Microbiol. 3:3-14(1989) [PubMed: 2785629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (AMY1 AND AMY2). Strain: DSM 63303.
[2]	"Aspergillus oryzae has two nearly identical Taka-amylase genes, each containing eight introns." Genes M.J., Dove M.J., Seligy V.L. Gene 79:107-117(1989) [PubMed: 2789162] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Cloning and nucleotide sequence of the genomic Taka-amylase A gene of Aspergillus oryzae." Tada S., Iimura Y., Gomi K., Takahashi K., Hara S., Yoshizawa K. Agric. Biol. Chem. 53:593-599(1989) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 16372010] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AMY1 AND AMY2). Strain: ATCC 42149 / RIB 40.
[5]	"The complete amino acid sequence of Taka-amylase A." Toda H., Kondo K., Narita K. Proc. Jpn. Acad., B, Phys. Biol. Sci. 58:208-212(1982) Cited for: PROTEIN SEQUENCE OF 22-499.
[6]	"The amino acid sequences of glycopeptides obtained from Taka-amylase A with trypsin and chymotrypsin." Isemura S., Ikenaka T. J. Biochem. 74:1-10(1973) [PubMed: 4733850] [Abstract] Cited for: PROTEIN SEQUENCE OF 206-225.
[7]	"Amino acid sequence of the C-terminal sixty-six residues of Taka-amylase A." Narita K. Proc. Jpn. Acad. 51:285-290(1975) Cited for: PROTEIN SEQUENCE OF 434-499.
[8]	"Molecular structure of taka-amylase A. I. Backbone chain folding at 3-A resolution." Matsuura Y., Kusunoki M., Harada W., Tanaka N., Iga Y., Yasuoka N., Toda H., Narita K., Kakudo M. J. Biochem. 87:1555-1558(1980) [PubMed: 6156152] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
[9]	"Structure and possible catalytic residues of Taka-amylase A." Matsuura Y., Kusunoki M., Harada W., Kakudo M. J. Biochem. 95:697-702(1984) [PubMed: 6609921] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
[10]	"Structure of the Aspergillus oryzae alpha-amylase complexed with the inhibitor acarbose at 2.0-A resolution." Brzozowski A.M., Davies G.J. Biochemistry 36:10837-10845(1997) [PubMed: 9283074] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH CALCIUM AND ACARBOSE, DISUFIDE BONDS.
[11]	"Monoclinic crystal form of Aspergillus niger alpha-amylase in complex with maltose at 1.8 angstroms resolution." Vujicic-Zagar A., Dijkstra B.W. Acta Crystallogr. F 62:716-721(2006) [PubMed: 16880540] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 22-499 IN COMPLEX WITH MALTOSE AND CALCIUM IONS, GLYCOSYLATION AT ASN-218, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X12725 Genomic DNA. Translation: CAA31218.1.
X12726 Genomic DNA. Translation: CAA31219.1.
D00434 Genomic DNA. Translation: BAA00336.1.
AP007157 Genomic DNA. Translation: BAE59434.1.
AP007166 Genomic DNA. Translation: BAE62808.1.

PIR

JK0201.
JT0466.
ALAS1. S04548.

RefSeq

XP_001821436.1. XM_001821384.2.
XP_001823941.1. XM_001823889.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GUY	X-ray	1.59	A	22-499	[»]
2GVY	X-ray	1.80	A/B	22-499	[»]
2TAA	X-ray	3.00	A/B/C	22-497	[»]
3KWX	X-ray	2.40	A	22-499	[»]
6TAA	X-ray	2.10	A	22-499	[»]
7TAA	X-ray	1.98	A	22-499	[»]

ProteinModelPortal

P0C1B3.

SMR

P0C1B3. Positions 22-497.

ModBase

Search...

Protein-protein interaction databases

STRING

P0C1B3.

Protein family/group databases

Allergome

86. Asp o 21.

CAZy

GH13. Glycoside Hydrolase Family 13.

PTM databases

GlycoSuiteDB

P10529.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

CADAORAT00008024; CADAORAP00007860; CADAORAG00008024.
CADAORAT00011354; CADAORAP00011123; CADAORAG00011354.

GeneID

5993438.
5996200.

GenomeReviews

Gene locus amy2 in contig AP007157_GR.
Gene locus amy2 in contig AP007166_GR.

KEGG

aor:AOR_1_1668144.
aor:AOR_1_336094.

Phylogenomic databases

OrthoDB

EOG4SFDF6.

Family and domain databases

InterPro

IPR013777. A-amylase_fun.
IPR015340. A_amylase_DUF1966_C.
IPR015902. Alpha_amylase.
IPR006046. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

KO

K01176.

PANTHER

PTHR10357. Alpha_amylase. 1 hit.

Pfam

PF00128. Alpha-amylase. 1 hit.
PF09260. DUF1966. 1 hit.
[Graphical view]

PIRSF

PIRSF001024. Alph-amyl_fung. 1 hit.

PRINTS

PR00110. ALPHAAMYLASE.

SMART

SM00642. Aamy. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

ProtoNet

Search...

Entry information

Entry name

AMYA1_ASPOR

Accession

Primary (citable) accession number: P0C1B3
Secondary accession number(s): P10529 , P11763, Q00250, Q2U6K7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	May 2, 2006
Last modified:	January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program