ID   D2BR19_LACLK            Unreviewed;       491 AA.
AC   D2BR19;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:ADA64994.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:ADA64994.1};
GN   Name=amyL {ECO:0000313|EMBL:ADA64994.1};
GN   OrderedLocusNames=LLKF_1316 {ECO:0000313|EMBL:ADA64994.1};
OS   Lactococcus lactis subsp. lactis (strain KF147).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=684738 {ECO:0000313|EMBL:ADA64994.1, ECO:0000313|Proteomes:UP000001886};
RN   [1] {ECO:0000313|EMBL:ADA64994.1, ECO:0000313|Proteomes:UP000001886}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KF147 {ECO:0000313|EMBL:ADA64994.1,
RC   ECO:0000313|Proteomes:UP000001886};
RX   PubMed=18039825; DOI=10.1128/AEM.01850-07;
RA   Siezen R.J., Starrenburg M.J., Boekhorst J., Renckens B., Molenaar D.,
RA   van Hylckama Vlieg J.E.;
RT   "Genome-scale genotype-phenotype matching of two Lactococcus lactis
RT   isolates from plants identifies mechanisms of adaptation to the plant
RT   niche.";
RL   Appl. Environ. Microbiol. 74:424-436(2008).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   EMBL; CP001834; ADA64994.1; -; Genomic_DNA.
DR   RefSeq; WP_012897858.1; NC_013656.1.
DR   AlphaFoldDB; D2BR19; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; llk:LLKF_1316; -.
DR   HOGENOM; CLU_024572_2_1_9; -.
DR   Proteomes; UP000001886; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11318; AmyAc_bac_fung_AmyA; 1.
DR   Gene3D; 2.40.30.140; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR013776; A-amylase_thermo.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   PIRSF; PIRSF001021; Alph-amls_thrmst; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR001021-2};
KW   Glycosidase {ECO:0000313|EMBL:ADA64994.1};
KW   Hydrolase {ECO:0000313|EMBL:ADA64994.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2}.
FT   DOMAIN          2..386
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        229
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT   ACT_SITE        259
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT   BINDING         102
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         181
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         192
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         198
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         200
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         233
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         298
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         402
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ   SEQUENCE   491 AA;  57088 MW;  BFAF30BEFF2DF7D5 CRC64;
     MKTILQAFEW YLPSDSQHWN NIKENIPDLG KLGFSGLWLP PASKAASGVE DVGYGTYDLF
     DLGEFDQKGT IPTKYGTKDE YLDLINTLHH NNIEVYADIV FNHMMGADET ETIEADIKAE
     DNHLHNIENN KTVEVWTKFT FPGRQGKYDN YIWTWHNFTG IDYDERKNQE EILEFEGHEW
     DENVDSENNN FDYLMGADLD FSVSETVEQL EKWGHWFSEM TKIDGFRLDA IKHIDFKYFD
     KWLEQRAKQL DKKLFIVGEY WSDDLGKLEY YLEQSGDKIQ LFDVPLHFNM KEASSSNGEF
     DMRTLFDHTL TASQPELSVT FVDNHDTQEG QALESWIPAW FKEHAYSLIL LRKKGTPTVF
     WGDLYGIHSR NVNPVGDNLR TMIALRKDSE FLRENDYFDH PDIIGWTNIL KIDNKEYGLS
     CILTNKNGGS KYMIIDKAYA GKVYIDLFGR HEIPITLDQN GGAEFYVNDG SVSVWVDKEI
     VSKIDQMNFQ N
//