ID S4SKD6_ACTCH Unreviewed; 413 AA.
AC S4SKD6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
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 Name=AMY2 {ECO:0000313|EMBL:AFO84071.1};
OS Actinidia chinensis (Kiwi) (Yangtao).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Actinidiaceae; Actinidia.
OX NCBI_TaxID=3625 {ECO:0000313|EMBL:AFO84071.1};
RN [1] {ECO:0000313|EMBL:AFO84071.1}
RP NUCLEOTIDE SEQUENCE.
RA Nardozza S., Boldingh H.L., Osorio S., Hohne M., Gleave A.P., MacRae E.A.,
RA Richardson A.C., Atkinson R.G., Sulpice R., Fernie A.R., Clearwater M.J.;
RT "Metabolic Analysis of Kiwifruit (Actinidia deliciosa) Berries from Extreme
RT Genotypes Reveals Drivers for Fruit Starch Metabolism.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; JX067526; AFO84071.1; -; mRNA.
DR AlphaFoldDB; S4SKD6; -.
DR OMA; GWAVWEN; -.
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:UniProtKB-KW.
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: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 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 2: Evidence at transcript level;
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}.
FT DOMAIN 26..366
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; 46950 MW; 75275525F20F7608 CRC64;
MGYLNNGTGE SNQETDVGAV ICNGREILLQ AFNWESHKHD WWRNLENKVP DIAKSGFTSA
WLPPATHSFS PEGYLPQNLY SLNSSYGSEQ QLKALLQKMK LYNVRAMADI VINHRIGTTT
GHGGMYNRYD GIPLSWDERA VTCCTGGLGS RSTGDNFNGV PNIDHSQNFV RKDIIGWLKW
LRNTVGFQDF RFDFARGYSA QYVKEYNEGA KPVFSVGEYW DSCSYNGQHL DYNQDGHRQR
IISWIDGTGG LSTAFDFTTK GILQEAVKGE FWRLRDPQGK PPGVMGWWPS RAVTFLDNHD
TGSTQAHWPF PSHHIMEGYA YILTHPGNPT VFYDHFYDWG NSIHDEIVKL IDVRKRQDLN
SRSSIRILEA QANLYAAMIG EKVCMKIGDG SWCPTGREWT LATCGHRYAV WHK
//
