Reviewed, UniProtKB/Swiss-Prot Q9Y7S9 (AMY3_SCHPO)

Names and origin

Protein names

Recommended name:
    Alpha-amylase 3
    EC=3.2.1.1
Alternative name(s):
    1,4-alpha-D-glucan glucanohydrolase

Gene names

Name:	aah3
ORF Names:	SPCC63.02c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	564 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has a role in cell wall biosynthesis where it is involved in maintaining cell wall strength and shape. Ref.3
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.
Post-translational modification	N-glycosylated.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Cell membrane Membrane
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ascospore wall assembly Ref.2 Inferred from mutant phenotype. Source: GeneDB_SPombe cell morphogenesis Ref.2 Inferred from mutant phenotype. Source: GeneDB_SPombe cellular polysaccharide catabolic process Inferred by curator. Source: GeneDB_SPombe vesicle-mediated transport Inferred from mutant phenotype. Source: GeneDB_SPombe
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell wall Ref.2 Inferred from direct assay. Source: GeneDB_SPombe endoplasmic reticulum Ref.4 Inferred from direct assay. Source: GeneDB_SPombe external side of plasma membrane Ref.3 Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	alpha-amylase activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 538	517	Alpha-amylase 3		PRO_0000001358
	Propeptide	539 – 564	26	Removed in mature form Potential		PRO_0000255453
Regions
	Compositional bias	537 – 540	4	Poly-Ser
Sites
	Active site	229	1	Nucleophile By similarity
	Active site	253	1	Proton donor By similarity
	Active site	322	1	By similarity
	Metal binding	143	1	Calcium 1 By similarity
	Metal binding	198	1	Calcium 1 By similarity
	Metal binding	229	1	Calcium 2 By similarity
	Metal binding	253	1	Calcium 2 By similarity
Amino acid modifications
	Lipidation	538	1	GPI-anchor amidated serine Potential
	Glycosylation	181	1	N-linked (GlcNAc...) Potential
	Glycosylation	235	1	N-linked (GlcNAc...) Potential
	Glycosylation	282	1	N-linked (GlcNAc...) Potential
	Glycosylation	305	1	N-linked (GlcNAc...) Potential
	Glycosylation	438	1	N-linked (GlcNAc...) Potential
	Glycosylation	447	1	N-linked (GlcNAc...) Potential
	Glycosylation	498	1	N-linked (GlcNAc...) Potential
	Disulfide bond	51 ↔ 59		By similarity
	Disulfide bond	172 ↔ 188		By similarity
	Disulfide bond	263 ↔ 306		By similarity
Experimental info
	Mutagenesis	229	1	D → A: No activity. Ref.3
	Mutagenesis	253	1	E → A: No activity. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9Y7S9-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 1229FD4AEC702FD0	FASTA	564	63,206
	10 20 30 40 50 60 MFGVYFVLLF LSSALIHVAN AGSNAEWRKR IIYQILTDRF AVDDGSTDNP CDPDANQYCG 70 80 90 100 110 120 GTWKGIENKL DYIEDMGFNA IWISPIDKNI EGDIDGAGYA YHGYWNTDYE SLNEHFGTED 130 140 150 160 170 180 DLVSLITAAH KAGIWVMLDS IVNSMALAPP LADADYSSLN PFNKESYFHP YCLIDWDITD 190 200 210 220 230 240 NETNVMDCWQ DSGVLLADLD VESSDVSSYL SDHFKSLISK YDFDGLRIDA VKMMNYTFFP 250 260 270 280 290 300 DFVDATGVYS VGEVFSYDPD TMCSYMSVLP GVTNYFLQLY INFSFTATGA GFTLIPTYQE 310 320 330 340 350 360 VMASNCSKYD STLMLTFIEN HDLYRFPYYT SDQSQIMGAL SFVLIWDGIP SIFYGQEQGF 370 380 390 400 410 420 NGGEDPANRP ALWLTDYDQS NPYYTVIKTM VAFRKFVITQ DPDWVTSTYQ SIESAVDHYV 430 440 450 460 470 480 GQKNDVLVMF NNMGVTNNLT IYEVETNYTA NEVVSDVFGH RTLTVGADKT LTASMTNGYP 490 500 510 520 530 540 LIMYPHSKMS GFTLPTVNRT VMPSTSATAT TTVYTSYYSP SYSARSFTGT GSIFTISSSS 550 560 RLILSFKTLV FGLGVTAMLF VLFF

References

	« Hide 'large scale' referencesShow '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. , 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]	"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: FUNCTION, GPI-ANCHOR, N-GLCOSYLATION, 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: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329672 Genomic DNA. Translation: CAB40006.1.
PIR	T41503.
RefSeq	NP_587976.1.
3D structure databases
HSSP	HSSP built from PDB template 2AAA based on UniProtKB P56271.
ModBase	Search...
Protein family/group databases
CAZy	GH13. Glycoside Hydrolase Family 13.
Genome annotation databases
GeneID	2539415.
GenomeReviews	Gene locus aah3 in contig CU329672_GR.
KEGG	spo:SPCC63.02c.
NMPDR	fig|4896.1.peg.314.
Organism-specific databases
GeneDB_Spombe	SPCC63.02c.
Phylogenomic databases
OMA	CGGTWKG.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002307-MON.
BRENDA	3.2.1.1. 653.
Gene expression databases
ArrayExpress	Q9Y7S9.
Family and domain databases
InterPro	IPR013777. A-amylase_fun. IPR015340. Alpha_amylase_DUF1966_C. IPR013780. Glyco_hydro_13_b. IPR006047. Glyco_hydro_13_cat. IPR006589. Glyco_hydro_13_sub_cat. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. PF09260. DUF1966. 1 hit. [Graphical view]
PIRSF	PIRSF001024. Alph-amyl_fung. 1 hit.
SMART	SM00642. Aamy. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMY3_SCHPO

Accession

Primary (citable) accession number: Q9Y7S9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 2002
Last sequence update:	November 1, 1999
Last modified:	November 3, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)