Reviewed, UniProtKB/Swiss-Prot P0C1B4 (AMYA3_ASPOR)

Names and origin

Protein names

Recommended name:
    Alpha-amylase A type-3
    EC=3.2.1.1
Alternative name(s):
    Taka-amylase A
      Short name=TAA
    1,4-alpha-D-glucan glucanohydrolase

Gene names

Name:	amy3
Synonyms:	amyIII, Taa-G3
ORF Names:	AO090003001210

Organism

Aspergillus oryzae [Complete proteome]

Taxonomic identifier

5062 [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	Inferred from homology.

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides.
Cofactor	Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations By similarity.
Subunit structure	Monomer By similarity.
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	Complete proteome
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: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21
	Chain	22 – 499	478	Alpha-amylase A type-3		PRO_0000233271
Sites
	Active site	227	1	Nucleophile By similarity
	Active site	251	1	Proton donor By similarity
	Active site	318	1	By similarity
	Metal binding	142	1	Calcium 1 By similarity
	Metal binding	183	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	196	1	Calcium 1 By similarity
	Metal binding	227	1	Calcium 2 By similarity
	Metal binding	231	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	251	1	Calcium 2 By similarity
Amino acid modifications
	Glycosylation	218	1	N-linked (GlcNAc...) Potential
	Disulfide bond	51 ↔ 59		By similarity
	Disulfide bond	171 ↔ 185		By similarity
	Disulfide bond	261 ↔ 304		By similarity
	Disulfide bond	461 ↔ 496		By similarity
Experimental info
	Sequence conflict	56	1	R → Q in AAA32708. Ref.3
	Sequence conflict	291	1	D → H in AAA32708. Ref.3
	Sequence conflict	370	1	L → A in AAA32708. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P0C1B4-1 [UniParc]. Last modified May 2, 2006. Version 1. Checksum: EEF42ADA71D20DA9	FASTA	499	54,804
	10 20 30 40 50 60 MMVAWWSLFL YGLQVAAPAL AATPADWRSQ SIYFLLTDRF ARTDGSTTAT CNTADRKYCG 70 80 90 100 110 120 GTWQGIIDKL DYIQGMGFTA IWITPVTAQL PQTTAYGDAY HGYWQQDIYS LNENYGTADD 130 140 150 160 170 180 LKALSSALHE RGMYLMVDVV ANHMGYDGAG SSVDYSVFKP FSSQDYFHPF CLIQNYEDQT 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]. 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]	"Isolation of a cDNA encoding Aspergillus oryzae Taka-amylase A: evidence for multiple related genes." Tsukagoshi N., Furukawa M., Nagaba H., Kirita N., Tsuboi A., Udaka S. Gene 84:319-327(1989) [PubMed: 2612911] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Molecular cloning and characterization of a transcriptional activator gene, amyR, involved in the amylolytic gene expression in Aspergillus oryzae." Gomi K., Akeno T., Minetoki T., Ozeki K., Kumagai C., Okazaki N., Iimura Y. Biosci. Biotechnol. Biochem. 64:816-827(2000) [PubMed: 10830498] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.
[5]	"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]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X12727 Genomic DNA. Translation: CAA31220.1. M33218 Genomic DNA. Translation: AAA32708.1. AB021876 Genomic DNA. Translation: BAA95703.1. AP007155 Genomic DNA. No translation available.
PIR	JN0588. ALAS3. S04549.
3D structure databases
SMR	P0C1B4. Positions 22-497.
ModBase	Search...
Protein family/group databases
CAZy	GH13. Glycoside Hydrolase Family 13.
Enzyme and pathway databases
BRENDA	3.2.1.1. 2240.
Family and domain databases
InterPro	IPR013777. A-amylase_fun. IPR015340. Alpha_amylase_DUF1966_C. IPR006046. Glyco_hydro_13. IPR013780. Glyco_hydro_13_b. IPR006047. Glyco_hydro_13_cat. IPR006589. Glyco_hydro_13_sub_cat. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 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]
ProtoNet	Search...

Entry information

Entry name

AMYA3_ASPOR

Accession

Primary (citable) accession number: P0C1B4
Secondary accession number(s): P10529 , P11763, Q00250, Q96TH4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	May 2, 2006
Last modified:	June 16, 2009
This is version 21 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)