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P0C1B3

- AMYA1_ASPOR

UniProt

P0C1B3 - AMYA1_ASPOR

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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

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

Ca2+Note: 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
Complete GO annotation...

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
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MMVAWWSLFL YGLQVAAPAL AATPADWRSQ SIYFLLTDRF ARTDGSTTAT
60 70 80 90 100
CNTADQKYCG GTWQGIIDKL DYIQGMGFTA IWITPVTAQL PQTTAYGDAY
110 120 130 140 150
HGYWQQDIYS LNENYGTADD LKALSSALHE RGMYLMVDVV ANHMGYDGAG
160 170 180 190 200
SSVDYSVFKP FSSQDYFHPF CFIQNYEDQT QVEDCWLGDN TVSLPDLDTT
210 220 230 240 250
KDVVKNEWYD WVGSLVSNYS IDGLRIDTVK HVQKDFWPGY NKAAGVYCIG
260 270 280 290 300
EVLDGDPAYT CPYQNVMDGV LNYPIYYPLL NAFKSTSGSM DDLYNMINTV
310 320 330 340 350
KSDCPDSTLL GTFVENHDNP RFASYTNDIA LAKNVAAFII LNDGIPIIYA
360 370 380 390 400
GQEQHYAGGN DPANREATWL SGYPTDSELY KLIASANAIR NYAISKDTGF
410 420 430 440 450
VTYKNWPIYK DDTTIAMRKG TDGSQIVTIL SNKGASGDSY TLSLSGAGYT
460 470 480 490
AGQQLTEVIG CTTVTVGSDG NVPVPMAGGL PRVLYPTEKL AGSKICSSS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 68 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