ID   AMYA_PYRFU              Reviewed;         649 AA.
AC   P49067;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Alpha-amylase;
DE            EC=3.2.1.1;
GN   Name=amyA; OrderedLocusNames=PF0272;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=8226990; DOI=10.1016/s0021-9258(20)80539-0;
RA   Laderman K.A., Asada K., Uemori T., Mukai H., Taguchi Y., Kato I.,
RA   Anfinsen C.B.;
RT   "Alpha-amylase from the hyperthermophilic archaebacterium Pyrococcus
RT   furiosus. Cloning and sequencing of the gene and expression in Escherichia
RT   coli.";
RL   J. Biol. Chem. 268:24402-24407(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
RN   [3]
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=8226989; DOI=10.1016/s0021-9258(20)80538-9;
RA   Laderman K.A., Davis B.R., Krutzsch H.C., Lewis M.S., Griko Y.V.,
RA   Privalov P.L., Anfinsen C.B.;
RT   "The purification and characterization of an extremely thermostable alpha-
RT   amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus.";
RL   J. Biol. Chem. 268:24394-24401(1993).
CC   -!- FUNCTION: Displays a broad range of substrate specificity, with the
CC       capacity to hydrolyze carbohydrates as simple as maltotriose.
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 6.5-7.5.;
CC       Temperature dependence:
CC         Optimum temperature is 100 degrees Celsius. Inactive below 40 degrees
CC         Celsius. Extremely thermostable.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 57 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL80396.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L22346; AAA72035.1; -; Unassigned_DNA.
DR   EMBL; AE009950; AAL80396.1; ALT_INIT; Genomic_DNA.
DR   PIR; A49512; A49512.
DR   AlphaFoldDB; P49067; -.
DR   SMR; P49067; -.
DR   STRING; 186497.PF0272; -.
DR   CAZy; GH57; Glycoside Hydrolase Family 57.
DR   PRIDE; P49067; -.
DR   EnsemblBacteria; AAL80396; AAL80396; PF0272.
DR   KEGG; pfu:PF0272; -.
DR   PATRIC; fig|186497.12.peg.284; -.
DR   eggNOG; arCOG03280; Archaea.
DR   HOGENOM; CLU_026700_0_0_2; -.
DR   OMA; HFMSAGL; -.
DR   PhylomeDB; P49067; -.
DR   BioCyc; MetaCyc:MON-16304; -.
DR   Proteomes; UP000001013; Chromosome.
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; Direct protein sequencing; Glycosidase; Hydrolase;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..649
FT                   /note="Alpha-amylase"
FT                   /id="PRO_0000184573"
FT   ACT_SITE        124
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        215
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   649 AA;  76309 MW;  B75840D33D17146F CRC64;
     MGDKINFIFG IHNHQPLGNF GWVFEEAYEK CYWPFLETLE EYPNMKVAIH TSGPLIEWLQ
     DNRPEYIDLL RSLVKRGQVE IVVAGFYEPV LASIPKEDRI EQIRLMKEWA KSIGFDARGV
     WLTERVWQPE LVKTLKESGI DYVIVDDYHF MSAGLSKEEL YWPYYTEDGG EVIAVFPIDE
     KLRYLIPFRP VDKVLEYLHS LIDGDESKVA VFHDDGEKFG IWPGTYEWVY EKGWLREFFD
     RISSDEKINL MLYTEYLEKY KPRGLVYLPI ASYFEMSEWS LPAKQARLFV EFVNELKVKG
     IFEKYRVFVR GGIWKNFFYK YPESNYMHKR MLMVSKLVRN NPEARKYLLR AQCNDAYWHG
     LFGGVYLPHL RRAIWNNLIK ANSYVSLGKV IRDIDYDGFE EVLIENDNFY AVFKPSYGGS
     LVEFSSKNRL VNYVDVLARR WEHYHGYVES QFDGVASIHE LEKKIPDEIR KEVAYDKYRR
     FMLQDHVVPL GTTLEDFMFS RQQEIGEFPR VPYSYELLDG GIRLKREHLG IEVEKTVKLV
     NDGFEVEYIV NNKTGNPVLF AVELNVAVQS IMESPGVLRG KEIVVDDKYA VGKFALKFED
     EMEVWKYPVK TLSQSESGWD LIQQGVSYIV PIRLEDKIRF KLKFEEASG