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Reviewed, UniProtKB/Swiss-Prot O74922 (AMY1_SCHPO)

Last modified November 24, 2009. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
Gene names
Name: aah1
ORF Names: SPCC757.12
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

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Protein attributes

Sequence length625 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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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.

Subcellular location

Cell membrane; Lipid-anchor › GPI-anchor Potential.

Sequence similarities

Belongs to the glycosyl hydrolase 13 family.

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Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
GPI-anchor
Glycoprotein
Lipoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcellular polysaccharide catabolic process

Inferred by curator. Source: GeneDB_SPombe

   Cellular componentanchored to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell surface

Inferred by curator. Source: GeneDB_SPombe

endoplasmic reticulum

Inferred from direct assay. Source: GeneDB_SPombe

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionalpha-amylase activity

Inferred from electronic annotation. Source: EC

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 603581Alpha-amylase 1
PRO_0000374015
Propeptide604 – 62522Removed in mature form Potential
PRO_0000374016

Regions

Compositional bias502 – 604103Ser-rich

Sites

Active site2291Nucleophile By similarity
Active site2531Proton donor By similarity
Active site3221 By similarity
Metal binding1431Calcium 1 By similarity
Metal binding1851Calcium 1; via carbonyl oxygen By similarity
Metal binding1981Calcium 1 By similarity
Metal binding2291Calcium 2 By similarity
Metal binding2531Calcium 2 By similarity

Amino acid modifications

Lipidation6031GPI-anchor amidated serine Potential
Glycosylation1531N-linked (GlcNAc...) Potential
Glycosylation1631N-linked (GlcNAc...) Potential
Glycosylation1801N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Potential
Glycosylation2601N-linked (GlcNAc...) Potential
Glycosylation2861N-linked (GlcNAc...) Potential
Glycosylation3311N-linked (GlcNAc...) Potential
Glycosylation4401N-linked (GlcNAc...) Potential
Glycosylation4611N-linked (GlcNAc...) Potential
Disulfide bond51 ↔ 59 By similarity
Disulfide bond263 ↔ 306 By similarity

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Sequences

Sequence LengthMass (Da)Tools
O74922-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 30A58CE6D6BC07B3

FASTA62568,087
        10         20         30         40         50         60 
MGFSKIALFS LFALFGLPTS LAKSSEEWRD RIIYQVITDR FAVDSDNTPD CSFDDSSYCG 

        70         80         90        100        110        120 
GTWSGIRSKL DYIQGMGFNA IWISPVEKNL EGSYGSDGEA YHGYWNTDFT QLNEHFGSED 

       130        140        150        160        170        180 
DLIDLITDMH NRDMWIMFDA LANSMAIPGP TDNISYSNLV PFNDSSYFHP YCWIDYGSNN 

       190        200        210        220        230        240 
NTDIEDCWTG DDNVILADLD IESTNVADYL HEHIHDMVER YQIDGIRIDA VKQMNPEFFP 

       250        260        270        280        290        300 
NYTSAAGVFA IGEMFSYDPN VSCSVRNYLD SITSYPIRQG IEFAFNYTGA AFEYLQEIDT 

       310        320        330        340        350        360 
QFQQACEGQD MSVIGNFLEN HDLPRYTSIT NDTSQDIGAI VFLLLHTGIP IIYYGEEQRL 

       370        380        390        400        410        420 
PGGSDTPENR AALWNYGYDT DANYYQTIRT AIALRKQAIS DSDSWTTDSH SYLDYDLRHA 

       430        440        450        460        470        480 
VVRKGDVLGV YTNYESSSDN VTYDVSSNFD DGTVLREVLS NTTTTVGSSG ALHVTVVSGL 

       490        500        510        520        530        540 
PQVYYPEASL TSFGNFLGTA TSYSSASASY PSTSMSASLS SVHTSSATSS SKSSSSSSSR 

       550        560        570        580        590        600 
SGSSSSSSSR SGSTSSSGSS HTITSTSQSV HTSGSSTSTS SVAVTSTAYS SSSSSSSSSS 

       610        620 
IESSANAVRV SILGVAAFIA IVLFI

« Hide

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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: ATCC 38366 / 972.
[2]"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.

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Cross-references

Sequence databases

CU329672 Genomic DNA. Translation: CAA21237.1.
PIRT41603.
RefSeqNP_587687.1.

3D structure databases

HSSPHSSP built from PDB template 2AAA based on UniProtKB P56271.
ModBaseSearch...

Genome annotation databases

GeneID2538825.
GenomeReviewsGene locus aah1 in contig CU329672_GR.
KEGGspo:SPCC757.12.
NMPDRfig|4896.1.peg.25.

Organism-specific databases

GeneDB_SpombeSPCC757.12.

Phylogenomic databases

OrthoDBEOG9BVT9P

Gene expression databases

ArrayExpressO74922.

Family and domain databases

InterProIPR013777. A-amylase_fun.
IPR015340. Alpha_amylase_DUF1966_C.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat.
IPR006589. Glyco_hydro_13_sub_cat.
IPR017853. Glyco_hydro_catalytic_core.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 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]
ProtoNetSearch...

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Entry information

Entry nameAMY1_SCHPO
AccessionPrimary (citable) accession number: O74922
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: November 1, 1998
Last modified: November 24, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents