Q08806 (AMY2_SCHOC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-amylase 2
EC=3.2.1.1

Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase 2

Gene names

Name:

SWA2

Organism

Schwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis)

Taxonomic identifier

27300 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Schwanniomyces

Protein attributes

Sequence length	507 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 – 20	20	Potential
	Chain	21 – 507	487	Alpha-amylase 2		PRO_0000001353
Regions
	Region	241 – 242	2	Substrate binding By similarity
Sites
	Active site	238	1	Nucleophile By similarity
	Active site	262	1	Proton donor By similarity
	Metal binding	153	1	Calcium 1 By similarity
	Metal binding	194	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	207	1	Calcium 1 By similarity
	Metal binding	238	1	Calcium 2 By similarity
	Metal binding	242	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	262	1	Calcium 2 By similarity
	Binding site	115	1	Substrate By similarity
	Binding site	154	1	Substrate By similarity
	Binding site	236	1	Substrate By similarity
	Binding site	266	1	Substrate; via amide nitrogen By similarity
	Binding site	328	1	Substrate By similarity
	Binding site	376	1	Substrate By similarity
	Site	329	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	229	1	N-linked (GlcNAc...) Probable
	Disulfide bond	62 ↔ 70		By similarity
	Disulfide bond	182 ↔ 196		By similarity
	Disulfide bond	272 ↔ 315		By similarity
	Disulfide bond	470 ↔ 505		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q08806 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 3A562E95BD8AAD63	FASTA	507	55,967
	10 20 30 40 50 60 MKFATILSTT ALALSSLVAS KPIFLSKRDA GSSAAAAWRS ESIYQLVTDR FARTDGSTSA 70 80 90 100 110 120 TCNTGDRVYC GGTFQGIIDK LDYIQGMGFT AIWISPVVEQ IPDDTGYGYA YHGYWMKDIY 130 140 150 160 170 180 AINSNFGTAD DLKNLSNELH KRNMKLMVDI VTNHYAWNGA GSSVAYSNYN PFNQQSYFHD 190 200 210 220 230 240 YCLITNYDDQ TNVEDCWEGD NTVSLPDLRT EDSDVSSIFN LWVAELVSNY SIDGLRIDSA 250 260 270 280 290 300 KHVDESFYPS FQSAAGVYLL GEVYDGDPAY TCPYQNYMSG VTNYPLYYPM LRFFQGTSNS 310 320 330 340 350 360 VDELNAMISS LESDCKDITL LGNFIENHDQ PRLPSYTSDS ALIKNAIAFN LMSDGIPIIY 370 380 390 400 410 420 YGQEQGYSGS SDPNNREALW LSGYSTSNGY YKLISSVNQI RNQAIYKDSK YTTYWSDVLY 430 440 450 460 470 480 ASGHVIALQR GADDQRIVSV FNNLGSSGSQ TVTFSTKYSG GEKVVDVLTC QTSYANSDST 490 500 LTVSISGGAP RIYAPASLIA NSGICNF

References

[1]	"Molecular structure of the SWA2 gene encoding an AMY1-related alpha-amylase from Schwanniomyces occidentalis." Claros M.G., Abarca D., Fernandez-Lobato M., Jimenez A. Curr. Genet. 24:75-83(1993) [PubMed: 8358835] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 26077 / CBS 2863 / JCM 8124 / BCRC 20332 / NBRC 1840 / NRRL Y-2477.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X73497 Genomic DNA. Translation: CAA51912.1.
PIR	S33921.
3D structure databases
ProteinModelPortal	Q08806.
SMR	Q08806. Positions 36-506.
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. 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.
SMART	SM00642. Aamy. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

AMY2_SCHOC

Accession

Primary (citable) accession number: Q08806

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program