ID   AMY3_DICT6              Reviewed;         499 AA.
AC   P14899; B5YAB2;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Alpha-amylase 3;
DE            EC=3.2.1.1;
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
GN   Name=amyC; OrderedLocusNames=DICTH_1568;
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].
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;
CC         Evidence={ECO:0000250|UniProtKB:Q8A1G3};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8A1G3};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: The profile of production of reducing sugar from soluble
CC       starch by the action of AmyC was intermediate between those of AmyA and
CC       AmyB.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; X15948; CAA34072.1; -; Genomic_DNA.
DR   EMBL; CP001146; ACI19039.1; -; Genomic_DNA.
DR   PIR; S01313; S01313.
DR   RefSeq; WP_012547671.1; NC_011297.1.
DR   AlphaFoldDB; P14899; -.
DR   SMR; P14899; -.
DR   STRING; 309799.DICTH_1568; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ACI19039; ACI19039; DICTH_1568.
DR   KEGG; dth:DICTH_1568; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_006462_2_4_0; -.
DR   OMA; CARTPMQ; -.
DR   OrthoDB; 1573900at2; -.
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   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.90.400.10; -; 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   Pfam; PF00128; Alpha-amylase; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Calcium; Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase;
KW   Metal-binding.
FT   CHAIN           1..499
FT                   /note="Alpha-amylase 3"
FT                   /id="PRO_0000054286"
FT   ACT_SITE        213
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        248
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q8A1G3"
FT   BINDING         183
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q8A1G3"
FT   BINDING         217
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:Q8A1G3"
FT   SITE            315
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        279..296
FT                   /note="VANQKDLGIIEFLEFERE -> SSKSKRLRNYRISRLKR (in Ref. 1;
FT                   CAA34072)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        341..344
FT                   /note="PGIP -> AGNT (in Ref. 1; CAA34072)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   499 AA;  59086 MW;  FE6E3FC8F5D0CDAB CRC64;
     MKIKFFIKRT LIFIFILVTF LTYIHGYNEP WYKNAIFYEV FVRSFADSDG DRVGDLNGLI
     DKLDYFKNLN ITALWLMPIF PSVSYHGYDV TDYYDIHPGY GTMEDFENLI RKAHEKNIKI
     ILDLVVNHTS SRHPWFVSSA SSYNSPYRDY YIWSTEKPEK NSNLWYKKPT GYYYALFWSE
     MPDLNFDNPK VREEVKKIAK FWIEKGVDGF RLDAAKHIYD DDSKNIQWWK EFYSYLKSIK
     PDVYLVGEVW DNEYKIAEYY KGLPSNFNFP LSDKIMNSVA NQKDLGIIEF LEFERELFGE
     NNTDFADAIF LRNHDQVRVR TFFGGSIDKS ILAGSIYLTL PGIPFIYYGE EIGMEGSKPD
     EYIREPFKWT DDMKSKYQTY WIIPRYNLPG NGIALDTEEK DPNSIYNHYK KLLEIRVKCR
     ALSNGKIERI KTQDRSILAY KLELEDEKIM VVHNLNRIEN TFNFNNEIKE KDILYIRNAK
     TEKNKIILGP YSTVIVKIP