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Database: UniProt/TrEMBL
Entry: A0A1U7WV26_NICSY
LinkDB: A0A1U7WV26_NICSY
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ID   A0A1U7WV26_NICSY        Unreviewed;       407 AA.
AC   A0A1U7WV26;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=LOC104227526 {ECO:0000313|RefSeq:XP_009778085.1,
GN   ECO:0000313|RefSeq:XP_009778086.1};
OS   Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4096 {ECO:0000313|Proteomes:UP000189701, ECO:0000313|RefSeq:XP_009778085.1};
RN   [1] {ECO:0000313|Proteomes:UP000189701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23773524; DOI=10.1186/gb-2013-14-6-r60;
RA   Sierro N., Battey J.N., Ouadi S., Bovet L., Goepfert S., Bakaher N.,
RA   Peitsch M.C., Ivanov N.V.;
RT   "Reference genomes and transcriptomes of Nicotiana sylvestris and Nicotiana
RT   tomentosiformis.";
RL   Genome Biol. 14:R60.1-R60.17(2013).
RN   [2] {ECO:0000313|RefSeq:XP_009778085.1, ECO:0000313|RefSeq:XP_009778086.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_009778085.1,
RC   ECO:0000313|RefSeq:XP_009778086.1};
RG   RefSeq;
RL   Submitted (NOV-2023) 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   -!- 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   RefSeq; XP_009778085.1; XM_009779783.1.
DR   RefSeq; XP_009778086.1; XM_009779784.1.
DR   STRING; 4096.A0A1U7WV26; -.
DR   GeneID; 104227526; -.
DR   KEGG; nsy:104227526; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   OrthoDB; 201664at2759; -.
DR   Proteomes; UP000189701; Unplaced.
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   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:UP000189701}.
FT   DOMAIN          20..348
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          349..407
FT                   /note="Alpha-amylase C-terminal beta-sheet"
FT                   /evidence="ECO:0000259|SMART:SM00810"
FT   ACT_SITE        187
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
FT   ACT_SITE        212
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
SQ   SEQUENCE   407 AA;  46584 MW;  76C19439E6F48D69 CRC64;
     MGFDESQQTD PLVVIRNGKE IILQAFNWES HKHDWWRNLD RKVPDIAKSG FTTAWLPPAS
     QSLSPEGYLP QNLYSLNSSY GSEHLLKALL NKMKQYKVRA MADIVINHRV GTTQGHGGMY
     NRYDGIPLSW DEHAVTSCTG GRGNKSTGDN FNGVPNIDHT QSFVRRDLTD WMRWLRSSVG
     FQDFRFDFAK GYSPKYVKEY IEGAKPIFSV GEYWDTCNYK GSYLDCNQDS HRQRIINWID
     QTGQLSSAFD FTTKAILQEA VKGELWRLRD SKGKPPGVLG WWPSRAVTFI DNHDTGSTQA
     HWPFPSNHIM EGYTYILTHP GIPSVFYDHF YDWGNSTHDQ IVKLIDIRRH QGIHSRSSVQ
     ILESQPNLYA ATIGEKVSMK IGDGSWCPAG KEWKLATSGY RYAVWQK
//
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