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Protein

Alpha-amylase 2

Gene

aah2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.

Cofactori

Ca2+By similarityNote: Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei109 – 1091SubstrateBy similarity
Metal bindingi147 – 1471Calcium 1By similarity
Metal bindingi202 – 2021Calcium 1By similarity
Binding sitei231 – 2311SubstrateBy similarity
Active sitei233 – 2331NucleophileBy similarity
Metal bindingi233 – 2331Calcium 2By similarity
Metal bindingi237 – 2371Calcium 1; via carbonyl oxygenBy similarity
Active sitei257 – 2571Proton donorBy similarity
Metal bindingi257 – 2571Calcium 2By similarity
Binding sitei261 – 2611Substrate; via amide nitrogenBy similarity
Binding sitei324 – 3241SubstrateBy similarity
Sitei325 – 3251Transition state stabilizerBy similarity
Binding sitei372 – 3721SubstrateBy similarity

GO - Molecular functioni

  1. alpha-amylase activity Source: UniProtKB-EC
  2. calcium ion binding Source: InterPro

GO - Biological processi

  1. cellular polysaccharide catabolic process Source: PomBase
  2. extracellular polysaccharide metabolic process Source: PomBase
  3. fungal-type cell wall biogenesis Source: PomBase
  4. regulation of cell shape Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase 2 (EC:3.2.1.1)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene namesi
Name:aah2
ORF Names:SPAC23D3.14c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC23D3.14c.

Subcellular locationi

GO - Cellular componenti

  1. anchored component of external side of plasma membrane Source: PomBase
  2. endoplasmic reticulum Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 551527Alpha-amylase 2PRO_0000001355Add
BLAST
Propeptidei552 – 58130Removed in mature formSequence AnalysisPRO_0000255452Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi56 ↔ 64By similarity
Disulfide bondi176 ↔ 191By similarity
Disulfide bondi267 ↔ 311By similarity
Glycosylationi291 – 2911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi332 – 3321N-linked (GlcNAc...)Sequence Analysis
Lipidationi551 – 5511GPI-anchor amidated serineSequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Interactioni

Protein-protein interaction databases

MINTiMINT-4695620.
STRINGi4896.SPAC23D3.14c-1.

Structurei

3D structure databases

ProteinModelPortaliQ09840.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni236 – 2372Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0366.
HOGENOMiHOG000165530.
InParanoidiQ09840.
KOiK01176.
OMAiCWIDYSN.
OrthoDBiEOG7RBZJ4.
PhylomeDBiQ09840.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR013777. A-amylase_fun.
IPR015340. A_amylase_DUF1966_C.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF09260. DUF1966. 1 hit.
[Graphical view]
PIRSFiPIRSF001024. Alph-amyl_fung. 1 hit.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q09840-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNYRRNICLR IGWMLLFAFI PAYAGHSAEE WKRRSIYQII TDRFSLEEGA
60 70 80 90 100
TERIPCDPVR FMYCGGTWNG IRNHLDYIQG MGFDAIWISP IFENVEGNDI
110 120 130 140 150
DGSSYHGYWT TNLYELNHHF GTKEEFMELI QELHKRDIWI LLDVAINSMA
160 170 180 190 200
INGPLEQMSF EKVIPFNDAS FFHPHCWVDY ESNDIESVQN CWLGDENLLL
210 220 230 240 250
ADVDTENEVV LSVLEKWIKN VVQEYDIDGI RFDAIKHAPI EFWLRMSKAA
260 270 280 290 300
DIFTIGEYFT GSPAEACDYQ NSGLDSFLNF PLYWPITWAF NNTGLQCEAL
310 320 330 340 350
AIAINQINEE CNDINVLGTF IGNHDLPRIS HNNTDQARIM NAITFVMMWD
360 370 380 390 400
GIPIIYYGTE QNFNSYHDPF NREALWLSNF DMENVYYKLI GILNRFRKSV
410 420 430 440 450
QRQEENYVNT RSTILSVKIH HIVVQKLNVI TVLNNYGIHN EERLSIVFKP
460 470 480 490 500
LGASPKDTFF DIINNQKYVV NTDGTLKVVI TNGFPIVLYP TSKIETSLPQ
510 520 530 540 550
FTATLLPEIT FVPSITVTTH YVLPTLLAPL GYDIREHPGG QQFWNTLTAK
560 570 580
SEAKTIRSFT KLKLFILLIA VPFALPMIIL I
Length:581
Mass (Da):67,005
Last modified:February 1, 1996 - v1
Checksum:iFE9DE99D323E1890
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA91249.1.
PIRiT38289. S62505.
RefSeqiNP_594551.1. NM_001019980.1.

Genome annotation databases

EnsemblFungiiSPAC23D3.14c.1; SPAC23D3.14c.1:pep; SPAC23D3.14c.
GeneIDi2541501.
KEGGispo:SPAC23D3.14c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA91249.1.
PIRiT38289. S62505.
RefSeqiNP_594551.1. NM_001019980.1.

3D structure databases

ProteinModelPortaliQ09840.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4695620.
STRINGi4896.SPAC23D3.14c-1.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC23D3.14c.1; SPAC23D3.14c.1:pep; SPAC23D3.14c.
GeneIDi2541501.
KEGGispo:SPAC23D3.14c.

Organism-specific databases

PomBaseiSPAC23D3.14c.

Phylogenomic databases

eggNOGiCOG0366.
HOGENOMiHOG000165530.
InParanoidiQ09840.
KOiK01176.
OMAiCWIDYSN.
OrthoDBiEOG7RBZJ4.
PhylomeDBiQ09840.

Miscellaneous databases

NextBioi20802600.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR013777. A-amylase_fun.
IPR015340. A_amylase_DUF1966_C.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF09260. DUF1966. 1 hit.
[Graphical view]
PIRSFiPIRSF001024. Alph-amyl_fung. 1 hit.
SMARTiSM00642. Aamy. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PREDICTION OF 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAMY2_SCHPO
AccessioniPrimary (citable) accession number: Q09840
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: January 7, 2015
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.