AMY3_SCHPO
ID AMY3_SCHPO Reviewed; 564 AA.
AC Q9Y7S9;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Alpha-amylase 3;
DE EC=3.2.1.1;
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE Flags: Precursor;
GN Name=aah3; ORFNames=SPCC63.02c;
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 FUNCTION, GPI-ANCHOR, GLYCOSYLATION, AND MUTAGENESIS OF ASP-229 AND
RP GLU-253.
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 -!- FUNCTION: Has a role in cell wall biosynthesis where it is involved in
CC maintaining cell wall strength and shape.
CC {ECO:0000269|PubMed:16751704}.
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 -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16751704}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; CU329672; CAB40006.1; -; Genomic_DNA.
DR PIR; T41503; T41503.
DR RefSeq; NP_587976.1; NM_001022967.2.
DR AlphaFoldDB; Q9Y7S9; -.
DR SMR; Q9Y7S9; -.
DR BioGRID; 275980; 4.
DR STRING; 4896.SPCC63.02c.1; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR MaxQB; Q9Y7S9; -.
DR PaxDb; Q9Y7S9; -.
DR PRIDE; Q9Y7S9; -.
DR EnsemblFungi; SPCC63.02c.1; SPCC63.02c.1:pep; SPCC63.02c.
DR GeneID; 2539415; -.
DR KEGG; spo:SPCC63.02c; -.
DR PomBase; SPCC63.02c; aah3.
DR VEuPathDB; FungiDB:SPCC63.02c; -.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_006462_7_2_1; -.
DR InParanoid; Q9Y7S9; -.
DR OMA; VFGHRTL; -.
DR PhylomeDB; Q9Y7S9; -.
DR PRO; PR:Q9Y7S9; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; IC:PomBase.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:PomBase.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0004556; F:alpha-amylase activity; ISM:PomBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:PomBase.
DR GO; GO:0070591; P:ascospore wall biogenesis; IMP:PomBase.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IMP: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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..538
FT /note="Alpha-amylase 3"
FT /id="PRO_0000001358"
FT PROPEP 539..564
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000255453"
FT ACT_SITE 229
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:16751704"
FT ACT_SITE 253
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:16751704"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 232..233
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 369
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT SITE 322
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT LIPID 538
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..59
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 172..188
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT DISULFID 263..306
FT /evidence="ECO:0000250|UniProtKB:P56271"
FT MUTAGEN 229
FT /note="D->A: No activity."
FT /evidence="ECO:0000269|PubMed:16751704"
FT MUTAGEN 253
FT /note="E->A: No activity."
FT /evidence="ECO:0000269|PubMed:16751704"
SQ SEQUENCE 564 AA; 63206 MW; 1229FD4AEC702FD0 CRC64;
MFGVYFVLLF LSSALIHVAN AGSNAEWRKR IIYQILTDRF AVDDGSTDNP CDPDANQYCG
GTWKGIENKL DYIEDMGFNA IWISPIDKNI EGDIDGAGYA YHGYWNTDYE SLNEHFGTED
DLVSLITAAH KAGIWVMLDS IVNSMALAPP LADADYSSLN PFNKESYFHP YCLIDWDITD
NETNVMDCWQ DSGVLLADLD VESSDVSSYL SDHFKSLISK YDFDGLRIDA VKMMNYTFFP
DFVDATGVYS VGEVFSYDPD TMCSYMSVLP GVTNYFLQLY INFSFTATGA GFTLIPTYQE
VMASNCSKYD STLMLTFIEN HDLYRFPYYT SDQSQIMGAL SFVLIWDGIP SIFYGQEQGF
NGGEDPANRP ALWLTDYDQS NPYYTVIKTM VAFRKFVITQ DPDWVTSTYQ SIESAVDHYV
GQKNDVLVMF NNMGVTNNLT IYEVETNYTA NEVVSDVFGH RTLTVGADKT LTASMTNGYP
LIMYPHSKMS GFTLPTVNRT VMPSTSATAT TTVYTSYYSP SYSARSFTGT GSIFTISSSS
RLILSFKTLV FGLGVTAMLF VLFF
