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Database: UniProt
Entry: K3Y7N6_SETIT
LinkDB: K3Y7N6_SETIT
Original site: K3Y7N6_SETIT 
ID   K3Y7N6_SETIT            Unreviewed;       413 AA.
AC   K3Y7N6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|PIRNR:PIRNR001028};
DE            EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|PIRNR:PIRNR001028};
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase {ECO:0000256|ARBA:ARBA00030238, ECO:0000256|PIRNR:PIRNR001028};
OS   Setaria italica (Foxtail millet) (Panicum italicum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX   NCBI_TaxID=4555 {ECO:0000313|EnsemblPlants:KQK97087, ECO:0000313|Proteomes:UP000004995};
RN   [1] {ECO:0000313|EnsemblPlants:KQK97087, ECO:0000313|Proteomes:UP000004995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQK97087,
RC   ECO:0000313|Proteomes:UP000004995};
RX   PubMed=22580951; DOI=10.1038/nbt.2196;
RA   Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA   Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA   Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA   Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA   Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA   Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT   "Reference genome sequence of the model plant Setaria.";
RL   Nat. Biotechnol. 30:555-561(2012).
RN   [2] {ECO:0000313|EnsemblPlants:KQK97087}
RP   IDENTIFICATION.
RC   STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQK97087};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
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|PIRNR:PIRNR001028};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913,
CC         ECO:0000256|PIRNR:PIRNR001028};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|PIRNR:PIRNR001028}.
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DR   EMBL; AGNK02004326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; K3Y7N6; -.
DR   EnsemblPlants; KQK97087; KQK97087; SETIT_010224mg.
DR   Gramene; KQK97087; KQK97087; SETIT_010224mg.
DR   HOGENOM; CLU_030069_1_0_1; -.
DR   Proteomes; UP000004995; Chromosome VII.
DR   ExpressionAtlas; K3Y7N6; baseline.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11314; AmyAc_arch_bac_plant_AmyA; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR012850; A-amylase_bs_C.
DR   InterPro; IPR013775; A-amylase_pln.
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; PF07821; Alpha-amyl_C2; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   PIRSF; PIRSF001028; Alph-amls_plant; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00810; Alpha-amyl_C2; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000004995}.
FT   DOMAIN          26..360
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          355..413
FT                   /note="Alpha-amylase C-terminal beta-sheet"
FT                   /evidence="ECO:0000259|SMART:SM00810"
FT   ACT_SITE        193
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
FT   ACT_SITE        218
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
SQ   SEQUENCE   413 AA;  47334 MW;  9920B83C3508F3DA CRC64;
     MGQMVSDDKF EEQAARHGGI IKNGREILFQ AFNWESNKHN WWSKLEDKVT DMAESGFTSA
     WLPPPTQSLS QEGYLPQNLY CLDSSYGSLP ELKSLLHKMN EHHIRAMADV VINHRIGTTQ
     GSNGMYNRYD GIPISWDEHA VTSCSGGKGN KSTGDNFNGV PNIDHTQTFV RKDIIEWLIW
     LRKSVGFQDF RFDFTKGYAA KFVKEYIEES KPLFAVGEYW DSCEYSPPDY RLNYNQDNHR
     QRIINWIDST GGLCAAFDFT TKGILQEAVK GELWRLRDPE GKPPGVMGWW PSRSVTFIEN
     HDTGSTQGHW PFPSDHIMEG YAYILTHPGI PTVFYDHFYD QGQSLHDEIA KLIRKCQDIH
     SRSSVKILEA RSDLYSAIIN EKLCMKIGDG SWCPSDPEWR LAASGDRYAV WHK
//
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