ID Q7LYT7_PYRWO Unreviewed; 460 AA. AC Q7LYT7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 79. DE SubName: Full=Alpha amylase {ECO:0000313|EMBL:AAD54338.1}; DE EC=3.2.1.1 {ECO:0000313|EMBL:AAD54338.1}; GN Name=amyA {ECO:0000313|EMBL:AAD54338.1}; OS Pyrococcus woesei. OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=2262 {ECO:0000313|EMBL:AAD54338.1}; RN [1] {ECO:0000313|EMBL:AAD54338.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM3773 {ECO:0000313|EMBL:AAD54338.1}; RA Chunlin Lu, Weizheng J., Yunyan Y.; RT "Cloning and Expression of Alpha Amylase from Pyrococcus woesei."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD} RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 26-460 IN COMPLEX WITH CALCIUM; RP GLUCOSE; MAGNESIUM AND ZINC, AND DISULFIDE BONDS. RX PubMed=12482867; DOI=10.1074/jbc.M211339200; RA Linden A., Mayans O., Meyer-Klaucke W., Antranikian G., Wilmanns M.; RT "Differential regulation of a hyperthermophilic alpha-amylase with a novel RT (Ca,Zn) two-metal center by zinc."; RL J. Biol. Chem. 278:9875-9884(2003). CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|ARBA:ARBA00001913}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. CC {ECO:0000256|ARBA:ARBA00008061}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF177906; AAD54338.1; -; Genomic_DNA. DR PDB; 1MWO; X-ray; 2.20 A; A=26-460. DR PDB; 1MXD; X-ray; 2.00 A; A=26-460. DR PDB; 1MXG; X-ray; 1.60 A; A=26-460. DR PDBsum; 1MWO; -. DR PDBsum; 1MXD; -. DR PDBsum; 1MXG; -. DR AlphaFoldDB; Q7LYT7; -. DR SMR; Q7LYT7; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd11314; AmyAc_arch_bac_plant_AmyA; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR InterPro; IPR013776; A-amylase_thermo. DR InterPro; IPR015237; Alpha-amylase_C_pro. 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 PANTHER; PTHR43447; ALPHA-AMYLASE; 1. DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1. DR Pfam; PF09154; Alpha-amy_C_pro; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR PIRSF; PIRSF001021; Alph-amls_thrmst; 1. DR PRINTS; PR00110; ALPHAAMYLASE. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD}; KW Calcium {ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:AAD54338.1}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AAD54338.1}; KW Metal-binding {ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD}; KW Zinc {ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD}. FT DOMAIN 35..380 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" FT BINDING 49 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1MXG" FT BINDING 58 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1MWO" FT BINDING 61 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1MXD" FT BINDING 61 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1MWO" FT BINDING 105 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1MXG" FT BINDING 105 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD" FT BINDING 113 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1MXG" FT BINDING 113 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD" FT BINDING 135 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0007829|PDB:1MXG" FT BINDING 172 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD" FT BINDING 177 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD" FT BINDING 180 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD" FT BINDING 182 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD" FT BINDING 189 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD" FT BINDING 191 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD" FT BINDING 223 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD" FT BINDING 227 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD" FT BINDING 247 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD" FT BINDING 277 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1MXG" FT BINDING 277 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD" FT BINDING 281 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1MXG" FT BINDING 281 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD" FT BINDING 314 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD" FT BINDING 317 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1MXG" FT BINDING 317 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD" FT BINDING 343 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1MXD" FT BINDING 343 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1MWO" FT BINDING 348 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1MXD" FT BINDING 372 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:1MXG" FT BINDING 372 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="7" FT /evidence="ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD" FT BINDING 374 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:1MXG" FT BINDING 374 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="7" FT /evidence="ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD" FT BINDING 375 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:1MXG" FT BINDING 375 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="7" FT /evidence="ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD" FT CARBOHYD 316 FT /note="Glucose" FT /evidence="ECO:0007829|PDB:1MXD" FT CARBOHYD 321 FT /note="Glucose" FT /evidence="ECO:0007829|PDB:1MXD" FT DISULFID 178..179 FT /evidence="ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD" FT DISULFID 413..457 FT /evidence="ECO:0007829|PDB:1MWO, ECO:0007829|PDB:1MXD" SQ SEQUENCE 460 AA; 52910 MW; 0E0A2AEB5FCAF541 CRC64; MNIKKLTPLL TLLLFFIVLA SPVSAAKYLE LEEGGVIMQA FYWDVPGGGI WWDHIRSKIP EWYEAGISAI WLPPPSKGMS GGYSMGYDPY DYFDLGEYYQ KGTVETRFGS KEELVRLIQT AHAYGIKVIA DVVINHRAGG DLEWNPFVGD YTWTDFSKVA SGKYTANYLD FHPNELHCCD EGTFGGFPDI CHHKEWDQYW LWKSNESYAA YLRSIGFDGW RFDYVKGYGA WVVRDWLNWW GGWAVGEYWD TNVDALLSWA YESGAKVFDF PLYYKMDEAF DNNNIPALVY ALQNGQTVVS RDPFKAVTFV ANHDTDIIWN KYPAYAFILT YEGQPVIFYR DFEEWLNKDK LINLIWIHDH LAGGSTTIVY YDNDELIFVR NGDSRRPGLI TYINLSPNWV GRWVYVPKFA GACIHEYTGN LGGWVDKRVD SSGWVYLEAP PHDPANGYYG YSVWSYCGVG //