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Protein

Alpha-amylase 3

Gene

aah3

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

Functioni

Has a role in cell wall biosynthesis where it is involved in maintaining cell wall strength and shape.1 Publication

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 sitei56 – 561SubstrateBy similarity
Binding sitei105 – 1051SubstrateBy similarity
Metal bindingi143 – 1431Calcium 1By similarity
Metal bindingi198 – 1981Calcium 1By similarity
Binding sitei227 – 2271SubstrateBy similarity
Active sitei229 – 2291Nucleophile1 Publication
Metal bindingi229 – 2291Calcium 2By similarity
Active sitei253 – 2531Proton donor1 Publication
Metal bindingi253 – 2531Calcium 2By similarity
Binding sitei322 – 3221SubstrateBy similarity
Sitei322 – 3221Transition state stabilizerBy similarity
Binding sitei369 – 3691SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

  • ascospore wall assembly Source: PomBase
  • ascospore wall biogenesis Source: PomBase
  • carbohydrate catabolic process Source: InterPro
  • fungal-type cell wall biogenesis 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 3 (EC:3.2.1.1)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Gene namesi
Name:aah3
ORF Names:SPCC63.02c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC63.02c.
PomBaseiSPCC63.02c. aah3.

Subcellular locationi

GO - Cellular componenti

  • anchored component of external side of plasma membrane Source: PomBase
  • anchored component of plasma membrane Source: PomBase
  • cell wall Source: PomBase
  • endoplasmic reticulum Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi229 – 2291D → A: No activity. 1 Publication
Mutagenesisi253 – 2531E → A: No activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 538517Alpha-amylase 3PRO_0000001358Add
BLAST
Propeptidei539 – 56426Removed in mature formSequence analysisPRO_0000255453Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi51 ↔ 59By similarity
Disulfide bondi172 ↔ 188By similarity
Glycosylationi181 – 1811N-linked (GlcNAc...)Sequence analysis
Glycosylationi235 – 2351N-linked (GlcNAc...)Sequence analysis
Disulfide bondi263 ↔ 306By similarity
Glycosylationi282 – 2821N-linked (GlcNAc...)Sequence analysis
Glycosylationi305 – 3051N-linked (GlcNAc...)Sequence analysis
Glycosylationi438 – 4381N-linked (GlcNAc...)Sequence analysis
Glycosylationi447 – 4471N-linked (GlcNAc...)Sequence analysis
Glycosylationi498 – 4981N-linked (GlcNAc...)Sequence analysis
Lipidationi538 – 5381GPI-anchor amidated serineSequence analysis

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiQ9Y7S9.
PRIDEiQ9Y7S9.

Interactioni

Protein-protein interaction databases

BioGridi275980. 2 interactions.
MINTiMINT-4718683.

Structurei

3D structure databases

ProteinModelPortaliQ9Y7S9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni232 – 2332Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi537 – 5404Poly-Ser

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000165530.
InParanoidiQ9Y7S9.
KOiK01176.
OMAiITDYNDY.
OrthoDBiEOG7RBZJ4.
PhylomeDBiQ9Y7S9.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR015340. A_amylase_DUF1966_C.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
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]
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.

Q9Y7S9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFGVYFVLLF LSSALIHVAN AGSNAEWRKR IIYQILTDRF AVDDGSTDNP
60 70 80 90 100
CDPDANQYCG GTWKGIENKL DYIEDMGFNA IWISPIDKNI EGDIDGAGYA
110 120 130 140 150
YHGYWNTDYE SLNEHFGTED DLVSLITAAH KAGIWVMLDS IVNSMALAPP
160 170 180 190 200
LADADYSSLN PFNKESYFHP YCLIDWDITD NETNVMDCWQ DSGVLLADLD
210 220 230 240 250
VESSDVSSYL SDHFKSLISK YDFDGLRIDA VKMMNYTFFP DFVDATGVYS
260 270 280 290 300
VGEVFSYDPD TMCSYMSVLP GVTNYFLQLY INFSFTATGA GFTLIPTYQE
310 320 330 340 350
VMASNCSKYD STLMLTFIEN HDLYRFPYYT SDQSQIMGAL SFVLIWDGIP
360 370 380 390 400
SIFYGQEQGF NGGEDPANRP ALWLTDYDQS NPYYTVIKTM VAFRKFVITQ
410 420 430 440 450
DPDWVTSTYQ SIESAVDHYV GQKNDVLVMF NNMGVTNNLT IYEVETNYTA
460 470 480 490 500
NEVVSDVFGH RTLTVGADKT LTASMTNGYP LIMYPHSKMS GFTLPTVNRT
510 520 530 540 550
VMPSTSATAT TTVYTSYYSP SYSARSFTGT GSIFTISSSS RLILSFKTLV
560
FGLGVTAMLF VLFF
Length:564
Mass (Da):63,206
Last modified:November 1, 1999 - v1
Checksum:i1229FD4AEC702FD0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAB40006.1.
PIRiT41503.
RefSeqiNP_587976.1. NM_001022967.2.

Genome annotation databases

EnsemblFungiiSPCC63.02c.1; SPCC63.02c.1:pep; SPCC63.02c.
GeneIDi2539415.
KEGGispo:SPCC63.02c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAB40006.1.
PIRiT41503.
RefSeqiNP_587976.1. NM_001022967.2.

3D structure databases

ProteinModelPortaliQ9Y7S9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275980. 2 interactions.
MINTiMINT-4718683.

Protein family/group databases

CAZyiGH13. Glycoside Hydrolase Family 13.

Proteomic databases

MaxQBiQ9Y7S9.
PRIDEiQ9Y7S9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC63.02c.1; SPCC63.02c.1:pep; SPCC63.02c.
GeneIDi2539415.
KEGGispo:SPCC63.02c.

Organism-specific databases

EuPathDBiFungiDB:SPCC63.02c.
PomBaseiSPCC63.02c. aah3.

Phylogenomic databases

HOGENOMiHOG000165530.
InParanoidiQ9Y7S9.
KOiK01176.
OMAiITDYNDY.
OrthoDBiEOG7RBZJ4.
PhylomeDBiQ9Y7S9.

Miscellaneous databases

PROiQ9Y7S9.

Family and domain databases

Gene3Di2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR015340. A_amylase_DUF1966_C.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013780. Glyco_hydro_b.
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]
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: FUNCTION, GPI-ANCHOR, GLYCOSYLATION, MUTAGENESIS OF ASP-229 AND GLU-253.
  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 nameiAMY3_SCHPO
AccessioniPrimary (citable) accession number: Q9Y7S9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: November 1, 1999
Last modified: June 8, 2016
This is version 128 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

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 one 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.