ID Q41770_MAIZE Unreviewed; 439 AA.
AC Q41770;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 24-JAN-2024, entry version 127.
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};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AAA50161.1};
RN [1] {ECO:0000313|EMBL:AAA50161.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Aleurone {ECO:0000313|EMBL:AAA50161.1};
RX PubMed=8066139; DOI=10.1104/pp.105.2.759;
RA Young T.E., DeMason D.A., Close T.J.;
RT "Cloning of an alpha-amylase cDNA from aleurone tissue of germinating maize
RT seed.";
RL Plant Physiol. 105:759-760(1994).
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; L25805; AAA50161.1; -; mRNA.
DR PIR; T02956; T02956.
DR RefSeq; NP_001105539.1; NM_001112069.1.
DR AlphaFoldDB; Q41770; -.
DR SMR; Q41770; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GeneID; 542522; -.
DR KEGG; zma:542522; -.
DR OrthoDB; 201664at2759; -.
DR ExpressionAtlas; Q41770; baseline and differential.
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:SF48; ALPHA-AMYLASE ISOZYME 3C; 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};
KW Signal {ECO:0000256|PIRNR:PIRNR001028}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|PIRNR:PIRNR001028"
FT CHAIN 29..439
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|PIRNR:PIRNR001028"
FT /id="PRO_5010605125"
FT DOMAIN 29..373
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 368..428
FT /note="Alpha-amylase C-terminal beta-sheet"
FT /evidence="ECO:0000259|SMART:SM00810"
FT ACT_SITE 207
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
FT ACT_SITE 232
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
SQ SEQUENCE 439 AA; 48269 MW; 61A2E362B1F3D8D5 CRC64;
MAKHLAAMCR CSLLVLVLLC LGSQLAQSQV LFQGFNWESW KKQGGWYNYL LGRVDDIAAT
GATHVWLPPP SHSVAPQGYM PGRLYDLDAS KYGTHAELKS LTAAFHAKGV KCVADVVINH
RCADYKDGRG IYCVFEGGTP DSRLDWGPDM ICSDDTQYSN GRGHRDTGAD FAAAPDIDHL
NPRVQQELSD WLNWLKSDLG FDGWRLDFAK GYSAAVAKVY VDSTAPTFVV AEIWSSLHYD
GNGEPSSNQD ADRQELVNWA QAVGGPAAAF DFTTKGVLQA AVQGELWRMK DGNGKAPGMI
GWLPEKAVTF VDNHDTGSTQ NSWPFPSDKV MQGYAYILTH PGTPCIFYDH VFDWNLKQEI
SALSAVRSRN GIHPGSELNI LAADGDLYVA KIDDKVIVKI GSRYDVGNLI PSDFHAVAHG
NNYCVWEKHG LRVPAGRHH
//
