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Database: UniProt/SWISS-PROT
Entry: AMY1_SCHPO
LinkDB: AMY1_SCHPO
Original site: AMY1_SCHPO 
ID   AMY1_SCHPO              Reviewed;         625 AA.
AC   O74922;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   20-JUN-2018, entry version 110.
DE   RecName: Full=Alpha-amylase 1;
DE            EC=3.2.1.1;
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE   Flags: Precursor;
GN   Name=aah1; ORFNames=SPCC757.12;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
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
RT   protein required for cell wall integrity and morphogenesis in
RT   Schizosaccharomyces pombe.";
RL   Biosci. Biotechnol. Biochem. 70:1454-1463(2006).
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-alpha-D-glucosidic
CC       linkages in polysaccharides containing three or more (1->4)-alpha-
CC       linked D-glucose units.
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
CC       high concentrations. {ECO:0000250|UniProtKB:P0C1B3};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor,
CC       GPI-anchor {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000305}.
DR   EMBL; CU329672; CAA21237.1; -; Genomic_DNA.
DR   PIR; T41603; T41603.
DR   RefSeq; NP_587687.1; NM_001022682.2.
DR   ProteinModelPortal; O74922; -.
DR   BioGrid; 275406; 9.
DR   STRING; 4896.SPCC757.12.1; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   MaxQB; O74922; -.
DR   PaxDb; O74922; -.
DR   PRIDE; O74922; -.
DR   EnsemblFungi; SPCC757.12.1; SPCC757.12.1:pep; SPCC757.12.
DR   GeneID; 2538825; -.
DR   KEGG; spo:SPCC757.12; -.
DR   EuPathDB; FungiDB:SPCC757.12; -.
DR   PomBase; SPCC757.12; -.
DR   HOGENOM; HOG000165530; -.
DR   InParanoid; O74922; -.
DR   KO; K01176; -.
DR   OMA; HTTWIKS; -.
DR   OrthoDB; EOG092C1HLH; -.
DR   PhylomeDB; O74922; -.
DR   PRO; PR:O74922; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0031362; C:anchored component of external side of plasma membrane; TAS:PomBase.
DR   GO; GO:0005618; C:cell wall; ISS:PomBase.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0004556; F:alpha-amylase activity; ISM:PomBase.
DR   GO; GO:0103025; F:alpha-amylase activity (releasing maltohexaose); IEA:UniProtKB-EC.
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_DUF1966_C.
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   3: Inferred from homology;
KW   Calcium; Carbohydrate metabolism; Cell membrane; Complete proteome;
KW   Disulfide bond; Glycoprotein; Glycosidase; GPI-anchor; Hydrolase;
KW   Lipoprotein; Membrane; Metal-binding; Reference proteome; Signal.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   CHAIN        23    603       Alpha-amylase 1.
FT                                /FTId=PRO_0000374015.
FT   PROPEP      604    625       Removed in mature form. {ECO:0000255}.
FT                                /FTId=PRO_0000374016.
FT   REGION      232    233       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   COMPBIAS    502    604       Ser-rich.
FT   ACT_SITE    229    229       Nucleophile.
FT                                {ECO:0000250|UniProtKB:P56271}.
FT   ACT_SITE    253    253       Proton donor.
FT                                {ECO:0000250|UniProtKB:P56271}.
FT   METAL       143    143       Calcium 1.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   METAL       185    185       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P56271}.
FT   METAL       198    198       Calcium 1.
FT                                {ECO:0000250|UniProtKB:P56271}.
FT   METAL       229    229       Calcium 2.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   METAL       253    253       Calcium 2.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   BINDING     105    105       Substrate.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   BINDING     227    227       Substrate.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   BINDING     322    322       Substrate.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   BINDING     370    370       Substrate.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   SITE        322    322       Transition state stabilizer.
FT                                {ECO:0000250|UniProtKB:P0C1B3}.
FT   LIPID       603    603       GPI-anchor amidated serine.
FT                                {ECO:0000255}.
FT   CARBOHYD    153    153       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    163    163       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    180    180       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    241    241       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    260    260       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    286    286       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    331    331       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    440    440       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    461    461       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     51     59       {ECO:0000250|UniProtKB:P56271}.
FT   DISULFID    172    187       {ECO:0000250|UniProtKB:P56271}.
FT   DISULFID    263    306       {ECO:0000250|UniProtKB:P56271}.
SQ   SEQUENCE   625 AA;  68087 MW;  30A58CE6D6BC07B3 CRC64;
     MGFSKIALFS LFALFGLPTS LAKSSEEWRD RIIYQVITDR FAVDSDNTPD CSFDDSSYCG
     GTWSGIRSKL DYIQGMGFNA IWISPVEKNL EGSYGSDGEA YHGYWNTDFT QLNEHFGSED
     DLIDLITDMH NRDMWIMFDA LANSMAIPGP TDNISYSNLV PFNDSSYFHP YCWIDYGSNN
     NTDIEDCWTG DDNVILADLD IESTNVADYL HEHIHDMVER YQIDGIRIDA VKQMNPEFFP
     NYTSAAGVFA IGEMFSYDPN VSCSVRNYLD SITSYPIRQG IEFAFNYTGA AFEYLQEIDT
     QFQQACEGQD MSVIGNFLEN HDLPRYTSIT NDTSQDIGAI VFLLLHTGIP IIYYGEEQRL
     PGGSDTPENR AALWNYGYDT DANYYQTIRT AIALRKQAIS DSDSWTTDSH SYLDYDLRHA
     VVRKGDVLGV YTNYESSSDN VTYDVSSNFD DGTVLREVLS NTTTTVGSSG ALHVTVVSGL
     PQVYYPEASL TSFGNFLGTA TSYSSASASY PSTSMSASLS SVHTSSATSS SKSSSSSSSR
     SGSSSSSSSR SGSTSSSGSS HTITSTSQSV HTSGSSTSTS SVAVTSTAYS SSSSSSSSSS
     IESSANAVRV SILGVAAFIA IVLFI
//
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