ID A0A345XJZ7_9ACTN Unreviewed; 455 AA.
AC A0A345XJZ7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303, ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN ORFNames=DVA86_04170 {ECO:0000313|EMBL:AXK31963.1};
OS Streptomyces armeniacus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=83291 {ECO:0000313|EMBL:AXK31963.1, ECO:0000313|Proteomes:UP000254425};
RN [1] {ECO:0000313|EMBL:AXK31963.1, ECO:0000313|Proteomes:UP000254425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15676 {ECO:0000313|EMBL:AXK31963.1,
RC ECO:0000313|Proteomes:UP000254425};
RA Labana P., Gosse J.T., Boddy C.N.;
RT "Draft genome of the type strain Streptomyces armeniacus ATCC 15676.";
RL Submitted (JUL-2018) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP031320; AXK31963.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345XJZ7; -.
DR Proteomes; UP000254425; Chromosome.
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 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:UP000254425};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..455
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038970886"
FT DOMAIN 36..363
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 372..454
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
SQ SEQUENCE 455 AA; 47954 MW; 9FDE5AB15159CCCF CRC64;
MRKRLFGGVM AGVLATGGLY AAAPWQSQAT PPGEKTVTAT LFETPFATVG KACTDSLGPA
GYGYVEVSPA TEHIEGDQWW TSYQPVSYKI AGRLGDAEAF KSMVSACHEA GVKVIADAVV
NHMSAGSGTG TGGTQYTKYD YPGLYQDGDF HGCREDIADY TNREEVQNCE LVGLADLDTG
SDAVQTKIAA YLDSLREMGV DGFRIDAAKH MSAADMEAIK GKMADPGFWV SEVIYGGGEP
VTPEEYTGLG DVDEFRYGSH LKSAFQGGDL AGLQNIADGK LESGKARTFV DNWDTERNGS
TLTYKDGELH TLANAFMLAH PYGSPNVFSG YEWSDKDAGP PSGGDGWTNM HARPEITGMV
GFRNAVGDAE LTDWWAEGSA LAFSRGDRGF VALNAGDGDL QQAFTTSLPG GTYCNVAKAA
PGDCAGNTVT VGDDGKVEAT VPAKGALALH ADAKE
//
