ID W9SAM5_9ROSA Unreviewed; 425 AA.
AC W9SAM5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
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 ORFNames=L484_006341 {ECO:0000313|EMBL:EXC19766.1};
OS Morus notabilis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX NCBI_TaxID=981085 {ECO:0000313|EMBL:EXC19766.1, ECO:0000313|Proteomes:UP000030645};
RN [1] {ECO:0000313|Proteomes:UP000030645}
RP NUCLEOTIDE SEQUENCE.
RA He N., Zhao S.;
RT "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL Submitted (JAN-2013) 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 -!- 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; KE345892; EXC19766.1; -; Genomic_DNA.
DR RefSeq; XP_010108610.1; XM_010110308.1.
DR AlphaFoldDB; W9SAM5; -.
DR STRING; 981085.W9SAM5; -.
DR GeneID; 21389772; -.
DR KEGG; mnt:21389772; -.
DR eggNOG; KOG0471; Eukaryota.
DR OrthoDB; 2728918at2759; -.
DR Proteomes; UP000030645; Unassembled WGS sequence.
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:UP000030645};
KW Signal {ECO:0000256|PIRNR:PIRNR001028}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|PIRNR:PIRNR001028"
FT CHAIN 24..425
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|PIRNR:PIRNR001028"
FT /id="PRO_5010605299"
FT DOMAIN 24..363
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 364..424
FT /note="Alpha-amylase C-terminal beta-sheet"
FT /evidence="ECO:0000259|SMART:SM00810"
FT ACT_SITE 201
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
FT ACT_SITE 226
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001028-1"
SQ SEQUENCE 425 AA; 47717 MW; 1CA50044AA786F5F CRC64;
MKVPIAFGLL CLFISLFPPF TSPTILFQGF NWASSENAGW YNSLKNTIPD LAKVGITHVW
LPPPSHSAAD QGYLPGRLYD LNASKYGTQE ELKSLIAALR EKGIKVIADI VLNHRSAEKR
DERGILCIFE GGTSDARLDW GPSFICRDDT EFSDGTGNLD TGDSWGEVPD IDHLNPQVQR
ELSEWMNWLK TEIGFVGWRF DMVRGYAPNI TKIYMEQTSP EFAVGEKWDR QEFAVGEDGK
PNANQDYHRG LLVNWVEAAG GSVTAFDFTT KGILQAAVEG ELWRLKDSNG KPPGLIGIKP
ESAVTFIDNH DTWSQKLWPF PEDKIMLGYV YILTHPGIPT IFYDHLFIKR ELMAPISNVT
AIRNRHGINS RSVVNILAAE ADLYMSRIDE KIIMKIGPKT DLGNLLPSDY QVAYSGQDFA
VWEKK
//
