ID A0A3N1A5H9_9ACTN Unreviewed; 733 AA.
AC A0A3N1A5H9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303, ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
GN ORFNames=EDC02_6956 {ECO:0000313|EMBL:ROO52057.1};
OS Micromonospora sp. Llam0.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=2485143 {ECO:0000313|EMBL:ROO52057.1, ECO:0000313|Proteomes:UP000275308};
RN [1] {ECO:0000313|EMBL:ROO52057.1, ECO:0000313|Proteomes:UP000275308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Llam0 {ECO:0000313|EMBL:ROO52057.1,
RC ECO:0000313|Proteomes:UP000275308};
RA D'Agostino P.;
RT "Genome mining of underrepresented organisms for secondary metabolites.";
RL Submitted (NOV-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROO52057.1}.
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DR EMBL; RJJY01000002; ROO52057.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1A5H9; -.
DR Proteomes; UP000275308; 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:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR CDD; cd05808; CBM20_alpha_amylase; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
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 Pfam; PF00686; CBM_20; 2.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SMART; SM01065; CBM_2; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 2.
DR PROSITE; PS51166; CBM20; 2.
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:UP000275308};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..733
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018332117"
FT DOMAIN 537..653
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT DOMAIN 634..733
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT REGION 709..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 733 AA; 76908 MW; F42CB0FBE5FE1FB6 CRC64;
MSVPGSTVSR PMATAVAAVL GIPLAVTLAA PATATTPAPT TATTRAAAPA TTADATATAV
GNGDAIVHLF QWRWDSIAEE CETTLGPDGW GGVQVSPPQE HVVLPSAEGA SYPWWQDYQP
VSYRIDQTRR GDRADFIDMV ERCRDQGVKI YVDMVLNHMS GTGSVGSGPG SAGTVYSKYG
YPDLFGDGSG DSYGYADFGP CYRTISNWGS KTEVQDCELL DLADLNTADP EVRRKIAKYM
NSVIALGVAG FRVDAAKHVQ EAHLADIISR LDDVPGFGGR PDLFHEVYGD GTVPYTAYAP
YGAVTNFDYQ RAVSAAFRDG NVAQLASMPN YGGLTSDQAV VFIDNHDTQR NTPTLTYQDG
DRYYLADAFM LAHPYGTPQL MSSYAFGSVV AQGPPSTGDG TTLPTDCASA EWICEHRDEQ
VAGMVGFRNA TAGTGVGGVV TDGNGRLGFA RADRGYAAFN ATGSTWSRSF TTSLPDGWYC
NVARGTYRPD SGTCTGGTIA VTDGGFHADI PANRAVALHV AARLDCTDPA GCGPVDPPPG
DGTPVTATVQ TVFGQQVRVV GSLPELGSWD PADAAPLSTD ATSYPTWTGS VDVPDGTAFE
WKLVKVDANG TVEWEGGANR SGVGGTPLTA TWGQPGSGTV PVTFDVTATT WYGQEVLVVG
SVPALGSWDP TRAVALAPDG YPVWSGSVTL PAGEPFEYKY VKRAPDGTVD WESGGNRSAT
PAGGATTLTD TWR
//
