P21567 (AMY1_SACFI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-amylase
EC=3.2.1.1

Gene names

Name:

ALP1

Organism

Saccharomycopsis fibuligera (Yeast)

Taxonomic identifier

4944 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycopsidaceae › Saccharomycopsis

Protein attributes

Sequence length	494 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 – 26	26	Potential
	Chain	27 – 494	468	Alpha-amylase		PRO_0000001351
Regions
	Region	236 – 237	2	Substrate binding By similarity
Sites
	Active site	233	1	Nucleophile By similarity
	Active site	257	1	Proton donor By similarity
	Metal binding	148	1	Calcium 1 By similarity
	Metal binding	202	1	Calcium 1 By similarity
	Metal binding	233	1	Calcium 2 By similarity
	Metal binding	237	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	257	1	Calcium 2 By similarity
	Binding site	110	1	Substrate By similarity
	Binding site	149	1	Substrate By similarity
	Binding site	231	1	Substrate By similarity
	Binding site	261	1	Substrate; via amide nitrogen By similarity
	Binding site	323	1	Substrate By similarity
	Binding site	371	1	Substrate By similarity
	Site	324	1	Transition state stabilizer By similarity
Amino acid modifications
	Glycosylation	224	1	N-linked (GlcNAc...) Probable
	Disulfide bond	57 ↔ 65		By similarity
	Disulfide bond	177 ↔ 191		By similarity
	Disulfide bond	267 ↔ 310		By similarity
	Disulfide bond	462 ↔ 493		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P21567 [UniParc]. Last modified May 1, 1991. Version 1. Checksum: 7F7D8FFD6BF58B67	FASTA	494	54,387
	10 20 30 40 50 60 MQISKAALLA SLAALVYAQP VTLFKRETNA DKWRSQSIYQ IVTDRFARTD GDTSASCNTE 70 80 90 100 110 120 DRLYCGGSFQ GIIKKLDYIK DMGFTAIWIS PVVENIPDNT AYGYAYHGYW MKNIYKINEN 130 140 150 160 170 180 FGTADDLKSL AQELHDRDML LMVDIVTNHY GSDGSGDSID YSEYTPFNDQ KYFHNYCLIS 190 200 210 220 230 240 NYDDQAQVQS CWEGDSSVAL PDLRTEDSDV ASVFNSWVKD FVGNYSIDGL RIDSAKHVDQ 250 260 270 280 290 300 GFFPDFVSAS GVYSVGEVFQ GDPAYTCPYQ NYIPGVSNYP LYYPTTRFFK TTDSSSSELT 310 320 330 340 350 360 QMISSVASSC SDPTLLTNFV ENHDNERFAS MTSDQSLISN AIAFVLLGDG IPVIYYGQEQ 370 380 390 400 410 420 GLSGKSDPNN REALWLSGYN KESDYYKLIA KANAARNAAV YQDSSYATSQ LSVIFSNDHV 430 440 450 460 470 480 IATKRGSVVS VFNNLGSSGS SDVTISNTGY SSGEDLVEVL TCSTVSGSSD LQVSIQGGQP 490 QIFVPAKYAS DICS

References

[1]	"Nucleotide sequence of the alpha-amylase gene (ALP1) in the yeast Saccharomycopsis fibuligera." Itoh T., Yamashita I., Fukui S. FEBS Lett. 219:339-342(1987) [PubMed: 3497057] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X05791 Genomic DNA. Translation: CAA29233.1.
PIR	ALBYAF. S00064.
3D structure databases
ProteinModelPortal	P21567.
SMR	P21567. Positions 31-494.
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

AMY1_SACFI

Accession

Primary (citable) accession number: P21567

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1991
Last modified:	December 14, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program