Reviewed, UniProtKB/Swiss-Prot P19269 (AMY1_DEBOC)

Names and origin

Protein names

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

Gene names

Name:

AMY1

Organism

Debaryomyces occidentalis (Yeast) (Schwanniomyces occidentalis)

Taxonomic identifier

27300 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Debaryomyces

Protein attributes

Sequence length	512 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.
Enzyme regulation	Alpha-amylase expression underlies catabolite repression by glucose.
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 – 25	25	Potential
	Chain	26 – 512	487	Alpha-amylase 1		PRO_0000001352
Sites
	Active site	242	1	Nucleophile By similarity
	Active site	266	1	Proton donor By similarity
	Active site	333	1	By similarity
	Metal binding	157	1	Calcium 1 By similarity
	Metal binding	198	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	211	1	Calcium 1 By similarity
	Metal binding	242	1	Calcium 2 By similarity
	Metal binding	246	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	266	1	Calcium 2 By similarity
Amino acid modifications
	Glycosylation	233	1	N-linked (GlcNAc...) Probable
	Disulfide bond	66 ↔ 74		By similarity
	Disulfide bond	186 ↔ 200		By similarity
	Disulfide bond	276 ↔ 319		By similarity
	Disulfide bond	475 ↔ 510		By similarity
Natural variations
	Natural variant	32	1	M → K in strain: CCRC 21164 and ATCC 26077 / CBS 2863.
	Natural variant	36	1	S → G in strain: CCRC 21164.
	Natural variant	73	1	Y → I in strain: ATCC 26077 / CBS 2863.
	Natural variant	280	1	N → S in strain: CCRC 21164.
	Natural variant	350	1	D → A in strain: CCRC 21164 and ATCC 26077 / CBS 2863.
	Natural variant	479	1	L → S in strain: CCRC 21164 and ATCC 26077 / CBS 2863.
	Natural variant	483	1	S → F in strain: CCRC 21164.

Sequences

	Sequence		Length	Mass (Da)
	P19269-1 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: 857552B2CF60F965	FASTA	512	56,527
	10 20 30 40 50 60 MRFSTEGFTS KVVAAILAFS RLVSAQPIIF DMRDVSSSAD KWKDQSIYQI VTDRFARSDG 70 80 90 100 110 120 STTADCLVSD RKYCGGSYKG IIDKLDYIQG MGFTAIWISP VVEQIPDNTA YGYAYHGYWM 130 140 150 160 170 180 KNIDELNTNF GTADELKQLA SELHSRSMLL MVDVVYNHYA WNGDGSSVDY SSFTPFNQQS 190 200 210 220 230 240 YFHDYCLITN YNDQTNVEDC WEGDTEVSLP DLSTEDNEVI GVFQTWVSDF VQNYSIDGLR 250 260 270 280 290 300 IDSAKHVDTA SLTKFEDASG VYNLGEVYQG DPTYTCPYQN YMKGVTNYPL YYPVYRFFSD 310 320 330 340 350 360 TSATSSELTS MISTLQSSCS DVSLLGNFIE NHDQVRFPSV TSDTSLIKND MAFIILGDGI 370 380 390 400 410 420 PIIYYGQEQG LNGGSDPANR EALWLSGYNT DSEYYELISK LNQIRNQAIK KDSAYSTYKS 430 440 450 460 470 480 SVVSSSDHYI ATRKGSDANQ LISIFNNLGS NGSQDITVSN TGYSSGDKVI DIISCNSVLA 490 500 510 GDSGSLSVSI SGGMPQVYAP SSVLSGSGIC NQ

References

[1]	"Analysis of the alpha-amylase gene of Schwanniomyces occidentalis and the secretion of its gene product in transformants of different yeast genera." Strasser A.W.M., Selk R., Dohmen R.J., Niermann T., Bielefeld M., Seeboth P., Tu G., Hollenberg C.P. Eur. J. Biochem. 184:699-706(1989) [PubMed: 2806251] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 26076 / CBS 2864 / CCRC 22059 / NRRL Y-2470.
[2]	"The nucleotide sequence of Schwanniomyces occidentalis alpha-amylase gene." Wu F.M., Wang T.T., Hsu W.H. FEMS Microbiol. Lett. 66:313-318(1991) [PubMed: 1769525] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: CCRC 21164.
[3]	"Nucleotide sequence of the extracellular alpha-amylase gene in the yeast Schwanniomyces occidentalis ATCC 26077." Park J.C., Bai S., Tai C.Y., Chun S.B. FEMS Microbiol. Lett. 72:17-23(1992) [PubMed: 1612414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 26077 / CBS 2863 / IFO 1840 / JCM 8124 / NRRL Y-2477.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S77586 Genomic DNA. Translation: AAB21151.2. X16040 Genomic DNA. Translation: CAA34162.1. X62079 Genomic DNA. Translation: CAA43995.1. S38381 Genomic DNA. Translation: AAB22383.2.
PIR	S06115. S23355.
3D structure databases
SMR	P19269. Positions 39-511.
ModBase	Search...
Protein family/group databases
CAZy	GH13. Glycoside Hydrolase Family 13.
Enzyme and pathway databases
BRENDA	3.2.1.1. 290444.
Family and domain databases
InterPro	IPR013777. A-amylase_fun. IPR015340. A_amylase_DUF1966_C. 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.
SMART	SM00642. Aamy. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMY1_DEBOC

Accession

Primary (citable) accession number: P19269

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	January 19, 2010
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)