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Q09840 (AMY2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-amylase 2
EC=3.2.1.1
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene names
Name:aah2
ORF Names:SPAC23D3.14c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length581 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.

Subcellular location

Cell membrane; Lipid-anchor › GPI-anchor Potential Ref.2 Ref.4.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 551527Alpha-amylase 2
PRO_0000001355
Propeptide552 – 58130Removed in mature form Potential
PRO_0000255452

Regions

Region236 – 2372Substrate binding By similarity

Sites

Active site2331Nucleophile By similarity
Active site2571Proton donor By similarity
Metal binding1471Calcium 1 By similarity
Metal binding2021Calcium 1 By similarity
Metal binding2331Calcium 2 By similarity
Metal binding2371Calcium 1; via carbonyl oxygen By similarity
Metal binding2571Calcium 2 By similarity
Binding site1091Substrate By similarity
Binding site2311Substrate By similarity
Binding site2611Substrate; via amide nitrogen By similarity
Binding site3241Substrate By similarity
Binding site3721Substrate By similarity
Site3251Transition state stabilizer By similarity

Amino acid modifications

Lipidation5511GPI-anchor amidated serine Potential
Glycosylation2911N-linked (GlcNAc...) Potential
Glycosylation3321N-linked (GlcNAc...) Potential
Disulfide bond56 ↔ 64 By similarity
Disulfide bond176 ↔ 191 By similarity
Disulfide bond267 ↔ 311 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q09840 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: FE9DE99D323E1890

FASTA58167,005
        10         20         30         40         50         60 
MNYRRNICLR IGWMLLFAFI PAYAGHSAEE WKRRSIYQII TDRFSLEEGA TERIPCDPVR 

        70         80         90        100        110        120 
FMYCGGTWNG IRNHLDYIQG MGFDAIWISP IFENVEGNDI DGSSYHGYWT TNLYELNHHF 

       130        140        150        160        170        180 
GTKEEFMELI QELHKRDIWI LLDVAINSMA INGPLEQMSF EKVIPFNDAS FFHPHCWVDY 

       190        200        210        220        230        240 
ESNDIESVQN CWLGDENLLL ADVDTENEVV LSVLEKWIKN VVQEYDIDGI RFDAIKHAPI 

       250        260        270        280        290        300 
EFWLRMSKAA DIFTIGEYFT GSPAEACDYQ NSGLDSFLNF PLYWPITWAF NNTGLQCEAL 

       310        320        330        340        350        360 
AIAINQINEE CNDINVLGTF IGNHDLPRIS HNNTDQARIM NAITFVMMWD GIPIIYYGTE 

       370        380        390        400        410        420 
QNFNSYHDPF NREALWLSNF DMENVYYKLI GILNRFRKSV QRQEENYVNT RSTILSVKIH 

       430        440        450        460        470        480 
HIVVQKLNVI TVLNNYGIHN EERLSIVFKP LGASPKDTFF DIINNQKYVV NTDGTLKVVI 

       490        500        510        520        530        540 
TNGFPIVLYP TSKIETSLPQ FTATLLPEIT FVPSITVTTH YVLPTLLAPL GYDIREHPGG 

       550        560        570        580 
QQFWNTLTAK SEAKTIRSFT KLKLFILLIA VPFALPMIIL I

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"Genome-wide identification of fungal GPI proteins."
De Groot P.W., Hellingwerf K.J., Klis F.M.
Yeast 20:781-796(2003) [PubMed: 12845604] [Abstract]
Cited for: PROBABLE GPI-ANCHOR.
[3]"An alpha-amylase homologue, aah3, encodes a GPI-anchored membrane protein required for cell wall integrity and morphogenesis in Schizosaccharomyces pombe."
Morita T., Tanaka N., Hosomi A., Giga-Hama Y., Takegawa K.
Biosci. Biotechnol. Biochem. 70:1454-1463(2006) [PubMed: 16751704] [Abstract]
Cited for: GENE NAME.
[4]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329670 Genomic DNA. Translation: CAA91249.1.
PIRS62505. T38289.
RefSeqNP_594551.1. NM_001019980.1.

3D structure databases

ProteinModelPortalQ09840.
ModBaseSearch...

Protein family/group databases

CAZyGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC23D3.14c.1; SPAC23D3.14c.1:pep; SPAC23D3.14c.
GeneID2541501.
GenomeReviewsGene locus aah2 in contig CU329670_GR.
KEGGspo:SPAC23D3.14c.
NMPDRfig|4896.1.peg.4521.

Organism-specific databases

GeneDB_SpombeSPAC23D3.14c.

Phylogenomic databases

eggNOGfuNOG06463.
GeneTreeEFGT00050000000134.
HOGENOMHBG324773.
OMALPDLYTE.
OrthoDBEOG4DNJD2.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-002648-MONOMER.

Gene expression databases

ArrayExpressQ09840.

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.
KOK01176.
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 nameAMY2_SCHPO
AccessionPrimary (citable) accession number: Q09840
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: December 14, 2011
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents