Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0C1B3 (AMYA1_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Ref.5
Chain22 – 499478Alpha-amylase A type-1/2
PRO_0000001349

Regions

Region230 – 2312Substrate binding

Sites

Active site2271Nucleophile
Active site2511Proton donor
Metal binding1421Calcium 1
Metal binding1831Calcium 1; via carbonyl oxygen
Metal binding1961Calcium 1
Metal binding2271Calcium 2
Metal binding2311Calcium 1; via carbonyl oxygen
Metal binding2511Calcium 2
Binding site561Substrate
Binding site1041Substrate
Binding site1431Substrate
Binding site2251Substrate
Binding site2551Substrate; via amide nitrogen
Binding site3171Substrate
Binding site3651Substrate
Site3181Transition state stabilizer

Amino acid modifications

Glycosylation2181N-linked (GlcNAc...) Ref.11
CAR_000125
Disulfide bond51 ↔ 59 Ref.10 Ref.11
Disulfide bond171 ↔ 185 Ref.10 Ref.11
Disulfide bond261 ↔ 304 Ref.10 Ref.11
Disulfide bond461 ↔ 496 Ref.10 Ref.11

Experimental info

Sequence conflict93 – 942TT → DC AA sequence Ref.5
Sequence conflict1011H → T AA sequence Ref.5
Sequence conflict1061Q → T AA sequence Ref.5
Sequence conflict1841D → Y in BAA00336. Ref.3
Sequence conflict1951P → L in BAA00336. Ref.3
Sequence conflict2551G → V in BAA00336. Ref.3
Sequence conflict3451I → L AA sequence Ref.5
Sequence conflict406 – 4094WPIY → PYI AA sequence Ref.5
Sequence conflict443 – 4442Missing AA sequence Ref.7
Sequence conflict4481G → Q AA sequence Ref.7
Sequence conflict4481G → S AA sequence Ref.5
Sequence conflict4581V → VGTTV AA sequence Ref.7
Sequence conflict465 – 4662Missing AA sequence Ref.7
Sequence conflict469 – 4713DGN → BGB AA sequence Ref.7
Sequence conflict4971S → SD AA sequence Ref.5

Secondary structure

...................................................................................................... 499
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C1B3 [UniParc].

Last modified May 2, 2006. Version 1.
Checksum: E407AE50DD071B52

FASTA49954,810
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] (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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH CALCIUM AND ACARBOSE, DISULFIDE 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] [Europe PMC] [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.
PIRJK0201.
JT0466.
ALAS1. S04548.
RefSeqXP_001821436.1. XM_001821384.2.
XP_001823941.1. XM_001823889.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GUYX-ray1.59A22-499[»]
2GVYX-ray1.80A/B22-499[»]
2TAAX-ray3.00A/B/C22-497[»]
3KWXX-ray2.40A22-499[»]
3VX0X-ray1.50A22-499[»]
3VX1X-ray2.20A22-499[»]
6TAAX-ray2.10A22-499[»]
7TAAX-ray1.98A22-499[»]
ProteinModelPortalP0C1B3.
SMRP0C1B3. Positions 22-497.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome86. Asp o 21.
CAZyGH13. Glycoside Hydrolase Family 13.

PTM databases

UniCarbKBP0C1B3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00008024; CADAORAP00007860; CADAORAG00008024.
CADAORAT00011354; CADAORAP00011123; CADAORAG00011354.
GeneID5993438.
5996200.
KEGGaor:AOR_1_1668144.
aor:AOR_1_336094.

Phylogenomic databases

HOGENOMHOG000165530.
KOK01176.
OMASELYTWI.
OrthoDBEOG7RBZJ4.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR013777. A-amylase_fun.
IPR015340. A_amylase_DUF1966_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF09260. DUF1966. 1 hit.
[Graphical view]
PIRSFPIRSF001024. Alph-amyl_fung. 1 hit.
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0C1B3.

Entry information

Entry nameAMYA1_ASPOR
AccessionPrimary (citable) accession number: P0C1B3
Secondary accession number(s): P10529 expand/collapse secondary AC list , P11763, Q00250, Q2U6K7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 2, 2006
Last modified: January 22, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries