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Database: UniProt
Entry: A0A067NZR1_PLEOS
LinkDB: A0A067NZR1_PLEOS
Original site: A0A067NZR1_PLEOS 
ID   A0A067NZR1_PLEOS        Unreviewed;       458 AA.
AC   A0A067NZR1;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
GN   ORFNames=PLEOSDRAFT_19514 {ECO:0000313|EMBL:KDQ32475.1};
OS   Pleurotus ostreatus PC15.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX   NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ32475.1, ECO:0000313|Proteomes:UP000027073};
RN   [1] {ECO:0000313|Proteomes:UP000027073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA   LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA   Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA   Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT   white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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         ECO:0000256|RuleBase:RU361134};
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, ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; KL198004; KDQ32475.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067NZR1; -.
DR   STRING; 1137138.A0A067NZR1; -.
DR   VEuPathDB; FungiDB:PLEOSDRAFT_19514; -.
DR   HOGENOM; CLU_013336_0_0_1; -.
DR   InParanoid; A0A067NZR1; -.
DR   OrthoDB; 3249969at2759; -.
DR   Proteomes; UP000027073; Unassembled WGS sequence.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027073};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..458
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001642765"
FT   DOMAIN          32..379
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          388..458
FT                   /note="Alpha-amylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00632"
FT   REGION          437..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   458 AA;  50271 MW;  CE9F3C35CF980540 CRC64;
     MNWFLLPSLW AACLALDVAA ASPSINSDVK KEVIIQMFQW DWDSIGEECA EFIGPAGYGF
     VQVNPPSEHV QGSQWWTDYQ PVSYKIALKH GNRDQFKRMV EKCHIAGVKV ITVDTLFNHI
     SAIQGPATGT AGSTFSKYDY PGLYSYKDFH HNCGTPNNDI LNFTNRNQLQ KCELLGLADL
     DTKSDVVRAR LVEYAKDLRS LGVDGFRIDA AKHIPADELE AILSKVPGFR SPSLYITQEV
     FGGTQPGEEV RATEYLGNGD VHVFDYANEI KAAFLSGNIA SLKGLDSRGW IPSASANVFV
     VNHDNERLDE SLNAHSPSNT YTLGHVFSLA YPYGHISVLS SYESGIDNHD PGPPNGGEWP
     NRWLCQHRWT AIAGMTRFRN AVRNTKLENW QSPQGDRIAF SRGNAGFVAI NNSDSPWIST
     LLTGLPKGWY CDVVSGGSSG RSNGRSEGGK GGGCTGRT
//
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