AMY1_DICT6
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 03-AUG-2022, entry version 113.
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; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; 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 PRIDE; P09961; -.
DR EnsemblBacteria; ACI18637; ACI18637; DICTH_0745.
DR KEGG; dth:DICTH_0745; -.
DR eggNOG; COG1449; Bacteria.
DR HOGENOM; CLU_026700_0_0_0; -.
DR OMA; HFMSAGL; -.
DR OrthoDB; 94039at2; -.
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 Gene3D; 2.70.98.10; -; 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 Pfam; PF09094; DUF1925; 1.
DR Pfam; PF09095; DUF1926; 1.
DR Pfam; PF03065; Glyco_hydro_57; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR SUPFAM; SSF88688; SSF88688; 1.
DR SUPFAM; SSF88713; SSF88713; 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