Q02905 (AMYA_ASPAW) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-amylase A
EC=3.2.1.1

Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase A

Gene names

Name:

amyA

Organism

Aspergillus awamori (Black koji mold)

Taxonomic identifier

105351 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	498 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.
Cofactor	Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	carbohydrate catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	alpha-amylase activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 498	477	Alpha-amylase A		PRO_0000001347
Regions
	Region	230 – 231	2	Substrate binding By similarity
Sites
	Active site	227	1	Nucleophile By similarity
	Active site	251	1	Proton donor By similarity
	Metal binding	142	1	Calcium 1 By similarity
	Metal binding	183	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	196	1	Calcium 1 By similarity
	Metal binding	227	1	Calcium 2 By similarity
	Metal binding	231	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	251	1	Calcium 2 By similarity
	Binding site	56	1	Substrate By similarity
	Binding site	104	1	Substrate By similarity
	Binding site	143	1	Substrate By similarity
	Binding site	225	1	Substrate By similarity
	Binding site	255	1	Substrate; via amide nitrogen By similarity
	Binding site	317	1	Substrate By similarity
	Binding site	365	1	Substrate By similarity
	Site	318	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	218	1	N-linked (GlcNAc...) Potential
	Disulfide bond	51 ↔ 59		By similarity
	Disulfide bond	171 ↔ 185		By similarity
	Disulfide bond	261 ↔ 304		By similarity
	Disulfide bond	461 ↔ 496		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q02905 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 7658511BC01A8A01	FASTA	498	54,880
	10 20 30 40 50 60 MMVAWWSLFL YGLQVAAPAL AATPADWRSQ SIYFLLTDRF ARTDGSTTAT CNTADQKYCG 70 80 90 100 110 120 GTWQGIIDKL DYIQGMGFTA IWITPVTAQL PQTTAYGDAY HGYWQQDIYS LNENYGTADD 130 140 150 160 170 180 LKALSSALHE RGMYLMVDVV ANHMGYDGAG SSVDYSVFKP FSSQDYFHPF CFIQNYEDQT 190 200 210 220 230 240 QVEDCWLGDN TVSLPDLDTT KDVVKNEWYD WVGSLVSNYS IDGLRIDTVK HVQKDFWPGY 250 260 270 280 290 300 NKAAGVYCIG EVLDGDPAYT CPYQNVMDGV LNYPIYYPLL NAFKSTSGSM DDLYNMINTV 310 320 330 340 350 360 KSDCPDSTLL GTFVENHDNP RFASYTNDIA LAKNVAAFII LNDGIPIIYA GQEQHYAGGN 370 380 390 400 410 420 DPANREATWL SGYPTDSELY KLIASRNAIR NYAISKDTGF VTYKNWPIYK DDTTIPMRKG 430 440 450 460 470 480 TDGSQIVTIL SNKGASGDSY TLSLSGAGYT AGQQLTEVIG CTTVTVGSDG NVPVPMAGGL 490 PRVLYPTEKL AGSKICYG

References

[1]	"Cloning, characterization, and expression of two alpha-amylase genes from Aspergillus niger var. awamori." Korman D.R., Bayliss F.T., Barnett C.C., Carmona C.L., Kodama K.H., Royer T.J., Thompson S.A., Ward M., Wilson L.J., Berka R.M. Curr. Genet. 17:203-212(1990) [PubMed: 2340591] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: UVK143F.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X52755 Genomic DNA. Translation: CAA36966.1.
PIR	A48305.
3D structure databases
ProteinModelPortal	Q02905.
SMR	Q02905. Positions 22-496.
ModBase	Search...
Protein family/group databases
CAZy	GH13. Glycoside Hydrolase Family 13.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR013777. A-amylase_fun. IPR015340. A_amylase_DUF1966_C. IPR015902. Alpha_amylase. IPR006046. Glyco_hydro_13. IPR013780. Glyco_hydro_13_b. IPR006047. Glyco_hydro_13_cat_dom. IPR006589. Glyco_hydro_13_sub_cat_dom. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHER	PTHR10357. Alpha_amylase. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. PF09260. DUF1966. 1 hit. [Graphical view]
PIRSF	PIRSF001024. Alph-amyl_fung. 1 hit.
PRINTS	PR00110. ALPHAAMYLASE.
SMART	SM00642. Aamy. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

AMYA_ASPAW

Accession

Primary (citable) accession number: Q02905

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program