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Database: UniProt/TrEMBL
Entry: A0A1U7V9M2_NICSY
LinkDB: A0A1U7V9M2_NICSY
Original site: A0A1U7V9M2_NICSY 
ID   A0A1U7V9M2_NICSY        Unreviewed;       422 AA.
AC   A0A1U7V9M2;
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=LOC104211213 {ECO:0000313|RefSeq:XP_009758535.1};
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_009758535.1};
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_009758535.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_009758535.1};
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_009758535.1; XM_009760233.1.
DR   AlphaFoldDB; A0A1U7V9M2; -.
DR   SMR; A0A1U7V9M2; -.
DR   STRING; 4096.A0A1U7V9M2; -.
DR   GeneID; 104211213; -.
DR   KEGG; nsy:104211213; -.
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:SF37; ALPHA-AMYLASE 1; 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};
KW   Signal {ECO:0000256|PIRNR:PIRNR001028}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|PIRNR:PIRNR001028"
FT   CHAIN           19..422
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR001028"
FT                   /id="PRO_5010605235"
FT   DOMAIN          21..359
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          360..420
FT                   /note="Alpha-amylase C-terminal beta-sheet"
FT                   /evidence="ECO:0000259|SMART:SM00810"
FT   ACT_SITE        199
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
FT   ACT_SITE        224
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
SQ   SEQUENCE   422 AA;  46677 MW;  EA070D434F67714E CRC64;
     MNSLFPLCLI LSLFPIFATP TLLFQGFNWE SSNQQGGWYN SLINLVPDLA KAGITHVWLP
     PSSNSVSPQG YMPGRLYDLD TSKYGNQQQL QALIKALHDQ GIKAVADIVI NHRCADKKDS
     RGIYCIFEGG TSDDRLDWGP HMICKGDSQY SDGTGNDDTG LDFAAAPDID HLNPQVQKEL
     SDWMNWLKTE IGFDGWRFDF VRGYAPSITK IYMENTSPDF AVGEFWNSIA YGGDGKPDYN
     QDNHRNELAG WVQNGGGAVT AFDFTTKGIL QAAVEGELWR LKDSNGKPPG LIGILPQNAV
     TFIDNHDTGS TQKLWPFPSD KVMQGYAYIL THPGIPSVFY DHFFDWGLKD GISTLVSIRN
     RNGISATSNV QIMAADADLY VAMVDQKIVV KIGPKTDLGS LIPPNYQVAT SGQDYVVWEQ
     KS
//
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