ID   A0A0Q4RNA6_9BACL        Unreviewed;       564 AA.
AC   A0A0Q4RNA6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=ASF12_06140 {ECO:0000313|EMBL:KQO18212.1};
OS   Paenibacillus sp. Leaf72.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1736234 {ECO:0000313|EMBL:KQO18212.1, ECO:0000313|Proteomes:UP000051722};
RN   [1] {ECO:0000313|EMBL:KQO18212.1, ECO:0000313|Proteomes:UP000051722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf72 {ECO:0000313|EMBL:KQO18212.1,
RC   ECO:0000313|Proteomes:UP000051722};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQO18212.1, ECO:0000313|Proteomes:UP000051722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf72 {ECO:0000313|EMBL:KQO18212.1,
RC   ECO:0000313|Proteomes:UP000051722};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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|RuleBase:RU361134};
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:KQO18212.1}.
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DR   EMBL; LMLV01000001; KQO18212.1; -; Genomic_DNA.
DR   RefSeq; WP_056030945.1; NZ_LMLV01000001.1.
DR   AlphaFoldDB; A0A0Q4RNA6; -.
DR   STRING; 1736234.ASF12_06140; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000051722; Unassembled WGS sequence.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11316; AmyAc_bac2_AmyA; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
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   InterPro; IPR045857; O16G_dom_2.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF179; NEUTRAL AND BASIC AMINO ACID TRANSPORT PROTEIN RBAT; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Glycosidase {ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|RuleBase:RU361134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051722}.
FT   DOMAIN          80..476
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          40..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   564 AA;  62423 MW;  EDEE7965BDE7D6C1 CRC64;
     MGIRADDGKY ASVKEACLAA LILLPLLLLV AACSSDSGFS SSPSSSSSSS SSDSDSPSPT
     PSSEVGSYEV DEQPSTVYYE IFVRSFYDTN GDGIGDLNGV TAKLDYLKQL GIGGIWLMPI
     QPSPSYHGYD VTDYYAINPD YGTMEDLHKL LEEAHERNIK VIMDLVVNHT STEHPWFKEA
     VADAASPYRS WYHFAEQDER VQLDGAVGSN PWHAAGSGRY LGVFWEGMPD LNFDEPAVRD
     EMIQIGQFWL EQGLDGFRLD AAKHIYGDFA STVNRDAVKN NNQRWWQQFR SGLAKVNPGV
     FLIGEVWDSV TIVAPYLDRA FDSAFNFDLA GSLLRAASYE SDPDAAFSLN RAYKLYGDAS
     GGAFADAPFL SNHDQNRVMS LLNGNAAHAK TAASLLLTLP GNPFIYYGEE IGMKGMKPDE
     HIREPMLWYS ALSGGEGQTT WERSSSNANP NAISVEAQLN DEQSLLAYYQ MLIGWRNELP
     ALRDGGIEEY RLDPPLRQVS SYIRATAKER VLVLINLSNE QQIAELHEQE PFGLFDKVIR
     ASHKEVEIQE GLISLPPYSV IIVK
//