ID   R4LFC1_ACTS9            Unreviewed;       611 AA.
AC   R4LFC1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
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=L083_4517 {ECO:0000313|EMBL:AGL18027.1};
OS   Actinoplanes sp. (strain N902-109).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=649831 {ECO:0000313|EMBL:AGL18027.1, ECO:0000313|Proteomes:UP000013541};
RN   [1] {ECO:0000313|EMBL:AGL18027.1, ECO:0000313|Proteomes:UP000013541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N902-109 {ECO:0000313|EMBL:AGL18027.1,
RC   ECO:0000313|Proteomes:UP000013541};
RA   Hu H., Huang H., Lu X., Zhu B.;
RT   "Comparative analysis of rapamycin biosynthesis clusters between
RT   Streptomyces hygroscopicus ATCC 29253 and Actinoplanes sp. N902-109.";
RL   Submitted (MAY-2013) 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; CP005929; AGL18027.1; -; Genomic_DNA.
DR   RefSeq; WP_015622585.1; NC_021191.1.
DR   AlphaFoldDB; R4LFC1; -.
DR   STRING; 649831.L083_4517; -.
DR   KEGG; actn:L083_4517; -.
DR   PATRIC; fig|649831.3.peg.4448; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_013336_3_1_11; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000013541; 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:UP000013541}.
FT   DOMAIN          508..611
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
FT   REGION          589..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   611 AA;  63379 MW;  59B7AFE4AFDCBF93 CRC64;
     MRTPKVAVTA ATVVVAAAAA VVVAFGGTGI AHASPRIIPA AAGGAGTPTT ASAASPGTKD
     TIVHLFEWPW ASVANECTTV LGPKGFGGVQ VSPPQEHVVL PGQGYPWWQD YQPVSYQLTS
     RRGNRAAFAA MVSTCHAAGV KIYVDAVVNH MAGGASSGTG SGGSAYSHYA YPAVPYGNDD
     FHHCGRNGND DIVNYSDKWE VQNCELVDLS DLKTESSYVR GKLTSYLNDL VSLGVDGFRV
     DAAKHMPAAD MAAFIDPVAG DPYVFSEVIE GGSGEPTPEE YTGIGDVTEF RYGDVVGGAF
     QSGSLSGLNG LAGQMRLASG DAVAFIDNHD TQRNGRAKLT YQNGAPYALA EAFMIAYPYG
     VPQIMSSFTF SNNDAGPPAA SNGTTTAVSC GNGWQCEHRA RTTANMVGLR NAAAGAGVTN
     WWSNGSNQIA FGRGSNAYVA FNRSGSALTR TFQTSLPAGT YCDVMAGDFT NGTCSGPSYA
     VSSSGQVTAT VAANSAFALH INARGGSTNP TGCTSAAVDV EATVSTTFGQ NVFVTGNTAA
     LGNWDPNSAV ALSSASYPVW KATVTLPGNT SVQYKYIKKE GSTVIWESDP NRTRTTPGTG
     PCTATWSDSW R
//