ID K3ZM17_SETIT Unreviewed; 426 AA.
AC K3ZM17;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 62.
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|PIRNR:PIRNR001028};
GN ORFNames=SETIT_8G179800v2 {ECO:0000313|EMBL:RCV38905.1};
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:KQK95237, ECO:0000313|Proteomes:UP000004995};
RN [1] {ECO:0000313|EMBL:RCV38905.1, ECO:0000313|Proteomes:UP000004995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Yugu1 {ECO:0000313|EnsemblPlants:KQK95237,
RC ECO:0000313|Proteomes:UP000004995}, and Yugu1
RC {ECO:0000313|EMBL:RCV38905.1};
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|EMBL:RCV38905.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV38905.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK95237}
RP IDENTIFICATION.
RC STRAIN=Yugu1 {ECO:0000313|EnsemblPlants:KQK95237};
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|ARBA:ARBA00000548,
CC ECO:0000256|PIRNR:PIRNR001028, ECO:0000256|RuleBase:RU361134};
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,
CC ECO:0000256|RuleBase:RU003615}.
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DR EMBL; AGNK02005117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM003535; RCV38905.1; -; Genomic_DNA.
DR AlphaFoldDB; K3ZM17; -.
DR STRING; 4555.K3ZM17; -.
DR EnsemblPlants; KQK95237; KQK95237; SETIT_027629mg.
DR Gramene; KQK95237; KQK95237; SETIT_027629mg.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_030069_1_0_1; -.
DR InParanoid; K3ZM17; -.
DR OMA; LYMANID; -.
DR Proteomes; UP000004995; Chromosome VIII.
DR GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005987; P:sucrose catabolic process; IBA:GO_Central.
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; 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:SF19; ALPHA-AMYLASE; 1.
DR Pfam; PF07821; Alpha-amyl_C2; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF001028; Alph-amls_plant; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000004995};
KW Signal {ECO:0000256|PIRNR:PIRNR001028}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|PIRNR:PIRNR001028"
FT CHAIN 25..426
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|PIRNR:PIRNR001028"
FT /id="PRO_5010604965"
FT DOMAIN 25..365
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 366..426
FT /note="Alpha-amylase C-terminal beta-sheet"
FT /evidence="ECO:0000259|SMART:SM00810"
FT ACT_SITE 203
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
FT ACT_SITE 228
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
SQ SEQUENCE 426 AA; 46813 MW; E5EAA24335211128 CRC64;
MRKSQVCLLL FLVILGSLSQ SALSQILLQA FNWESCSQGG SGWYDLLSSQ VDAIAGAGIT
HVWLPPPSHS VDARGYLPGR LYDLNVSRYG NETQLRALVA AFHRRGIKCV ADVVLNHRTA
ERKDGRGVYC IFEGGTPDGR LDWGPHMLCR NDSYSDGTGN ADTGLDYQPA PDLDHLNARV
RSELADWLNW LKADVGFDGW RLDFANGYSP AVAGMYINAT SPDLAAAEIW TDLAYEADGK
PRANQDAHRQ ILAAWVDAVG GPAAAFDYTT KGVLQAALNF SELWRMQDAQ GRAPGLVGLR
PAQSVTFVDN HDTGSKTQHS WPFPPEKVLQ GYAYILSHPG IPCIFYDHFF DPTMKDEIAT
MIKIRTRDKI GPTSSLRILL AQHDAYVAEI DGKVVAKVGA RYDVSKIVPP EFVVTTSGND
FAIWEN
//
