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Protein

Alpha-amylase A

Gene

amyA

Organism
Aspergillus awamori (Black koji mold)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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+By similarityNote: Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei56SubstrateBy similarity1
Binding sitei104SubstrateBy similarity1
Metal bindingi142Calcium 1By similarity1
Binding sitei143SubstrateBy similarity1
Metal bindingi183Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi196Calcium 1By similarity1
Binding sitei225SubstrateBy similarity1
Active sitei227NucleophileBy similarity1
Metal bindingi227Calcium 2By similarity1
Metal bindingi231Calcium 1; via carbonyl oxygenBy similarity1
Active sitei251Proton donorBy similarity1
Metal bindingi251Calcium 2By similarity1
Binding sitei255Substrate; via amide nitrogenBy similarity1
Binding sitei318SubstrateBy similarity1
Sitei318Transition state stabilizerBy similarity1
Binding sitei365SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism
LigandCalcium, Metal-binding

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase A (EC:3.2.1.1)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase A
Gene namesi
Name:amyA
OrganismiAspergillus awamori (Black koji mold)
Taxonomic identifieri105351 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000000134722 – 498Alpha-amylase AAdd BLAST477

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi51 ↔ 59By similarity
Disulfide bondi171 ↔ 185By similarity
Glycosylationi218N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi261 ↔ 304By similarity
Disulfide bondi461 ↔ 496By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ02905.

Structurei

3D structure databases

ProteinModelPortaliQ02905.
SMRiQ02905.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni230 – 231Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiView protein in InterPro
IPR013777. A-amylase-like.
IPR015340. A_amylase_DUF1966_C.
IPR006046. Alpha_amylase.
IPR006047. Glyco_hydro_13_cat_dom.
IPR017853. Glycoside_hydrolase_SF.
PfamiView protein in Pfam
PF00128. Alpha-amylase. 1 hit.
PF09260. DUF1966. 1 hit.
PIRSFiPIRSF001024. Alph-amyl_fung. 1 hit.
PRINTSiPR00110. ALPHAAMYLASE.
SMARTiView protein in SMART
SM00642. Aamy. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q02905-1 [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 KLIASRNAIR NYAISKDTGF
410 420 430 440 450
VTYKNWPIYK DDTTIPMRKG TDGSQIVTIL SNKGASGDSY TLSLSGAGYT
460 470 480 490
AGQQLTEVIG CTTVTVGSDG NVPVPMAGGL PRVLYPTEKL AGSKICYG
Length:498
Mass (Da):54,880
Last modified:October 1, 1996 - v1
Checksum:i7658511BC01A8A01
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52755 Genomic DNA. Translation: CAA36966.1.
PIRiA48305.

Similar proteinsi

Entry informationi

Entry nameiAMYA_ASPAW
AccessioniPrimary (citable) accession number: Q02905
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 27, 2017
This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families