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P19269 (AMY1_SCHOC) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alpha-amylase 1
EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase 1
Gene names
Name:AMY1
OrganismSchwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis)
Taxonomic identifier27300 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Schwanniomyces

Protein attributes

Sequence length512 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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.

Enzyme regulation

Alpha-amylase expression underlies catabolite repression by glucose.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological processcarbohydrate catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionalpha-amylase activity

Inferred from electronic annotation. Source: EC

calcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 512487Alpha-amylase 1
PRO_0000001352

Regions

Region245 – 2462Substrate binding By similarity

Sites

Active site2421Nucleophile By similarity
Active site2661Proton donor By similarity
Metal binding1571Calcium 1 By similarity
Metal binding1981Calcium 1; via carbonyl oxygen By similarity
Metal binding2111Calcium 1 By similarity
Metal binding2421Calcium 2 By similarity
Metal binding2461Calcium 1; via carbonyl oxygen By similarity
Metal binding2661Calcium 2 By similarity
Binding site1191Substrate By similarity
Binding site1581Substrate By similarity
Binding site2401Substrate By similarity
Binding site2701Substrate; via amide nitrogen By similarity
Binding site3321Substrate By similarity
Binding site3801Substrate By similarity
Site3331Transition state stabilizer By similarity

Amino acid modifications

Glycosylation2331N-linked (GlcNAc...) Probable
Disulfide bond66 ↔ 74 By similarity
Disulfide bond186 ↔ 200 By similarity
Disulfide bond276 ↔ 319 By similarity
Disulfide bond475 ↔ 510 By similarity

Natural variations

Natural variant321M → K in strain: CCRC 21164 and ATCC 26077 / CBS 2863.
Natural variant361S → G in strain: CCRC 21164.
Natural variant731Y → I in strain: ATCC 26077 / CBS 2863.
Natural variant2801N → S in strain: CCRC 21164.
Natural variant3501D → A in strain: CCRC 21164 and ATCC 26077 / CBS 2863.
Natural variant4791L → S in strain: CCRC 21164 and ATCC 26077 / CBS 2863.
Natural variant4831S → F in strain: CCRC 21164.

Sequences

Sequence LengthMass (Da)Tools
P19269 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 857552B2CF60F965

FASTA51256,527
        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

« Hide

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 / DSM 3794 / CBS 2864 / BCRC 22059 / NCYC 954 / 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: BCRC 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 / JCM 8124 / BCRC 20332 / NBRC 1840 / NRRL Y-2477.
+Additional computationally mapped references.

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.
PIRS06115.
S23355.

3D structure databases

ProteinModelPortalP19269.
SMRP19269. Positions 39-511.
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR013777. 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]
Gene3DG3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHERPTHR10357. Alpha_amylase. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF09260. DUF1966. 1 hit.
[Graphical view]
PIRSFPIRSF001024. Alph-amyl_fung. 1 hit.
SMARTSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAMY1_SCHOC
AccessionPrimary (citable) accession number: P19269
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: December 14, 2011
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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