ID   D8Q7N0_SCHCM            Unreviewed;       490 AA.
AC   D8Q7N0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE            EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN   ORFNames=SCHCODRAFT_235431 {ECO:0000313|EMBL:EFI96050.1};
OS   Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX   NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN   [1] {ECO:0000313|EMBL:EFI96050.1, ECO:0000313|Proteomes:UP000007431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX   PubMed=20622885; DOI=10.1038/nbt.1643;
RA   Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA   de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA   Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA   Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA   Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA   Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA   Woesten H.A.B.;
RT   "Genome sequence of the model mushroom Schizophyllum commune.";
RL   Nat. Biotechnol. 28:957-963(2010).
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; GL377307; EFI96050.1; -; Genomic_DNA.
DR   RefSeq; XP_003030953.1; XM_003030907.1.
DR   AlphaFoldDB; D8Q7N0; -.
DR   STRING; 578458.D8Q7N0; -.
DR   GeneID; 9586700; -.
DR   KEGG; scm:SCHCO_02749442; -.
DR   VEuPathDB; FungiDB:SCHCODRAFT_02749442; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   HOGENOM; CLU_006462_7_2_1; -.
DR   InParanoid; D8Q7N0; -.
DR   OMA; AHNWLFT; -.
DR   OrthoDB; 3249969at2759; -.
DR   Proteomes; UP000007431; 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; 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; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF223; ALPHA-AMYLASE MDE5; 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, ECO:0000313|EMBL:EFI96050.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007431};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..490
FT                   /note="alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003120696"
FT   DOMAIN          31..387
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        222
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT   ACT_SITE        246
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         313
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   BINDING         361
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT   SITE            313
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-2"
FT   DISULFID        48..56
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT   DISULFID        167..180
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT   DISULFID        256..299
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT   DISULFID        453..488
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
SQ   SEQUENCE   490 AA;  54358 MW;  BA75C63A39F47A8F CRC64;
     MFSKSLLLSL PLISGAFAAT AEDWRKRSIY ELVTDRFART DGSTTAPCNT GDRVFCGGTW
     QGLTNHLDYI KNMGFTAVWI SPITMQIYGN THSGEAYHGY WPKDYYQLNP NFGTADDLRN
     LAKALHDRGM YLMVDLVVNH YASWGDEDIQ WSQYVPFNDQ KYFHDKCWIN WNNQQSIEDC
     WMGDGYVPLP DLDTENDYVV STLEKYVGEL VSNYSIDGLR LDATKNIRKD FWPGFCSAAG
     VYCQGEVWTA DVNQFCPWQD YMAGLHNYPM HDYTVSAFSW HKGDVNALAN TLNALTNQCA
     DVGLLGSFTE NHDNPRMGSV TNDLSQRKSL AAMTILSGNG IPIVYYGQEQ IFDAKKDPDN
     REALWLSGYA TGGDKLYDYF AQLNGLRNWL VWNIPEGDYL TAKPSYSVYD THTLVASKGV
     TKVLVSNMGA SVDGSVATSG WSAGEDVVDA LSCNTYTADS QGKATISMKL SLPAAVLPKS
     SLGGSGICGL
//