ID   AMYA_PYRAB              Reviewed;         655 AA.
AC   Q9V298; G8ZG11;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Alpha-amylase;
DE            EC=3.2.1.1;
GN   Name=amyA; OrderedLocusNames=PYRAB01760; ORFNames=PAB0118;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 57 family. {ECO:0000305}.
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DR   EMBL; AJ248283; CAB49100.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69552.1; -; Genomic_DNA.
DR   PIR; E75206; E75206.
DR   RefSeq; WP_010867300.1; NC_000868.1.
DR   AlphaFoldDB; Q9V298; -.
DR   SMR; Q9V298; -.
DR   STRING; 272844.PAB0118; -.
DR   CAZy; GH57; Glycoside Hydrolase Family 57.
DR   EnsemblBacteria; CAB49100; CAB49100; PAB0118.
DR   GeneID; 1495063; -.
DR   KEGG; pab:PAB0118; -.
DR   PATRIC; fig|272844.11.peg.190; -.
DR   eggNOG; arCOG03280; Archaea.
DR   HOGENOM; CLU_026700_0_0_2; -.
DR   OMA; HFMSAGL; -.
DR   OrthoDB; 3280at2157; -.
DR   PhylomeDB; Q9V298; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase.
FT   CHAIN           1..655
FT                   /note="Alpha-amylase"
FT                   /id="PRO_0000184572"
FT   ACT_SITE        123
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        214
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   655 AA;  77296 MW;  7F6F920B1A00EECE CRC64;
     MPRINFIFGI HNHQPLGNFG WVMEEAYEKA YRPFLEILEE YPNMKVAIHI SGILVEWLEE
     NKPDYIDLLK SLVRKGQVEI VVAGFYEPVL AAIPKEDRLE QIYLLKEWAK KIGYDAKGLW
     LTERVWQPEL VKTLREAGIE YVVVDDYHFM SAGLSKDQLF WPYYTEDGGE VITVFPIDEK
     LRYLIPFRPV DKVISYLHSL ASEDESKVAV FHDDGEKFGI WPMTYEWVYE KGWLREFFDR
     VSSDEAINIM LYSEYLQKFK PKGLVYLPIA SYFEMSEWSL PAQQAKLFVE FVEKLKELNM
     FERYRVFVRG GIWKNFFYKY PEANYMHKRM LMLSRLLRDN PSARRFVLRA QCNDAYWHGV
     FGGIYLPHLR RAIWSNLIKA HSHLEPKNKI LDVDFDGREE VFLENDNFII VVKPHYGGSI
     FELSSKRRAV NYADVIARRW EHYHNLGESE SDDNENQEGV SSIHEIGKRI PEDIRKELAY
     DRYRRGILQD HFFSANETLD RYRLAKYWEL GDFIEGVYNY EVGNGLVLWR RGKVLNVTVD
     VKKSIEVRED GFSVRYTVLS EEDIEALFGI ELNIAVHSIK ESPEELIGKR IKVNDKYGVG
     EFEIVLNKKA RIWKYPVKTL SQSEAGWDYI QQGVSYTIIY PINGRLDIEL YFREL