ID   AMY2_DICT6              Reviewed;         562 AA.
AC   P14898;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Alpha-amylase 2;
DE            EC=3.2.1.1;
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
GN   Name=amyB; OrderedLocusNames=DICTH_0636.1;
OS   Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12).
OC   Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus.
OX   NCBI_TaxID=309799;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-8.
RX   PubMed=2458257; DOI=10.1111/j.1432-1033.1988.tb14275.x;
RA   Horinouchi S., Fukusumi S., Ohshima T., Beppu T.;
RT   "Cloning and expression in Escherichia coli of two additional amylase genes
RT   of a strictly anaerobic thermophile, Dictyoglomus thermophilum, and their
RT   nucleotide sequences with extremely low guanine-plus-cytosine contents.";
RL   Eur. J. Biochem. 176:243-253(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35947 / DSM 3960 / H-6-12;
RX   PubMed=24558247; DOI=10.1128/genomea.00109-14;
RA   Coil D.A., Badger J.H., Forberger H.C., Riggs F., Madupu R., Fedorova N.,
RA   Ward N., Robb F.T., Eisen J.A.;
RT   "Complete Genome Sequence of the Extreme Thermophile Dictyoglomus
RT   thermophilum H-6-12.";
RL   Genome Announc. 2:0-0(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;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: When compared to AmyA, AmyB produced larger amounts of
CC       reducing sugar.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; X13199; CAA31586.1; -; Genomic_DNA.
DR   EMBL; CP001146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S01312; S01312.
DR   RefSeq; WP_049751865.1; NC_011297.1.
DR   AlphaFoldDB; P14898; -.
DR   SMR; P14898; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PRIDE; P14898; -.
DR   OrthoDB; 99080at2; -.
DR   Proteomes; UP000001733; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00128; Alpha-amylase; 2.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Calcium; Carbohydrate metabolism; Cytoplasm; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Metal-binding.
FT   CHAIN           1..562
FT                   /note="Alpha-amylase 2"
FT                   /id="PRO_0000054285"
FT   ACT_SITE        309
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        338
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255"
FT   SITE            404
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        124
FT                   /note="N -> S (in Ref. 1; CAA31586)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   562 AA;  67027 MW;  368FF33D155FC3F4 CRC64;
     MIYDDKIFGD LCHKEFLVER EVKKLEEIYL EEVLPEDPKP EDEIEFTFNC PLKFHITSGK
     IVKDNREIYT FNIQERKTQW NDSIFNFSEI IKIKIPPLKE NGLYQIHLYE MNEKIYEQYL
     SIDNFEAPLW SEESIIYHIF IDRFAKDEKE VEYSENLKEK LGGNLKGILS RLDYIENLGI
     NTIWISPIFK STSYHGYDIE DYFEIDPIWG TKEDLKKLVR EAFNRGIRII LDFVPNHMSY
     KNPIFQKALK DKNSNLRSWF IFKGEDYETF FGVKSMPKIN LKNKEAIDYI INAAKYWIRE
     FGISGYRMDH ATGPDINFWS IFYYNLKSEF PETFYFGEIV ETPKETKKYV GKFDGTLDFY
     LFKIIRDFFI GKRWSTKEFV KMIDLEEKFY GNKFKRISFL ENHDSNRFLW VAKDKKLLRL
     ASIFQFSINA IPIIYNGQEM GCSQYRDILE GNRTLHEHAR LPIPWSDDKQ DKELIDFYRQ
     LVKIRKSHPA LYKGTFIPIF SDMISFIKET QEESILVLIN IEDKEEIFNL NGTYRDLFSG
     NIYTNSLKLG PMSAHLLLRI DH