ID   AMYM_BACLI              Reviewed;         578 AA.
AC   Q04977;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Maltogenic alpha-amylase;
DE            EC=3.2.1.133;
DE   AltName: Full=Glucan 1,4-alpha-maltohydrolase;
GN   Name=blmA;
OS   Bacillus licheniformis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27811 / BCRC 10494 / FERM P-1038;
RX   PubMed=1385394; DOI=10.1016/s0021-9258(18)41642-0;
RA   Kim I.C., Cha J.H., Kim J.R., Jang S.Y., Seo B.C., Cheong T.K., Lee D.S.,
RA   Choi Y.D., Park K.H.;
RT   "Catalytic properties of the cloned amylase from Bacillus licheniformis.";
RL   J. Biol. Chem. 267:22108-22114(1992).
CC   -!- FUNCTION: Converts starch into maltose. In contrary to other maltogenic
CC       alpha-amylases BlmA cannot hydrolyze 1,4-alpha-glucosidic linkage next
CC       to 1,6-alpha-glucosidic linkages.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC         polysaccharides so as to remove successive alpha-maltose residues
CC         from the non-reducing ends of the chains.; EC=3.2.1.133;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; X67133; CAA47612.1; -; Genomic_DNA.
DR   PIR; A44326; A44326.
DR   PIR; S25010; S25010.
DR   AlphaFoldDB; Q04977; -.
DR   SMR; Q04977; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; Q04977; -.
DR   GO; GO:0043897; F:glucan 1,4-alpha-maltohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02857; E_set_CDase_PDE_N; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR004185; Glyco_hydro_13_lg-like_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02903; Alpha-amylase_N; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase.
FT   CHAIN           1..578
FT                   /note="Maltogenic alpha-amylase"
FT                   /id="PRO_0000054296"
SQ   SEQUENCE   578 AA;  66924 MW;  F74B65F8672FAEC1 CRC64;
     MIELAAIHHQ PFNSDAYSYN GRTLHIKIRT KKDDAEHVAW FGAILTNTPA HMESERAYVA
     KIGRNKQPMI TGLPKCGLHS GSAIRIYLTA LMIETLFTEA MVHVRFRYRQ THVLNFRLFM
     RQTRLMHRLG QINRLVSNFS GAFRAGGKIC SGKPLPWGRK DPEAHDFFGG HLQGIMTSWT
     IWKTWGEAGI YLTPIFAAPS NHKYDTLDYC SIDPHFGDEE LFRTVVSRIH ERGMKIMLDA
     VFNHIGTSQE WQDVVKNGET SRYKDWFIFI LSLLKKAAMI HLRLVPRCRS SIAGTRKFRL
     ICLILRCTGS ANLISTAGVW MWQMKLIMRF GRNSGKPSPE KPDIFILGEI WHQADPWLRG
     DEFHIGHELP VHRTDDSLFF RRIDFSSQIA SRINSQKMSG MKQVKEVMLN LLDSHERILT
     RCGGDQRKGA RLFWHSCLLR QGRIYYPRKS GFTAAMIHCA GSAWFGKRKN RIKRCLAFMK
     PLIALRKQEN DVLTYGALEW KLVDDQNDFV SFSRTHEGKE LIYFFHQGRE VRRVRLRDLK
     IASDKRIYDA WTEEALHDDD VVDIQPGDFS FLGRSKFC