ID   G8SAJ1_ACTS5            Unreviewed;       707 AA.
AC   G8SAJ1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 63.
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   OrderedLocusNames=ACPL_5621 {ECO:0000313|EMBL:AEV86508.1};
OS   Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV86508.1, ECO:0000313|Proteomes:UP000005440};
RN   [1] {ECO:0000313|Proteomes:UP000005440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31044 / CBS 674.73 / SE50/110
RC   {ECO:0000313|Proteomes:UP000005440};
RA   Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA   Wehmeier U.F., Stoye J., Puehler A.;
RT   "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT   SE50/110.";
RL   Submitted (DEC-2011) 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}.
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DR   EMBL; CP003170; AEV86508.1; -; Genomic_DNA.
DR   RefSeq; WP_014692579.1; NZ_LT827010.1.
DR   AlphaFoldDB; G8SAJ1; -.
DR   STRING; 134676.ACPL_5621; -.
DR   KEGG; ase:ACPL_5621; -.
DR   PATRIC; fig|134676.3.peg.5539; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_013336_3_1_11; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000005440; 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: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   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; 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; 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:UP000005440};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..707
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003515763"
FT   DOMAIN          510..610
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
FT   DOMAIN          610..707
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
FT   REGION          492..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          686..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   707 AA;  72985 MW;  663F7B649958DAF2 CRC64;
     MTKRLVLAAV TSLALAGAGV AGISLAGTAS AAVSLNNSDV TANLWEWNFD SVAAACTSQL
     GPAGYGAVQV APPQESVTLA STSDGAHPWW EVYQPVSYDV SGRLGTQAQF TSMVTTCHNA
     GVRVYVDAVI NHMAGSNNTG GSGYGGSTFN ATGYSYPAVP YSYNDFHHPN DGYCNDDDGQ
     IDDYSNAAEV QNCELVSLSD LKSQDTGVRT KIAGYLNKLV DWGVDGFRVD AAKHMAAADL
     SAIKALLHNT TEGRSPYFAQ EVIPGGSGAI APSAYTGIGD VLGFSYAYGL KTQFANGTLS
     NLSGIPSWSL DATSDQTAAM VTNHDLERNG STLRYQDGST YLLANYFLLA YPYGQPFVYD
     GFAFSTSATG ASPPADANGY VTSTSCTNGA WQCTTQSAGV KGMVAWHNAT RSATTVSNWT
     NTASNVIGFS RGSLGWFGVN RSGSASTATY TTGLADGAYR DRIAGTTITV SGGRASVTIP
     ANGAVAIDVN ARSGSSASPS TSPSVSTSPT SSTGTVQATF NVYAATTAGT SVYVVGSTAA
     LGNWDTAKAV ALSAGGYPIW SSTVAVPSGS SFEYKYLKKD AAGNVTWESN ANRAVTTGSS
     AVTFTNSFGV ANAGATAVTF TESATGTGLY VVGSIASLGS WNTADAIPLT STGASGWSRL
     VALPQRTTFQ YKYLRKDSSG TVTWESGSNR SYTTGTASSY TISDTWK
//