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Database: UniProt
Entry: A0A069DD67_9BACL
LinkDB: A0A069DD67_9BACL
Original site: A0A069DD67_9BACL 
ID   A0A069DD67_9BACL        Unreviewed;       575 AA.
AC   A0A069DD67;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=TCA2_2732 {ECO:0000313|EMBL:GAK40242.1};
OS   Paenibacillus sp. TCA20.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1499968 {ECO:0000313|EMBL:GAK40242.1, ECO:0000313|Proteomes:UP000028160};
RN   [1] {ECO:0000313|EMBL:GAK40242.1, ECO:0000313|Proteomes:UP000028160}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCA20 {ECO:0000313|EMBL:GAK40242.1,
RC   ECO:0000313|Proteomes:UP000028160};
RA   Fujinami S., Takeda-Yano K., Onodera T., Satoh K., Sano M., Takahashi Y.,
RA   Narumi I., Ito M.;
RT   "Draft Genome Sequence of Calcium-Dependent Paenibacillus sp. Strain TCA20,
RT   Isolated from a Hot Spring Containing a High Concentration of Calcium
RT   Ions.";
RL   Genome Announc. 2:e00866-14(2014).
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:GAK40242.1}.
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DR   EMBL; BBIW01000004; GAK40242.1; -; Genomic_DNA.
DR   RefSeq; WP_047911390.1; NZ_BBIW01000004.1.
DR   AlphaFoldDB; A0A069DD67; -.
DR   eggNOG; COG0366; Bacteria.
DR   Proteomes; UP000028160; 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; IPR032091; Malt_amylase_C.
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   Pfam; PF16657; Malt_amylase_C; 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:UP000028160};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..575
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001660142"
FT   DOMAIN          87..491
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          35..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   575 AA;  63722 MW;  FA2545672DBA052A CRC64;
     MAPRHLLGLN KRFGYPAIVL LMACMLAACS SEGAEQPSQQ GEDSAAINTE AGQKSSDGNH
     SAEESEAGGQ GNAELVIDEQ PSTVYYEIFV RSFYDSDGDG IGDLNGITEK LDYLNDGQPG
     GDDLGVGGIW LMPINPSPSY HGYDVTDYYD VHPDYGTKDD LKHLLDEAHE RGIKVIMDLV
     VNHTSTEHPW FKESSASLDS AYRDWYSWAE DTGENTTGMS AAGSGPAWHE LGGKHYLGTF
     WSGMPDLNFD NEEVQSEMLA IGQHWLEFGF DGFRLDAAKH IYEDVQSDRS AETTEKNVAW
     WQEFRTAMNQ VKEDAYIVGE VWENSPVSVA PYLDNAFDSG FNFGLADQII RTVTNETNGG
     FIVQLTRNYE LFNEKSEGAF VDAVFLANHD QNRVMSQLGG SADHAHMAAS ILLTLPGNPF
     IYYGEEIGME GAKPDEQIRE PMLWYQAEAG AGQTTWQTPK HNLGEDAVSV EDQLQDSSSL
     LSHYRELIDW RNGSRALTDG TIADYDLDDD QLLGYVRAAE GERVLVLHNL SNEEKEVALD
     DSEVKYSELL HATNAEVQWA DQTLTLPPYT SVIIK
//
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