ID   F8JNS6_STREN            Unreviewed;       597 AA.
AC   F8JNS6; G8WMT7;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 76.
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=SCATT_02840 {ECO:0000313|EMBL:AEW92655.1};
OS   Streptantibioticus cattleyicolor (strain ATCC 35852 / DSM 46488 / JCM 4925
OS   / NBRC 14057 / NRRL 8057) (Streptomyces cattleya).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptantibioticus.
OX   NCBI_TaxID=1003195 {ECO:0000313|EMBL:AEW92655.1, ECO:0000313|Proteomes:UP000007842};
RN   [1] {ECO:0000313|Proteomes:UP000007842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057
RC   {ECO:0000313|Proteomes:UP000007842};
RA   Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.;
RT   "Complete genome sequence of Streptomyces cattleya strain DSM 46488.";
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; CP003219; AEW92655.1; -; Genomic_DNA.
DR   RefSeq; WP_014141049.1; NC_017586.1.
DR   AlphaFoldDB; F8JNS6; -.
DR   STRING; 1003195.SCATT_02840; -.
DR   KEGG; scy:SCATT_02840; -.
DR   PATRIC; fig|1003195.11.peg.1918; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_013336_0_0_11; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000007842; 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   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; 1.
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; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SMART; SM01065; CBM_2; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR   PROSITE; PS51166; CBM20; 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:UP000007842};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..45
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           46..597
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003378800"
FT   DOMAIN          497..597
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
FT   REGION          574..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..597
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   597 AA;  63025 MW;  B955E40EF88BBE8C CRC64;
     MLRHAHDRPA RRRPSRLRAA LASGALLTAG LVPLTLTAAA GPARAATPSG DVIANLFMWN
     WPSVARECTD VLGPDGYGGV QVAPPADSLS TSGHPWWEVY QPVDYHLTSR MGDESAFRSM
     VATCRKAGVK VYVDAVINHT SGVDGTSYGG VTYTKYAYPD YTDADFHHYP ADCPQSDGQI
     HNWNDYTEVT HCELLHLADL RTESAHVRTT LTSYLDKLID YGVSGFRVDA AKHIGHEDLA
     AIEAQLHTTA DGTRPYIAQE IAPGGTGDLS PASFENTGDV LGFDYADGLK SAFTGSLASL
     RNFSAGLLGS DQEEVFVQNH DTERDGSTLS YRDGAVNTLA TEFELAYGYG TPQVYAGFDF
     TGKDDSPPAD ASGHVTDTTC GTGWECTDRI PGVAAMVGWH DTVAGAPVAD WYDDGADLIA
     FGRGGKGWIA LNNGSTAQQR TFATGLPAGS YCDVIHGRAT ATGPCTGPAV TVDAAGDATV
     TVPAKDAVAI DVAARGTSTT ATVPVSFDPT VTTWYGQNVY VTGSLPALGG WDPGKAVALS
     PADYPVWKAT VALPANTPFE YKYVKKDPDG TVEWESGGNR TATTGASGGL TLNDTWK
//