GenomeNet

Database: UniProt/SWISS-PROT
Entry: AMYA1_ASPOR
LinkDB: AMYA1_ASPOR
Original site: AMYA1_ASPOR 
ID   AMYA1_ASPOR             Reviewed;         499 AA.
AC   P0C1B3; P10529; P11763; Q00250; Q2U6K7;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   25-APR-2018, entry version 90.
DE   RecName: Full=Alpha-amylase A type-1/2;
DE            EC=3.2.1.1 {ECO:0000305};
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE   AltName: Full=Taka-amylase A;
DE            Short=TAA;
DE   Flags: Precursor;
GN   Name=amy1; Synonyms=amyI, Taa-G1; ORFNames=AO090023000944;
GN   and
GN   Name=amy2; Synonyms=amyII, Taa-G2; ORFNames=AO090120000196;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (AMY1 AND AMY2).
RC   STRAIN=DSM 63303;
RX   PubMed=2785629; DOI=10.1111/j.1365-2958.1989.tb00097.x;
RA   Wirsel S., Lachmund A., Wildhardt G., Ruttkowski E.;
RT   "Three alpha-amylase genes of Aspergillus oryzae exhibit identical
RT   intron-exon organization.";
RL   Mol. Microbiol. 3:3-14(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2789162; DOI=10.1016/0378-1119(89)90096-6;
RA   Genes M.J., Dove M.J., Seligy V.L.;
RT   "Aspergillus oryzae has two nearly identical Taka-amylase genes, each
RT   containing eight introns.";
RL   Gene 79:107-117(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Tada S., Iimura Y., Gomi K., Takahashi K., Hara S., Yoshizawa K.;
RT   "Cloning and nucleotide sequence of the genomic Taka-amylase A gene of
RT   Aspergillus oryzae.";
RL   Agric. Biol. Chem. 53:593-599(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AMY1 AND AMY2).
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G.,
RA   Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K.,
RA   Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W.,
RA   Galagan J.E., Nierman W.C., Yu J., Archer D.B., Bennett J.W.,
RA   Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H.,
RA   Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R.,
RA   Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N.,
RA   Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I.,
RA   Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y.,
RA   Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y.,
RA   Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K.,
RA   Kuhara S., Ogasawara N., Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
RN   [5]
RP   PROTEIN SEQUENCE OF 22-499.
RX   DOI=10.2183/pjab.58.208;
RA   Toda H., Kondo K., Narita K.;
RT   "The complete amino acid sequence of Taka-amylase A.";
RL   Proc. Jpn. Acad., B, Phys. Biol. Sci. 58:208-212(1982).
RN   [6]
RP   PROTEIN SEQUENCE OF 206-225.
RX   PubMed=4733850;
RA   Isemura S., Ikenaka T.;
RT   "The amino acid sequences of glycopeptides obtained from Taka-amylase
RT   A with trypsin and chymotrypsin.";
RL   J. Biochem. 74:1-10(1973).
RN   [7]
RP   PROTEIN SEQUENCE OF 434-499.
RA   Narita K.;
RT   "Amino acid sequence of the C-terminal sixty-six residues of Taka-
RT   amylase A.";
RL   Proc. Jpn. Acad. 51:285-290(1975).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 22-499 IN COMPLEX WITH
RP   CALCIUM, COFACTOR, AND DISULFIDE BONDS.
RX   PubMed=6156152;
RA   Matsuura Y., Kusunoki M., Harada W., Tanaka N., Iga Y., Yasuoka N.,
RA   Toda H., Narita K., Kakudo M.;
RT   "Molecular structure of taka-amylase A. I. Backbone chain folding at
RT   3-A resolution.";
RL   J. Biochem. 87:1555-1558(1980).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
RX   PubMed=6609921;
RA   Matsuura Y., Kusunoki M., Harada W., Kakudo M.;
RT   "Structure and possible catalytic residues of Taka-amylase A.";
RL   J. Biochem. 95:697-702(1984).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH CALCIUM AND
RP   ACARBOSE, COFACTOR, DISULFIDE BONDS, AND ACTIVE SITE.
RX   PubMed=9283074; DOI=10.1021/bi970539i;
RA   Brzozowski A.M., Davies G.J.;
RT   "Structure of the Aspergillus oryzae alpha-amylase complexed with the
RT   inhibitor acarbose at 2.0-A resolution.";
RL   Biochemistry 36:10837-10845(1997).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 22-499 IN COMPLEX WITH
RP   MALTOSE AND CALCIUM IONS, GLYCOSYLATION AT ASN-218, AND DISULFIDE
RP   BONDS.
RX   PubMed=16880540; DOI=10.1107/S1744309106024729;
RA   Vujicic-Zagar A., Dijkstra B.W.;
RT   "Monoclinic crystal form of Aspergillus niger alpha-amylase in complex
RT   with maltose at 1.8 angstroms resolution.";
RL   Acta Crystallogr. F 62:716-721(2006).
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-alpha-D-glucosidic
CC       linkages in polysaccharides containing three or more (1->4)-alpha-
CC       linked D-glucose units. {ECO:0000305}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:16880540,
CC         ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074};
CC       Note=Binds 2 calcium ions per subunit (PubMed:6609921,
CC       PubMed:9283074, PubMed:16880540). Calcium is inhibitory at high
CC       concentrations. {ECO:0000269|PubMed:16880540,
CC       ECO:0000269|PubMed:6609921, ECO:0000269|PubMed:9283074,
CC       ECO:0000305};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16880540,
CC       ECO:0000269|PubMed:9283074}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- BIOTECHNOLOGY: Used in the brewing industry to increase the
CC       fermentability of beer worts (including those made from unmalted
CC       cereals), in the starch industry to make high maltose and high DE
CC       syrups (starch saccharification), in the alcohol industry to
CC       reduce fermentation time, in the cereal food industry for flour
CC       supplementation and improvement of chilled and frozen dough, and
CC       in the forestry industry for low-temperature modification of
CC       starch. Sold under the name Fungamyl by Novozymes.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000305}.
DR   EMBL; X12725; CAA31218.1; -; Genomic_DNA.
DR   EMBL; X12726; CAA31219.1; -; Genomic_DNA.
DR   EMBL; D00434; BAA00336.1; -; Genomic_DNA.
DR   EMBL; AP007157; BAE59434.1; -; Genomic_DNA.
DR   EMBL; AP007166; BAE62808.1; -; Genomic_DNA.
DR   PIR; JK0201; JK0201.
DR   PIR; JT0466; JT0466.
DR   PIR; S04548; ALAS1.
DR   RefSeq; XP_001821436.1; XM_001821384.2.
DR   RefSeq; XP_001823941.1; XM_001823889.2.
DR   PDB; 2GUY; X-ray; 1.59 A; A=22-499.
DR   PDB; 2GVY; X-ray; 1.80 A; A/B=22-499.
DR   PDB; 2TAA; X-ray; 3.00 A; A/B/C=22-499.
DR   PDB; 3KWX; X-ray; 2.40 A; A=22-499.
DR   PDB; 3VX0; X-ray; 1.50 A; A=22-499.
DR   PDB; 3VX1; X-ray; 2.20 A; A=22-499.
DR   PDB; 6TAA; X-ray; 2.10 A; A=22-499.
DR   PDB; 7TAA; X-ray; 1.98 A; A=22-499.
DR   PDBsum; 2GUY; -.
DR   PDBsum; 2GVY; -.
DR   PDBsum; 2TAA; -.
DR   PDBsum; 3KWX; -.
DR   PDBsum; 3VX0; -.
DR   PDBsum; 3VX1; -.
DR   PDBsum; 6TAA; -.
DR   PDBsum; 7TAA; -.
DR   ProteinModelPortal; P0C1B3; -.
DR   SMR; P0C1B3; -.
DR   STRING; 5062.CADAORAP00011123; -.
DR   Allergome; 86; Asp o 21.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GlyConnect; 25; -.
DR   UniCarbKB; P0C1B3; -.
DR   EnsemblFungi; BAE59434; BAE59434; AO090023000944.
DR   EnsemblFungi; BAE62808; BAE62808; AO090120000196.
DR   GeneID; 5993438; -.
DR   GeneID; 5996200; -.
DR   KEGG; aor:AO090023000944; -.
DR   KEGG; aor:AO090120000196; -.
DR   HOGENOM; HOG000165530; -.
DR   KO; K01176; -.
DR   OMA; NDQKYFH; -.
DR   OrthoDB; EOG092C1HLH; -.
DR   EvolutionaryTrace; P0C1B3; -.
DR   Proteomes; UP000006564; Chromosome 3.
DR   Proteomes; UP000006564; Chromosome 5.
DR   GO; GO:0030428; C:cell septum; IDA:AspGD.
DR   GO; GO:0030287; C:cell wall-bounded periplasmic space; IDA:AspGD.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0009277; C:fungal-type cell wall; IDA:AspGD.
DR   GO; GO:0032163; C:hyphal septin band; IDA:AspGD.
DR   GO; GO:0031521; C:spitzenkorper; IDA:AspGD.
DR   GO; GO:0004556; F:alpha-amylase activity; IGI:AspGD.
DR   GO; GO:0103025; F:alpha-amylase activity (releasing maltohexaose); IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IGI:AspGD.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR013777; A-amylase-like.
DR   InterPro; IPR015340; A_amylase_DUF1966_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF09260; DUF1966; 1.
DR   PIRSF; PIRSF001024; Alph-amyl_fung; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Carbohydrate metabolism; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Metal-binding; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     21       {ECO:0000269|Ref.5}.
FT   CHAIN        22    499       Alpha-amylase A type-1/2.
FT                                /FTId=PRO_0000001349.
FT   REGION      230    231       Substrate binding.
FT                                {ECO:0000305|PubMed:9283074}.
FT   ACT_SITE    227    227       Nucleophile.
FT                                {ECO:0000305|PubMed:9283074}.
FT   ACT_SITE    251    251       Proton donor.
FT                                {ECO:0000305|PubMed:9283074}.
FT   METAL       142    142       Calcium 1. {ECO:0000269|PubMed:16880540,
FT                                ECO:0000269|PubMed:6609921,
FT                                ECO:0000269|PubMed:9283074}.
FT   METAL       183    183       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000269|PubMed:16880540,
FT                                ECO:0000269|PubMed:6609921,
FT                                ECO:0000269|PubMed:9283074}.
FT   METAL       196    196       Calcium 1. {ECO:0000269|PubMed:16880540,
FT                                ECO:0000269|PubMed:6609921,
FT                                ECO:0000269|PubMed:9283074}.
FT   METAL       227    227       Calcium 2. {ECO:0000269|PubMed:9283074}.
FT   METAL       231    231       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000269|PubMed:16880540,
FT                                ECO:0000269|PubMed:6609921,
FT                                ECO:0000269|PubMed:9283074}.
FT   METAL       251    251       Calcium 2. {ECO:0000269|PubMed:9283074}.
FT   BINDING      56     56       Substrate. {ECO:0000305|PubMed:9283074}.
FT   BINDING     104    104       Substrate. {ECO:0000305|PubMed:9283074}.
FT   BINDING     143    143       Substrate. {ECO:0000305|PubMed:9283074}.
FT   BINDING     225    225       Substrate. {ECO:0000305|PubMed:9283074}.
FT   BINDING     255    255       Substrate; via amide nitrogen.
FT                                {ECO:0000305|PubMed:9283074}.
FT   BINDING     318    318       Substrate. {ECO:0000305|PubMed:9283074}.
FT   BINDING     365    365       Substrate. {ECO:0000305|PubMed:9283074}.
FT   SITE        318    318       Transition state stabilizer.
FT                                {ECO:0000305|PubMed:9283074}.
FT   CARBOHYD    218    218       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:16880540}.
FT                                /FTId=CAR_000125.
FT   DISULFID     51     59       {ECO:0000244|PDB:7TAA,
FT                                ECO:0000269|PubMed:16880540,
FT                                ECO:0000269|PubMed:6609921,
FT                                ECO:0000269|PubMed:9283074}.
FT   DISULFID    171    185       {ECO:0000244|PDB:7TAA,
FT                                ECO:0000269|PubMed:16880540,
FT                                ECO:0000269|PubMed:6609921,
FT                                ECO:0000269|PubMed:9283074}.
FT   DISULFID    261    304       {ECO:0000244|PDB:7TAA,
FT                                ECO:0000269|PubMed:16880540,
FT                                ECO:0000269|PubMed:6609921,
FT                                ECO:0000269|PubMed:9283074}.
FT   DISULFID    461    496       {ECO:0000244|PDB:7TAA,
FT                                ECO:0000269|PubMed:16880540,
FT                                ECO:0000269|PubMed:6609921,
FT                                ECO:0000269|PubMed:9283074}.
FT   CONFLICT     93     94       TT -> DC (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    101    101       H -> T (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    106    106       Q -> T (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    184    184       D -> Y (in Ref. 3; BAA00336).
FT                                {ECO:0000305}.
FT   CONFLICT    195    195       P -> L (in Ref. 3; BAA00336).
FT                                {ECO:0000305}.
FT   CONFLICT    255    255       G -> V (in Ref. 3; BAA00336).
FT                                {ECO:0000305}.
FT   CONFLICT    345    345       I -> L (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    406    409       WPIY -> PYI (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    443    444       Missing (in Ref. 7; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    448    448       G -> Q (in Ref. 7; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    448    448       G -> S (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    458    458       V -> VGTTV (in Ref. 7; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    465    466       Missing (in Ref. 7; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    469    471       DGN -> BGB (in Ref. 7; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    497    497       S -> SD (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   HELIX        24     27       {ECO:0000244|PDB:3VX0}.
FT   STRAND       32     35       {ECO:0000244|PDB:3VX0}.
FT   HELIX        37     40       {ECO:0000244|PDB:3VX0}.
FT   HELIX        53     55       {ECO:0000244|PDB:3VX0}.
FT   HELIX        63     68       {ECO:0000244|PDB:3VX0}.
FT   HELIX        70     74       {ECO:0000244|PDB:3VX0}.
FT   TURN         75     77       {ECO:0000244|PDB:3VX0}.
FT   STRAND       80     83       {ECO:0000244|PDB:3VX0}.
FT   STRAND       87     89       {ECO:0000244|PDB:3VX0}.
FT   STRAND      104    111       {ECO:0000244|PDB:3VX0}.
FT   TURN        113    115       {ECO:0000244|PDB:3VX0}.
FT   HELIX       118    130       {ECO:0000244|PDB:3VX0}.
FT   STRAND      134    139       {ECO:0000244|PDB:3VX0}.
FT   STRAND      146    148       {ECO:0000244|PDB:3VX0}.
FT   HELIX       150    152       {ECO:0000244|PDB:3VX0}.
FT   HELIX       155    157       {ECO:0000244|PDB:3VX0}.
FT   STRAND      158    160       {ECO:0000244|PDB:3VX0}.
FT   HELIX       164    166       {ECO:0000244|PDB:3VX0}.
FT   HELIX       176    178       {ECO:0000244|PDB:2TAA}.
FT   HELIX       179    184       {ECO:0000244|PDB:3VX0}.
FT   STRAND      185    188       {ECO:0000244|PDB:3VX0}.
FT   STRAND      190    194       {ECO:0000244|PDB:3VX0}.
FT   HELIX       202    219       {ECO:0000244|PDB:3VX0}.
FT   STRAND      223    227       {ECO:0000244|PDB:3VX0}.
FT   HELIX       229    231       {ECO:0000244|PDB:3VX0}.
FT   HELIX       234    236       {ECO:0000244|PDB:3VX0}.
FT   HELIX       237    244       {ECO:0000244|PDB:3VX0}.
FT   STRAND      246    250       {ECO:0000244|PDB:3VX0}.
FT   HELIX       257    260       {ECO:0000244|PDB:3VX0}.
FT   HELIX       261    265       {ECO:0000244|PDB:3VX0}.
FT   STRAND      267    271       {ECO:0000244|PDB:3VX0}.
FT   HELIX       273    283       {ECO:0000244|PDB:3VX0}.
FT   HELIX       290    303       {ECO:0000244|PDB:3VX0}.
FT   HELIX       307    309       {ECO:0000244|PDB:3VX0}.
FT   STRAND      310    312       {ECO:0000244|PDB:3VX0}.
FT   HELIX       322    325       {ECO:0000244|PDB:3VX0}.
FT   HELIX       329    341       {ECO:0000244|PDB:3VX0}.
FT   STRAND      342    349       {ECO:0000244|PDB:3VX0}.
FT   HELIX       352    354       {ECO:0000244|PDB:3VX0}.
FT   TURN        361    364       {ECO:0000244|PDB:3VX0}.
FT   HELIX       368    371       {ECO:0000244|PDB:3VX0}.
FT   STRAND      375    377       {ECO:0000244|PDB:7TAA}.
FT   HELIX       378    396       {ECO:0000244|PDB:3VX0}.
FT   TURN        398    402       {ECO:0000244|PDB:3VX0}.
FT   STRAND      406    410       {ECO:0000244|PDB:3VX0}.
FT   STRAND      412    421       {ECO:0000244|PDB:3VX0}.
FT   TURN        422    424       {ECO:0000244|PDB:3VX0}.
FT   STRAND      426    431       {ECO:0000244|PDB:3VX0}.
FT   STRAND      440    444       {ECO:0000244|PDB:3VX0}.
FT   STRAND      454    457       {ECO:0000244|PDB:3VX0}.
FT   TURN        458    461       {ECO:0000244|PDB:3VX0}.
FT   STRAND      462    465       {ECO:0000244|PDB:3VX0}.
FT   STRAND      468    470       {ECO:0000244|PDB:6TAA}.
FT   STRAND      472    476       {ECO:0000244|PDB:3VX0}.
FT   STRAND      482    486       {ECO:0000244|PDB:3VX0}.
FT   HELIX       487    490       {ECO:0000244|PDB:3VX0}.
FT   STRAND      493    495       {ECO:0000244|PDB:3KWX}.
SQ   SEQUENCE   499 AA;  54810 MW;  E407AE50DD071B52 CRC64;
     MMVAWWSLFL YGLQVAAPAL AATPADWRSQ SIYFLLTDRF ARTDGSTTAT CNTADQKYCG
     GTWQGIIDKL DYIQGMGFTA IWITPVTAQL PQTTAYGDAY HGYWQQDIYS LNENYGTADD
     LKALSSALHE RGMYLMVDVV ANHMGYDGAG SSVDYSVFKP FSSQDYFHPF CFIQNYEDQT
     QVEDCWLGDN TVSLPDLDTT KDVVKNEWYD WVGSLVSNYS IDGLRIDTVK HVQKDFWPGY
     NKAAGVYCIG EVLDGDPAYT CPYQNVMDGV LNYPIYYPLL NAFKSTSGSM DDLYNMINTV
     KSDCPDSTLL GTFVENHDNP RFASYTNDIA LAKNVAAFII LNDGIPIIYA GQEQHYAGGN
     DPANREATWL SGYPTDSELY KLIASANAIR NYAISKDTGF VTYKNWPIYK DDTTIAMRKG
     TDGSQIVTIL SNKGASGDSY TLSLSGAGYT AGQQLTEVIG CTTVTVGSDG NVPVPMAGGL
     PRVLYPTEKL AGSKICSSS
//
DBGET integrated database retrieval system