ID   D7TPJ1_VITVI            Unreviewed;       425 AA.
AC   D7TPJ1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 84.
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   OrderedLocusNames=VIT_03s0063g00450 {ECO:0000313|EMBL:CBI32414.3};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI32414.3, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
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; FN596006; CBI32414.3; -; Genomic_DNA.
DR   RefSeq; XP_002282184.1; XM_002282148.3.
DR   AlphaFoldDB; D7TPJ1; -.
DR   SMR; D7TPJ1; -.
DR   STRING; 29760.D7TPJ1; -.
DR   PaxDb; 29760-VIT_03s0063g00450-t01; -.
DR   EnsemblPlants; Vitvi03g01571_t001; Vitvi03g01571_P001; Vitvi03g01571.
DR   GeneID; 100250317; -.
DR   Gramene; Vitvi03g01571_t001; Vitvi03g01571_P001; Vitvi03g01571.
DR   KEGG; vvi:100250317; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   HOGENOM; CLU_030069_1_0_1; -.
DR   InParanoid; D7TPJ1; -.
DR   OMA; WRMRDEN; -.
DR   OrthoDB; 201664at2759; -.
DR   Proteomes; UP000009183; Chromosome 3.
DR   ExpressionAtlas; D7TPJ1; baseline and differential.
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: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   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:UP000009183};
KW   Signal {ECO:0000256|PIRNR:PIRNR001028}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|PIRNR:PIRNR001028"
FT   CHAIN           23..425
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR001028"
FT                   /id="PRO_5010605339"
FT   DOMAIN          24..368
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          363..424
FT                   /note="Alpha-amylase C-terminal beta-sheet"
FT                   /evidence="ECO:0000259|SMART:SM00810"
FT   REGION          150..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        202
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
FT   ACT_SITE        227
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
SQ   SEQUENCE   425 AA;  47779 MW;  F9156B3487F485A4 CRC64;
     MDIATSLSCL LFFITILPAL TASPILFQGF NWESSKKEGG WYNFLINSIP ELAASGITHV
     WLPPPSQSVS PEGYMPGRLY DLNASKYGTQ DELKTLIKVF HSKGVQCIAD IVINHRTAEK
     QDARGIWAIF EGGTPDDRLD WTPSFICKDD TPYSDGTGNP DSGDDYSAAP DIDHINPRVQ
     QELIDWMNWL KIEIGFDGWR FDFARGFSPA FTKFYMAKTR PKFAVGEIWK SLSYRSDGKP
     SYNQDSHRRE LVEWVRGAGG AVNAFDFTTK GILQAAVEGE LWRMKDLNGK PPGMIGLMPG
     NAVTFIDNHD TGSTLQHWPF PSDKVMQGYA YILTHPGIPS IFYDHFFEWG LKEEIMKLII
     IRSRNRIKPN SAVRILASDS DLYVAAIDGK IIVKIGPRFD VGNLVPKSFK KIATSGKDYC
     VWEKK
//