ID A0A093G9C5_DRYPU Unreviewed; 512 AA.
AC A0A093G9C5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
GN ORFNames=N307_03145 {ECO:0000313|EMBL:KFV63364.1};
OS Dryobates pubescens (Downy woodpecker) (Picoides pubescens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Piciformes; Picidae; Dryobates.
OX NCBI_TaxID=118200 {ECO:0000313|EMBL:KFV63364.1, ECO:0000313|Proteomes:UP000053875};
RN [1] {ECO:0000313|EMBL:KFV63364.1, ECO:0000313|Proteomes:UP000053875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N307 {ECO:0000313|EMBL:KFV63364.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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|RuleBase:RU361134};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000256|ARBA:ARBA00001923};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR EMBL; KL215152; KFV63364.1; -; Genomic_DNA.
DR RefSeq; XP_009909371.1; XM_009911069.1.
DR AlphaFoldDB; A0A093G9C5; -.
DR STRING; 118200.A0A093G9C5; -.
DR GeneID; 104309716; -.
DR KEGG; dpub:104309716; -.
DR OrthoDB; 3249969at2759; -.
DR Proteomes; UP000053875; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
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; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053875};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..512
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012700733"
FT DOMAIN 26..414
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 423..511
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
SQ SEQUENCE 512 AA; 57668 MW; 5B0B248B9AFA82B9 CRC64;
MQVLLLLVAV GLCWGQYTPN TLPGRTSIVH LFEWRWADIA LECERYLAPN GFGGVQVSPP
NENIVITNPN RPWWERYQPV SYKICTRSGN EDEFRDMVTR CNNVGVRIYV DAVVNHMCST
AGGAGTHSTC GSYFNAGNRD FPAVPYSGWD FNDGKCRTGS GDIENYGDIY QVRDCRLVSL
LDLALEKDYV RSKVAEYMNH LIDIGVAGFR IDAAKHMWPG DMRAFLDKLN DLNTKWFSPG
TKPFIYQEVI DLGGEPIKGS DYFGNGRVTE FKYGAKLGTV IRKWNGEKMA YLKNWGEGWG
FVPSDRALVF VDNHDNQRGH GAGGASILTF WDSRLYKMAV GFMLAHPYGV TRVMSSFRWP
RYFVDGRDIN DWVGPPSNAD GSIKPVTINA DTTCGNDWVC EHRWRQIRNM VIFRNVVDGE
PFSNWWDNGS NQVAFGRGNK GFIVFNNDDW YMNVYLQTGL PAGTYCDIIS GQKEGDKCTG
KVLYVSGDGM ANFQITNTDE DPFIAIHVDA KL
//
