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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: 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.Curated

Cofactori

Ca2+3 PublicationsNote: Binds 2 calcium ions per subunit (PubMed:6609921, PubMed:9283074, PubMed:16880540). Calcium is inhibitory at high concentrations.Curated3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei56Substrate1 Publication1
Binding sitei104Substrate1 Publication1
Metal bindingi142Calcium 13 Publications1
Binding sitei143Substrate1 Publication1
Metal bindingi183Calcium 1; via carbonyl oxygen3 Publications1
Metal bindingi196Calcium 13 Publications1
Binding sitei225Substrate1 Publication1
Active sitei227Nucleophile1 Publication1
Metal bindingi227Calcium 21 Publication1
Metal bindingi231Calcium 1; via carbonyl oxygen3 Publications1
Active sitei251Proton donor1 Publication1
Metal bindingi251Calcium 21 Publication1
Binding sitei255Substrate; via amide nitrogen1 Publication1
Binding sitei318Substrate1 Publication1
Sitei318Transition state stabilizer1 Publication1
Binding sitei365Substrate1 Publication1

GO - Molecular functioni

  • alpha-amylase activity Source: ASPGD
  • calcium ion binding Source: InterPro

GO - Biological processi

  • 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:3.2.1.1Curated)
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
Proteomesi
  • UP000006564 Componentsi: Chromosome 3, Chromosome 5

Subcellular locationi

GO - Cellular componenti

  • cell septum Source: ASPGD
  • cell wall-bounded periplasmic space Source: ASPGD
  • extracellular region Source: UniProtKB-SubCell
  • fungal-type cell wall Source: ASPGD
  • hyphal septin band Source: ASPGD
  • spitzenkorper Source: ASPGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 211 PublicationAdd BLAST21
ChainiPRO_000000134922 – 499Alpha-amylase A type-1/2Add BLAST478

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi51 ↔ 59Combined sources3 Publications
Disulfide bondi171 ↔ 185Combined sources3 Publications
GlycosylationiCAR_000125218N-linked (GlcNAc...)1 Publication1
Disulfide bondi261 ↔ 304Combined sources3 Publications
Disulfide bondi461 ↔ 496Combined sources3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

UniCarbKBiP0C1B3.

Interactioni

Subunit structurei

Monomer.2 Publications

Structurei

Secondary structure

1499
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi24 – 27Combined sources4
Beta strandi32 – 35Combined sources4
Helixi37 – 40Combined sources4
Helixi53 – 55Combined sources3
Helixi63 – 68Combined sources6
Helixi70 – 74Combined sources5
Turni75 – 77Combined sources3
Beta strandi80 – 83Combined sources4
Beta strandi87 – 89Combined sources3
Beta strandi104 – 111Combined sources8
Turni113 – 115Combined sources3
Helixi118 – 130Combined sources13
Beta strandi134 – 139Combined sources6
Beta strandi146 – 148Combined sources3
Helixi150 – 152Combined sources3
Helixi155 – 157Combined sources3
Beta strandi158 – 160Combined sources3
Helixi164 – 166Combined sources3
Helixi176 – 178Combined sources3
Helixi179 – 184Combined sources6
Beta strandi185 – 188Combined sources4
Beta strandi190 – 194Combined sources5
Helixi202 – 219Combined sources18
Beta strandi223 – 227Combined sources5
Helixi229 – 231Combined sources3
Helixi234 – 236Combined sources3
Helixi237 – 244Combined sources8
Beta strandi246 – 250Combined sources5
Helixi257 – 260Combined sources4
Helixi261 – 265Combined sources5
Beta strandi267 – 271Combined sources5
Helixi273 – 283Combined sources11
Helixi290 – 303Combined sources14
Helixi307 – 309Combined sources3
Beta strandi310 – 312Combined sources3
Helixi322 – 325Combined sources4
Helixi329 – 341Combined sources13
Beta strandi342 – 349Combined sources8
Helixi352 – 354Combined sources3
Turni361 – 364Combined sources4
Helixi368 – 371Combined sources4
Beta strandi375 – 377Combined sources3
Helixi378 – 396Combined sources19
Turni398 – 402Combined sources5
Beta strandi406 – 410Combined sources5
Beta strandi412 – 421Combined sources10
Turni422 – 424Combined sources3
Beta strandi426 – 431Combined sources6
Beta strandi440 – 444Combined sources5
Beta strandi454 – 457Combined sources4
Turni458 – 461Combined sources4
Beta strandi462 – 465Combined sources4
Beta strandi468 – 470Combined sources3
Beta strandi472 – 476Combined sources5
Beta strandi482 – 486Combined sources5
Helixi487 – 490Combined sources4
Beta strandi493 – 495Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C1B3.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni230 – 231Substrate binding1 Publication2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000165530.
KOiK01176.
OMAiVLNYAMY.
OrthoDBiEOG092C1HLH.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR015340. A_amylase_DUF1966_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
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]
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)DescriptionActionsGraphical viewLength
Sequence conflicti93 – 94TT → DC AA sequence (Ref. 5) Curated2
Sequence conflicti101H → T AA sequence (Ref. 5) Curated1
Sequence conflicti106Q → T AA sequence (Ref. 5) Curated1
Sequence conflicti184D → Y in BAA00336 (Ref. 3) Curated1
Sequence conflicti195P → L in BAA00336 (Ref. 3) Curated1
Sequence conflicti255G → V in BAA00336 (Ref. 3) Curated1
Sequence conflicti345I → L AA sequence (Ref. 5) Curated1
Sequence conflicti406 – 409WPIY → PYI AA sequence (Ref. 5) Curated4
Sequence conflicti443 – 444Missing AA sequence (Ref. 7) Curated2
Sequence conflicti448G → Q AA sequence (Ref. 7) Curated1
Sequence conflicti448G → S AA sequence (Ref. 5) Curated1
Sequence conflicti458V → VGTTV AA sequence (Ref. 7) Curated1
Sequence conflicti465 – 466Missing AA sequence (Ref. 7) Curated2
Sequence conflicti469 – 471DGN → BGB AA sequence (Ref. 7) Curated3
Sequence conflicti497S → SD AA sequence (Ref. 5) Curated1

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

EnsemblFungiiBAE59434; BAE59434; AO090023000944.
BAE62808; BAE62808; AO090120000196.
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.
PIRiJK0201.
JT0466.
S04548. ALAS1.
RefSeqiXP_001821436.1. XM_001821384.2.
XP_001823941.1. XM_001823889.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei86. Asp o 21.
CAZyiGH13. Glycoside Hydrolase Family 13.

PTM databases

UniCarbKBiP0C1B3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAE59434; BAE59434; AO090023000944.
BAE62808; BAE62808; AO090120000196.
GeneIDi5993438.
5996200.
KEGGiaor:AOR_1_1668144.
aor:AOR_1_336094.

Phylogenomic databases

HOGENOMiHOG000165530.
KOiK01176.
OMAiVLNYAMY.
OrthoDBiEOG092C1HLH.

Miscellaneous databases

EvolutionaryTraceiP0C1B3.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR015340. A_amylase_DUF1966_C.
IPR006046. Alpha_amylase.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
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]
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

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 30, 2016
This is version 82 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.