ID   AMY1_DICT6              Reviewed;         686 AA.
AC   P09961; B5YDK4;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=Alpha-amylase 1;
DE            EC=3.2.1.1;
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
GN   Name=amyA; OrderedLocusNames=DICTH_0745;
OS   Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12).
OC   Bacteria; Dictyoglomota; Dictyoglomia; Dictyoglomales; Dictyoglomaceae;
OC   Dictyoglomus.
OX   NCBI_TaxID=309799;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-13.
RX   PubMed=2453362; DOI=10.1111/j.1432-1033.1988.tb14056.x;
RA   Fukusumi S., Kamizono A., Horinouchi S., Beppu T.;
RT   "Cloning and nucleotide sequence of a heat-stable amylase gene from an
RT   anaerobic thermophile, Dictyoglomus thermophilum.";
RL   Eur. J. Biochem. 174:15-21(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   -!- FUNCTION: This amylase is a highly liquefying-type: oligomers appeared
CC       at the beginning of incubation, followed by a graded decrease in the
CC       amounts of maltotriose, maltose and glucose in prolonged incubation.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5. Stable above pH 5.5.;
CC       Temperature dependence:
CC         Optimum temperature is about 90 degrees Celsius. Highly thermostable.
CC         Retains 70% of its maximal activity after heating 1 hour at 90
CC         degrees Celsius, but no decrease in activity was observed within the
CC         same time at 80 degrees Celsius.;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 57 family. {ECO:0000305}.
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DR   EMBL; X07896; CAA30735.1; -; Genomic_DNA.
DR   EMBL; CP001146; ACI18637.1; -; Genomic_DNA.
DR   PIR; S00628; ALDYAT.
DR   RefSeq; WP_012547269.1; NC_011297.1.
DR   AlphaFoldDB; P09961; -.
DR   SMR; P09961; -.
DR   STRING; 309799.DICTH_0745; -.
DR   CAZy; GH57; Glycoside Hydrolase Family 57.
DR   PaxDb; 309799-DICTH_0745; -.
DR   KEGG; dth:DICTH_0745; -.
DR   eggNOG; COG1449; Bacteria.
DR   HOGENOM; CLU_026700_0_0_0; -.
DR   OrthoDB; 9757977at2; -.
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:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd10793; GH57N_TLGT_like; 1.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 3.20.110.20; -; 1.
DR   InterPro; IPR015179; A-amylase/a-glucTrfase_C.
DR   InterPro; IPR015178; A-amylase/a-glucTrfase_central.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR   InterPro; IPR004300; Glyco_hydro_57_N.
DR   PANTHER; PTHR36306:SF1; 4-ALPHA-GLUCANOTRANSFERASE; 1.
DR   PANTHER; PTHR36306; ALPHA-AMYLASE-RELATED-RELATED; 1.
DR   Pfam; PF09094; AmyA-A_glucT_m; 1.
DR   Pfam; PF09095; AmyA-gluTrfs_C; 1.
DR   Pfam; PF03065; Glyco_hydro_57; 1.
DR   SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cytoplasm; Direct protein sequencing; Glycosidase;
KW   Hydrolase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2453362"
FT   CHAIN           2..686
FT                   /note="Alpha-amylase 1"
FT                   /id="PRO_0000184571"
FT   ACT_SITE        125
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        216
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   686 AA;  81192 MW;  DFF73F94A439E187 CRC64;
     MTKSIYFSLG IHNHQPVGNF DFVIERAYEM SYKPLINFFF KHPDFPINVH FSGFLLLWLE
     KNHPEYFEKL KIMAERGQIE FVSGGFYEPI LPIIPDKDKV QQIKKLNKYI YDKFGQTPKG
     MWLAERVWEP HLVKYIAEAG IEYVVVDDAH FFSVGLKEED LFGYYLMEEQ GYKLAVFPIS
     MKLRYLIPFA DPEETITYLD KFASEDKSKI ALLFDDGEKF GLWPDTYRTV YEEGWLETFV
     SKIKENFLLV TPVNLYTYMQ RVKPKGRIYL PTASYREMME WVLFPEAQKE LEELVEKLKT
     ENLWDKFSPY VKGGFWRNFL AKYDESNHMQ KKMLYVWKKV QDSPNEEVKE KAMEEVFQGQ
     ANDAYWHGIF GGLYLPHLRT AIYEHLIKAE NYLENSEIRF NIFDFDCDGN DEIIVESPFF
     NLYLSPNHGG SVLEWDFKTK AFNLTNVLTR RKEAYHSKLS YVTSEAQGKS IHERWTAKEE
     GLENILFYDN HRRVSFTEKI FESEPVLEDL WKDSSRLEVD SFYENYDYEI NKDENKIRVL
     FSGVFRGFEL CKSYILYKDK SFVDVVYEIK NVSETPISLN FGWEINLNFL APNHPDYYFL
     IGDQKYPLSS FGIEKVNNWK IFSGIGIELE CVLDVEASLY RYPIETVSLS EEGFERVYQG
     SALIHFYKVD LPVGSTWRTT IRFWVK
//