AMY2_SCHPO
ID AMY2_SCHPO Reviewed; 581 AA.
AC Q09840;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Alpha-amylase 2;
DE EC=3.2.1.1;
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE Flags: Precursor;
GN Name=aah2; ORFNames=SPAC23D3.14c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PREDICTION OF GPI-ANCHOR.
RX PubMed=12845604; DOI=10.1002/yea.1007;
RA De Groot P.W., Hellingwerf K.J., Klis F.M.;
RT "Genome-wide identification of fungal GPI proteins.";
RL Yeast 20:781-796(2003).
RN [3]
RP GENE NAME.
RX PubMed=16751704; DOI=10.1271/bbb.50693;
RA Morita T., Tanaka N., Hosomi A., Giga-Hama Y., Takegawa K.;
RT "An alpha-amylase homologue, aah3, encodes a GPI-anchored membrane protein
RT required for cell wall integrity and morphogenesis in Schizosaccharomyces
RT pombe.";
RL Biosci. Biotechnol. Biochem. 70:1454-1463(2006).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P0C1B3};
CC Note=Binds 2 calcium ions per subunit. Calcium is inhibitory at high
CC concentrations. {ECO:0000250|UniProtKB:P0C1B3};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; CU329670; CAA91249.1; -; Genomic_DNA.
DR PIR; T38289; S62505.
DR RefSeq; NP_594551.1; NM_001019980.1.
DR AlphaFoldDB; Q09840; -.
DR SMR; Q09840; -.
DR STRING; 4896.SPAC23D3.14c.1; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; Q09840; -.
DR EnsemblFungi; SPAC23D3.14c.1; SPAC23D3.14c.1:pep; SPAC23D3.14c.
DR GeneID; 2541501; -.
DR KEGG; spo:SPAC23D3.14c; -.
DR PomBase; SPAC23D3.14c; aah2.
DR VEuPathDB; FungiDB:SPAC23D3.14c; -.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_006462_7_2_1; -.
DR InParanoid; Q09840; -.
DR OMA; IGEYFTG; -.
DR PhylomeDB; Q09840; -.
DR PRO; PR:Q09840; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; TAS:PomBase.
DR GO; GO:0004556; F:alpha-amylase activity; ISM:PomBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; ISS:PomBase.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR013777; A-amylase-like.
DR InterPro; IPR015340; A_amylase_C_dom.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF09260; DUF1966; 1.
DR PIRSF; PIRSF001024; Alph-amyl_fung; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Calcium; Carbohydrate metabolism; Cell membrane; Disulfide bond;
KW Glycoprotein; Glycosidase; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..551
FT /note="Alpha-amylase 2"
FT /id="PRO_0000001355"
FT PROPEP 552..581
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000255452"
FT ACT_SITE 233
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT ACT_SITE 257
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT BINDING 109
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 236..237
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 372
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT SITE 325
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT LIPID 551
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..64
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 176..191
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 267..311
FT /evidence="ECO:0000250|UniProtKB:P56271"
SQ SEQUENCE 581 AA; 67005 MW; FE9DE99D323E1890 CRC64;
MNYRRNICLR IGWMLLFAFI PAYAGHSAEE WKRRSIYQII TDRFSLEEGA TERIPCDPVR
FMYCGGTWNG IRNHLDYIQG MGFDAIWISP IFENVEGNDI DGSSYHGYWT TNLYELNHHF
GTKEEFMELI QELHKRDIWI LLDVAINSMA INGPLEQMSF EKVIPFNDAS FFHPHCWVDY
ESNDIESVQN CWLGDENLLL ADVDTENEVV LSVLEKWIKN VVQEYDIDGI RFDAIKHAPI
EFWLRMSKAA DIFTIGEYFT GSPAEACDYQ NSGLDSFLNF PLYWPITWAF NNTGLQCEAL
AIAINQINEE CNDINVLGTF IGNHDLPRIS HNNTDQARIM NAITFVMMWD GIPIIYYGTE
QNFNSYHDPF NREALWLSNF DMENVYYKLI GILNRFRKSV QRQEENYVNT RSTILSVKIH
HIVVQKLNVI TVLNNYGIHN EERLSIVFKP LGASPKDTFF DIINNQKYVV NTDGTLKVVI
TNGFPIVLYP TSKIETSLPQ FTATLLPEIT FVPSITVTTH YVLPTLLAPL GYDIREHPGG
QQFWNTLTAK SEAKTIRSFT KLKLFILLIA VPFALPMIIL I
