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Database: UniProt
Entry: D3XAS6_HORVS
LinkDB: D3XAS6_HORVS
Original site: D3XAS6_HORVS 
ID   D3XAS6_HORVS            Unreviewed;       414 AA.
AC   D3XAS6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 57.
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};
DE   Flags: Fragment;
GN   Name=amy2 {ECO:0000313|EMBL:ADC54281.1};
OS   Hordeum vulgare subsp. spontaneum (Wild barley) (Hordeum spontaneum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=77009 {ECO:0000313|EMBL:ADC54281.1};
RN   [1] {ECO:0000313|EMBL:ADC54281.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mt.Meron-4 {ECO:0000313|EMBL:ADC54281.1};
RA   Wang J.R., Wang Y., Chen X., Wei Y.M., Zheng Y.L.;
RT   "Diversity of amy2 genes in wild barley populations from Israel.";
RL   Submitted (DEC-2009) 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   -!- 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; GU269286; ADC54281.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3XAS6; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
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:0005983; P:starch catabolic process; IEA:UniProt.
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:SF38; ALPHA-AMYLASE ISOZYME 2A; 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   Germination {ECO:0000256|ARBA:ARBA00022544};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134}.
FT   DOMAIN          2..343
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          344..404
FT                   /note="Alpha-amylase C-terminal beta-sheet"
FT                   /evidence="ECO:0000259|SMART:SM00810"
FT   ACT_SITE        180
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
FT   ACT_SITE        205
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
FT   BINDING         45..47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-2"
FT   BINDING         52..53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-2"
FT   BINDING         178..183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-2"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-2"
FT   BINDING         209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-2"
FT   BINDING         227
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-2"
FT   BINDING         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-2"
FT   BINDING         271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-2"
FT   BINDING         277..279
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-2"
FT   BINDING         290
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-2"
FT   BINDING         296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-2"
FT   BINDING         375
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-2"
FT   BINDING         380..382
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-2"
FT   BINDING         392..398
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-2"
FT   BINDING         402
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADC54281.1"
SQ   SEQUENCE   414 AA;  45446 MW;  F0DDC02ABCF39B44 CRC64;
     HQVLFQGFNW ESWKQSGGWY NMMMGKVDDI AAAGVTHVWL PPPSHSVSNE GYMPGRLYDI
     DASKYGNAAE LKSLIGALHG KGVQAIADIV INHRCADYKD NRGIYCIFEG GTSDGRLDWG
     PHMICRDDTK YADGTANLDT GADFAAAPDI DHLNDRVQRE LKEWLLWLKS DLGFDAWRLD
     FARGYSPEMA KVYIDGTSPS LAVAEVWDNM ATGGDGKPNY DQDAHRQNLV NWVDKVGGAA
     SAGMVFDFTT KGILNAAVEG ELWRLIDPQG KAPGVMGWWP AKAVTFVDNH DTGSTQAVWP
     FPSDKVMQGY AYILTHPGTP CIFYDHFFNW GFKDEIAALV AIRKRNGITA TSALKILMHE
     GDAYVAEIDG KVVVKIGTRY DVGAVIPAGF ATSAHGKDYA VWEKTATAAT LQRS
//
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