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P0C1B3

- AMYA1_ASPOR

UniProt

P0C1B3 - AMYA1_ASPOR

Protein

Alpha-amylase A type-1/2

Gene

amy1

more
Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (02 May 2006)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.

    Cofactori

    Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei56 – 561Substrate
    Binding sitei104 – 1041Substrate
    Metal bindingi142 – 1421Calcium 11 Publication
    Binding sitei143 – 1431Substrate
    Metal bindingi183 – 1831Calcium 1; via carbonyl oxygen1 Publication
    Metal bindingi196 – 1961Calcium 11 Publication
    Binding sitei225 – 2251Substrate
    Active sitei227 – 2271Nucleophile
    Metal bindingi227 – 2271Calcium 21 Publication
    Metal bindingi231 – 2311Calcium 1; via carbonyl oxygen1 Publication
    Active sitei251 – 2511Proton donor
    Metal bindingi251 – 2511Calcium 21 Publication
    Binding sitei255 – 2551Substrate; via amide nitrogen
    Binding sitei317 – 3171Substrate
    Sitei318 – 3181Transition state stabilizer
    Binding sitei365 – 3651Substrate

    GO - Molecular functioni

    1. alpha-amylase activity Source: ASPGD
    2. calcium ion binding Source: InterPro

    GO - Biological processi

    1. carbohydrate catabolic process Source: ASPGD

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Protein family/group databases

    CAZyiGH13. Glycoside Hydrolase Family 13.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:amy1
    Synonyms:amyI, Taa-G1
    ORF Names:AO090023000944
    AND
    Name:amy2
    Synonyms:amyII, Taa-G2
    ORF Names:AO090120000196
    OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
    Taxonomic identifieri510516 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006564: Chromosome 3, UP000006564: Chromosome 5

    Subcellular locationi

    GO - Cellular componenti

    1. cell septum Source: ASPGD
    2. cell wall-bounded periplasmic space Source: ASPGD
    3. extracellular region Source: ASPGD
    4. fungal-type cell wall Source: ASPGD
    5. hyphal septin band Source: ASPGD
    6. spitzenkorper Source: ASPGD

    Pathology & Biotechi

    Biotechnological usei

    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.

    Protein family/group databases

    Allergomei86. Asp o 21.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 21211 PublicationAdd
    BLAST
    Chaini22 – 499478Alpha-amylase A type-1/2PRO_0000001349Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi51 ↔ 59
    Disulfide bondi171 ↔ 185
    Glycosylationi218 – 2181N-linked (GlcNAc...)1 PublicationCAR_000125
    Disulfide bondi261 ↔ 304
    Disulfide bondi461 ↔ 496

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    PTM databases

    UniCarbKBiP0C1B3.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Structurei

    Secondary structure

    1
    499
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi24 – 274
    Beta strandi32 – 354
    Helixi37 – 404
    Helixi53 – 553
    Helixi63 – 686
    Helixi70 – 745
    Turni75 – 773
    Beta strandi80 – 834
    Beta strandi87 – 893
    Beta strandi104 – 1118
    Turni113 – 1153
    Helixi118 – 13013
    Beta strandi134 – 1396
    Beta strandi146 – 1483
    Helixi150 – 1523
    Helixi155 – 1573
    Beta strandi158 – 1603
    Helixi164 – 1663
    Helixi176 – 1783
    Helixi179 – 1846
    Beta strandi185 – 1884
    Beta strandi190 – 1945
    Helixi202 – 21918
    Beta strandi223 – 2275
    Helixi229 – 2313
    Helixi234 – 2363
    Helixi237 – 2448
    Beta strandi246 – 2505
    Helixi257 – 2604
    Helixi261 – 2655
    Beta strandi267 – 2715
    Helixi273 – 28311
    Helixi290 – 30314
    Helixi307 – 3093
    Beta strandi310 – 3123
    Helixi322 – 3254
    Helixi329 – 34113
    Beta strandi342 – 3498
    Helixi352 – 3543
    Turni361 – 3644
    Helixi368 – 3714
    Beta strandi375 – 3773
    Helixi378 – 39619
    Turni398 – 4025
    Beta strandi406 – 4105
    Beta strandi412 – 42110
    Turni422 – 4243
    Beta strandi426 – 4316
    Beta strandi440 – 4445
    Beta strandi454 – 4574
    Turni458 – 4614
    Beta strandi462 – 4654
    Beta strandi468 – 4703
    Beta strandi472 – 4765
    Beta strandi482 – 4865
    Helixi487 – 4904
    Beta strandi493 – 4953

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GUYX-ray1.59A22-499[»]
    2GVYX-ray1.80A/B22-499[»]
    2TAAX-ray3.00A/B/C22-499[»]
    3KWXX-ray2.40A22-499[»]
    3VX0X-ray1.50A22-499[»]
    3VX1X-ray2.20A22-499[»]
    6TAAX-ray2.10A22-499[»]
    7TAAX-ray1.98A22-499[»]
    ProteinModelPortaliP0C1B3.
    SMRiP0C1B3. Positions 22-497.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0C1B3.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni230 – 2312Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000165530.
    KOiK01176.
    OMAiSELYTWI.
    OrthoDBiEOG7RBZJ4.

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR013777. 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]
    PANTHERiPTHR10357. PTHR10357. 1 hit.
    PfamiPF00128. Alpha-amylase. 1 hit.
    PF09260. DUF1966. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001024. Alph-amyl_fung. 1 hit.
    PRINTSiPR00110. ALPHAAMYLASE.
    SMARTiSM00642. Aamy. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0C1B3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMVAWWSLFL YGLQVAAPAL AATPADWRSQ SIYFLLTDRF ARTDGSTTAT    50
    CNTADQKYCG GTWQGIIDKL DYIQGMGFTA IWITPVTAQL PQTTAYGDAY 100
    HGYWQQDIYS LNENYGTADD LKALSSALHE RGMYLMVDVV ANHMGYDGAG 150
    SSVDYSVFKP FSSQDYFHPF CFIQNYEDQT QVEDCWLGDN TVSLPDLDTT 200
    KDVVKNEWYD WVGSLVSNYS IDGLRIDTVK HVQKDFWPGY NKAAGVYCIG 250
    EVLDGDPAYT CPYQNVMDGV LNYPIYYPLL NAFKSTSGSM DDLYNMINTV 300
    KSDCPDSTLL GTFVENHDNP RFASYTNDIA LAKNVAAFII LNDGIPIIYA 350
    GQEQHYAGGN DPANREATWL SGYPTDSELY KLIASANAIR NYAISKDTGF 400
    VTYKNWPIYK DDTTIAMRKG TDGSQIVTIL SNKGASGDSY TLSLSGAGYT 450
    AGQQLTEVIG CTTVTVGSDG NVPVPMAGGL PRVLYPTEKL AGSKICSSS 499
    Length:499
    Mass (Da):54,810
    Last modified:May 2, 2006 - v1
    Checksum:iE407AE50DD071B52
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti93 – 942TT → DC AA sequence 1 PublicationCurated
    Sequence conflicti101 – 1011H → T AA sequence 1 PublicationCurated
    Sequence conflicti106 – 1061Q → T AA sequence 1 PublicationCurated
    Sequence conflicti184 – 1841D → Y in BAA00336. 1 PublicationCurated
    Sequence conflicti195 – 1951P → L in BAA00336. 1 PublicationCurated
    Sequence conflicti255 – 2551G → V in BAA00336. 1 PublicationCurated
    Sequence conflicti345 – 3451I → L AA sequence 1 PublicationCurated
    Sequence conflicti406 – 4094WPIY → PYI AA sequence 1 PublicationCurated
    Sequence conflicti443 – 4442Missing AA sequence 1 PublicationCurated
    Sequence conflicti448 – 4481G → Q AA sequence 1 PublicationCurated
    Sequence conflicti448 – 4481G → S AA sequence 1 PublicationCurated
    Sequence conflicti458 – 4581V → VGTTV AA sequence 1 PublicationCurated
    Sequence conflicti465 – 4662Missing AA sequence 1 PublicationCurated
    Sequence conflicti469 – 4713DGN → BGB AA sequence 1 PublicationCurated
    Sequence conflicti497 – 4971S → SD AA sequence 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiJK0201.
    JT0466.
    S04548. ALAS1.
    RefSeqiXP_001821436.1. XM_001821384.2.
    XP_001823941.1. XM_001823889.2.

    Genome annotation databases

    EnsemblFungiiCADAORAT00008024; CADAORAP00007860; CADAORAG00008024.
    CADAORAT00011354; CADAORAP00011123; CADAORAG00011354.
    GeneIDi5993438.
    5996200.
    KEGGiaor:AOR_1_1668144.
    aor:AOR_1_336094.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi JK0201.
    JT0466.
    S04548. ALAS1.
    RefSeqi XP_001821436.1. XM_001821384.2.
    XP_001823941.1. XM_001823889.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 22-499 [» ]
    3KWX X-ray 2.40 A 22-499 [» ]
    3VX0 X-ray 1.50 A 22-499 [» ]
    3VX1 X-ray 2.20 A 22-499 [» ]
    6TAA X-ray 2.10 A 22-499 [» ]
    7TAA X-ray 1.98 A 22-499 [» ]
    ProteinModelPortali P0C1B3.
    SMRi P0C1B3. Positions 22-497.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    Allergomei 86. Asp o 21.
    CAZyi GH13. Glycoside Hydrolase Family 13.

    PTM databases

    UniCarbKBi P0C1B3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADAORAT00008024 ; CADAORAP00007860 ; CADAORAG00008024 .
    CADAORAT00011354 ; CADAORAP00011123 ; CADAORAG00011354 .
    GeneIDi 5993438.
    5996200.
    KEGGi aor:AOR_1_1668144.
    aor:AOR_1_336094.

    Phylogenomic databases

    HOGENOMi HOG000165530.
    KOi K01176.
    OMAi SELYTWI.
    OrthoDBi EOG7RBZJ4.

    Miscellaneous databases

    EvolutionaryTracei P0C1B3.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR013777. 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 ]
    PANTHERi PTHR10357. PTHR10357. 1 hit.
    Pfami PF00128. Alpha-amylase. 1 hit.
    PF09260. DUF1966. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001024. Alph-amyl_fung. 1 hit.
    PRINTSi PR00110. ALPHAAMYLASE.
    SMARTi SM00642. Aamy. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiAMYA1_ASPOR
    AccessioniPrimary (citable) accession number: P0C1B3
    Secondary accession number(s): P10529
    , P11763, Q00250, Q2U6K7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2006
    Last sequence update: May 2, 2006
    Last modified: October 1, 2014
    This is version 67 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3