AMYA3_ASPOR
ID AMYA3_ASPOR Reviewed; 499 AA.
AC P0C1B4; P10529; P11763; Q00250; Q96TH4;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Alpha-amylase A type-3;
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=amy3; Synonyms=amyIII, Taa-G3; ORFNames=AO090003001210;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 intron-
RT 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].
RX PubMed=2612911; DOI=10.1016/0378-1119(89)90506-4;
RA Tsukagoshi N., Furukawa M., Nagaba H., Kirita N., Tsuboi A., Udaka S.;
RT "Isolation of a cDNA encoding Aspergillus oryzae Taka-amylase A: evidence
RT for multiple related genes.";
RL Gene 84:319-327(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=10830498; DOI=10.1271/bbb.64.816;
RA Gomi K., Akeno T., Minetoki T., Ozeki K., Kumagai C., Okazaki N.,
RA Iimura Y.;
RT "Molecular cloning and characterization of a transcriptional activator
RT gene, amyR, involved in the amylolytic gene expression in Aspergillus
RT oryzae.";
RL Biosci. Biotechnol. Biochem. 64:816-827(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P0C1B3};
CC Note=Binds 2 calcium ions per subunit. Calcium is inhibitory at high
CC concentrations. {ECO:0000250|UniProtKB:P0C1B3};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P0C1B3}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0C1B3}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; X12727; CAA31220.1; -; Genomic_DNA.
DR EMBL; M33218; AAA32708.1; -; Genomic_DNA.
DR EMBL; AB021876; BAA95703.1; -; Genomic_DNA.
DR EMBL; AP007155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JN0588; JN0588.
DR PIR; S04549; ALAS3.
DR RefSeq; XP_003189619.1; XM_003189571.1.
DR AlphaFoldDB; P0C1B4; -.
DR SMR; P0C1B4; -.
DR STRING; 510516.P0C1B4; -.
DR Allergome; 3133; Asp o 21.0101.
DR Allergome; 86; Asp o 21.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR VEuPathDB; FungiDB:AO090003001591; -.
DR OMA; RSENFLM; -.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IDA:AspGD.
DR GO; GO:0004556; F:alpha-amylase activity; IGI:AspGD.
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_C_dom.
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 3: Inferred from homology;
KW Calcium; Carbohydrate metabolism; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Metal-binding; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT CHAIN 22..499
FT /note="Alpha-amylase A type-3"
FT /id="PRO_0000233271"
FT ACT_SITE 227
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT ACT_SITE 251
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 230..231
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT SITE 318
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..59
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 171..185
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 261..304
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 461..496
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT CONFLICT 56
FT /note="R -> Q (in Ref. 3; AAA32708)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="D -> H (in Ref. 3; AAA32708)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="L -> A (in Ref. 3; AAA32708)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 499 AA; 54804 MW; EEF42ADA71D20DA9 CRC64;
MMVAWWSLFL YGLQVAAPAL AATPADWRSQ SIYFLLTDRF ARTDGSTTAT CNTADRKYCG
GTWQGIIDKL DYIQGMGFTA IWITPVTAQL PQTTAYGDAY HGYWQQDIYS LNENYGTADD
LKALSSALHE RGMYLMVDVV ANHMGYDGAG SSVDYSVFKP FSSQDYFHPF CLIQNYEDQT
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
