ID   Q7S4K0_NEUCR            Unreviewed;       533 AA.
AC   Q7S4K0;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE            EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN   Name=gh13-1 {ECO:0000313|EMBL:EAA30438.1};
GN   ORFNames=NCU08131 {ECO:0000313|EMBL:EAA30438.1};
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110 {ECO:0000313|EMBL:EAA30438.1, ECO:0000313|Proteomes:UP000001805};
RN   [1] {ECO:0000313|EMBL:EAA30438.1, ECO:0000313|Proteomes:UP000001805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC   {ECO:0000313|Proteomes:UP000001805};
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA   FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA   Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA   Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA   Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA   Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA   Lander E.S., Nusbaum C., Birren B.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; Evidence={ECO:0000256|ARBA:ARBA00000548};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061}.
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DR   EMBL; CM002242; EAA30438.1; -; Genomic_DNA.
DR   RefSeq; XP_959674.1; XM_954581.3.
DR   AlphaFoldDB; Q7S4K0; -.
DR   SMR; Q7S4K0; -.
DR   STRING; 367110.Q7S4K0; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PaxDb; 5141-EFNCRP00000008311; -.
DR   EnsemblFungi; EAA30438; EAA30438; NCU08131.
DR   GeneID; 3875826; -.
DR   KEGG; ncr:NCU08131; -.
DR   VEuPathDB; FungiDB:NCU08131; -.
DR   HOGENOM; CLU_006462_7_2_1; -.
DR   InParanoid; Q7S4K0; -.
DR   OMA; HGYWIAD; -.
DR   OrthoDB; 3249969at2759; -.
DR   Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR   CDD; cd11319; AmyAc_euk_AmyA; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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   PANTHER; PTHR10357:SF208; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   Pfam; PF09260; A_amylase_dom_C; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   PIRSF; PIRSF001024; Alph-amyl_fung; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR001024-4};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001805};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..533
FT                   /note="alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004291033"
FT   DOMAIN          35..393
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        228
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT   ACT_SITE        252
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         321
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   SITE            321
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-2"
FT   DISULFID        51..57
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT   DISULFID        172..186
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT   DISULFID        262..307
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT   DISULFID        462..497
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
SQ   SEQUENCE   533 AA;  58657 MW;  7390701DA36C4006 CRC64;
     MRSSLLTGAI AAALSFSGYA AAADADAWKS RSIYQVMIDR FARDDGGSVD CKLYEFCGGT
     WKGLTNKLDY IQGMGFDAIQ ISPVIKNEDK NTAVGEPYHG YWSQDLTQVN PKFGTEEDLK
     NLIAEIHKRD MFLMVDVVVN HMAQEFDNVV PPKVDYSVFK PFNDKKYFHP YCNVTEWENA
     TNIQDCWLYP YGIALADLKT ESPDVVSLFT KWIKNLVSTY SIDGLRIDAA KHVNDEFLPQ
     FVQASGVFAL GEVLTGVTED MCRYQNKSKN LLPGMPNYLD YYPLNAAFNG GSFERLGEIR
     AQAQDSCNDT LALGTFIENH DMPRFASQNQ DMALAKNAMT YVIMNDGIPT VYQGQEQHFT
     GGATPENREP LWKSNYNTSA PLYVLAQTLN KVRKNAIKQS PTYVKQTSNV LIADTNHFCQ
     QKGPAENSVV FCVTNKSSKG DSYQMPVGGF RDSDEVVEVL SCATTTADGL GQITAYMGAG
     EPKVWVKKSA LEGTDICTKT TVDGPKEENG AVSKGAATGV LMAAVLGTAS LLL
//