Reviewed, UniProtKB/Swiss-Prot Q02906 (AMYB_ASPAW)

Names and origin

Protein names

Recommended name:
    Alpha-amylase B
    EC=3.2.1.1
Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase B

Gene names

Name:

amyB

Organism

Aspergillus awamori

Taxonomic identifier

105351 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	499 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 oligosaccharides and polysaccharides.
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: UniProtKB-KW
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 – 499	478	Alpha-amylase B		PRO_0000001348
Sites
	Active site	227	1	Nucleophile By similarity
	Active site	251	1	Proton donor By similarity
	Active site	318	1	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
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)
	Q02906-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 740B96B11BC01A8A	FASTA	499	54,921
	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 AGSKICSSS

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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X52756 Genomic DNA. Translation: CAA36967.1.
PIR	B48305.
3D structure databases
SMR	Q02906. Positions 22-497.
ModBase	Search...
Protein family/group databases
CAZy	GH13. Glycoside Hydrolase Family 13.
Enzyme and pathway databases
BRENDA	3.2.1.1. 15245.
Family and domain databases
InterPro	IPR013777. A-amylase_fun. IPR015340. A_amylase_DUF1966_C. IPR006046. Glyco_hydro_13. IPR013780. Glyco_hydro_13_b. IPR006047. Glyco_hydro_13_cat_dom. IPR006589. Glyco_hydro_13_sub_cat_dom. IPR017853. Glyco_hydro_catalytic_core. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 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]
ProtoNet	Search...

Entry information

Entry name

AMYB_ASPAW

Accession

Primary (citable) accession number: Q02906

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 19, 2010
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)