ID   A7E8Z8_SCLS1            Unreviewed;       448 AA.
AC   A7E8Z8;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE            EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN   ORFNames=SS1G_01776 {ECO:0000313|EMBL:EDN96850.1};
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN96850.1, ECO:0000313|Proteomes:UP000001312};
RN   [1] {ECO:0000313|Proteomes:UP000001312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX   PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476622; EDN96850.1; -; Genomic_DNA.
DR   RefSeq; XP_001597582.1; XM_001597532.1.
DR   AlphaFoldDB; A7E8Z8; -.
DR   STRING; 665079.A7E8Z8; -.
DR   EnsemblFungi; EDN96850; EDN96850; SS1G_01776.
DR   GeneID; 5493902; -.
DR   KEGG; ssl:SS1G_01776; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   HOGENOM; CLU_006462_7_2_1; -.
DR   InParanoid; A7E8Z8; -.
DR   OMA; VTNHMAW; -.
DR   OrthoDB; 3249969at2759; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
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; 2.
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:SF215; ALPHA-AMYLASE 1; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   Pfam; PF09260; A_amylase_dom_C; 1.
DR   Pfam; PF00128; Alpha-amylase; 2.
DR   PIRSF; PIRSF001024; Alph-amyl_fung; 2.
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:UP000001312};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..448
FT                   /note="alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002705928"
FT   DOMAIN          34..338
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        173
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT   ACT_SITE        197
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   SITE            264
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        118..131
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT   DISULFID        207..250
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT   DISULFID        411..446
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
SQ   SEQUENCE   448 AA;  48885 MW;  C0CCEE450368E769 CRC64;
     MKPSSLLRLI PVTYLATSVA ALSAAGWRSQ SIYQVITDRF ARTDGSTTAS CNVNEYCGGS
     WQGIIKHLDY IQNMGFTADG SSYHGYWAQN IYQVNSNFGT PADLKALSAA KSYYHPFCLI
     DYNNATSVVD CWEGDNIVSL PDLRTEDSDV YTEWNSWISQ LVANYSIDGL RVDSAQQTGK
     AFFPSFQNSA GVYVVGEIFN GDPAYVCPYQ NYMNGVLNYP AYYWITQAFQ STSGSISNLV
     NGINTMKSSC SDTTLLGSFL ENHDVARFPS YTSDASLTKN AIAFTILSDG IPIVYQGQEQ
     HLTGSSVPNN REALWSNSNS YSQSATYYRF IASVNQIRNQ AIYVDPTYLT YKAYPVYSDG
     TTIVMRKGFT GKQIIAVFSN KGASGSSYTL TLTSSQTGFT SNLQVVEVLT CTTSTTNGSG
     NLAVSMAGGV PRIFYPKSYL VGSGVCSL
//