ID AMY_ORYLA Reviewed; 512 AA. AC H2N0D4; DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2012, sequence version 1. DT 27-MAR-2024, entry version 81. DE RecName: Full=Alpha-amylase {ECO:0000303|PubMed:22613096}; DE EC=3.2.1.1 {ECO:0000269|PubMed:22613096}; DE Flags: Precursor; OS Oryzias latipes (Japanese rice fish) (Japanese killifish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae; OC Oryzias. OX NCBI_TaxID=8090 {ECO:0000312|Proteomes:UP000001038}; RN [1] {ECO:0000312|Proteomes:UP000001038} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR {ECO:0000312|Proteomes:UP000001038}; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T., RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A., RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S., RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S., RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K., RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome evolution."; RL Nature 447:714-719(2007). RN [2] {ECO:0007744|PDB:3VM5} RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 16-512 IN COMPLEX WITH CALCIUM RP AND CHLORIDE IONS, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, RP BIOPHYSICOCHEMICAL PROPERTIES, AND DISULFIDE BONDS. RX PubMed=22613096; DOI=10.1016/j.bbapap.2012.05.005; RA Mizutani K., Toyoda M., Otake Y., Yoshioka S., Takahashi N., Mikami B.; RT "Structural and functional characterization of recombinant medaka fish RT alpha-amylase expressed in yeast Pichia pastoris."; RL Biochim. Biophys. Acta 1824:954-962(2012). CC -!- FUNCTION: Catalyzes the hydrolysis of alpha-1,4 glycosidic linkages in CC starch, glycogen and similar oligosaccharides. CC {ECO:0000269|PubMed:22613096}. 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; Evidence={ECO:0000269|PubMed:22613096}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000269|PubMed:22613096}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:22613096}; CC -!- COFACTOR: CC Name=chloride; Xref=ChEBI:CHEBI:17996; CC Evidence={ECO:0000269|PubMed:22613096}; CC Note=Binds 1 Cl(-) ion per subunit. {ECO:0000269|PubMed:22613096}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.18 mg/ml for potato amylopectin {ECO:0000269|PubMed:22613096}; CC Vmax=2560 umol/min/mg enzyme {ECO:0000269|PubMed:22613096}; CC pH dependence: CC Optimum pH is 7.1. {ECO:0000269|PubMed:22613096}; CC Temperature dependence: CC Optimum temperature is 50 degrees Celsius. CC {ECO:0000269|PubMed:22613096}; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}. 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 RefSeq; XP_004085115.1; XM_004085067.2. DR PDB; 3VM5; X-ray; 2.85 A; A=16-512. DR PDBsum; 3VM5; -. DR AlphaFoldDB; H2N0D4; -. DR SMR; H2N0D4; -. DR STRING; 8090.ENSORLP00000024837; -. DR Ensembl; ENSORLT00000024838.2; ENSORLP00000024837.1; ENSORLG00000020006.2. DR GeneID; 101163630; -. DR KEGG; ola:101163630; -. DR CTD; 279; -. DR eggNOG; KOG2212; Eukaryota. DR GeneTree; ENSGT00940000163518; -. DR HOGENOM; CLU_013336_2_1_1; -. DR InParanoid; H2N0D4; -. DR OMA; FRYAYDL; -. DR OrthoDB; 3249969at2759; -. DR TreeFam; TF312850; -. DR BRENDA; 3.2.1.1; 3199. DR Proteomes; UP000001038; Chromosome 17. DR Proteomes; UP000265180; Unplaced. DR Proteomes; UP000265200; Unplaced. DR Bgee; ENSORLG00000020006; Expressed in intestine and 12 other cell types or tissues. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central. DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR InterPro; IPR006048; A-amylase/branching_C. DR InterPro; IPR031319; A-amylase_C. 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; PF00128; Alpha-amylase; 1. DR Pfam; PF02806; Alpha-amylase_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. DR SMART; SM00642; Aamy; 1. DR SMART; SM00632; Aamy_C; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Carbohydrate metabolism; Chloride; Disulfide bond; KW Glycoprotein; Glycosidase; Hydrolase; Metal-binding; Reference proteome; KW Secreted; Signal. FT SIGNAL 1..15 FT /evidence="ECO:0000255" FT CHAIN 16..512 FT /note="Alpha-amylase" FT /evidence="ECO:0000255" FT /id="PRO_5012994493" FT ACT_SITE 212 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:P04746" FT ACT_SITE 248 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P04746" FT BINDING 115 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:22613096, FT ECO:0007744|PDB:3VM5" FT BINDING 173 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:22613096, FT ECO:0007744|PDB:3VM5" FT BINDING 182 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:22613096, FT ECO:0007744|PDB:3VM5" FT BINDING 210 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /evidence="ECO:0000269|PubMed:22613096, FT ECO:0007744|PDB:3VM5" FT BINDING 216 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:22613096, FT ECO:0007744|PDB:3VM5" FT BINDING 352 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /evidence="ECO:0000269|PubMed:22613096, FT ECO:0007744|PDB:3VM5" FT SITE 315 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250|UniProtKB:P04746" FT CARBOHYD 496 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT DISULFID 43..101 FT /evidence="ECO:0000269|PubMed:22613096, FT ECO:0007744|PDB:3VM5" FT DISULFID 85..130 FT /evidence="ECO:0000269|PubMed:22613096, FT ECO:0007744|PDB:3VM5" FT DISULFID 156..175 FT /evidence="ECO:0000269|PubMed:22613096, FT ECO:0007744|PDB:3VM5" FT DISULFID 394..400 FT /evidence="ECO:0000269|PubMed:22613096, FT ECO:0007744|PDB:3VM5" FT DISULFID 466..478 FT /evidence="ECO:0000269|PubMed:22613096, FT ECO:0007744|PDB:3VM5" FT STRAND 27..30 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 36..45 FT /evidence="ECO:0007829|PDB:3VM5" FT TURN 46..51 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 54..57 FT /evidence="ECO:0007829|PDB:3VM5" FT TURN 67..70 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 73..77 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 91..103 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 107..112 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 115..119 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:3VM5" FT TURN 136..139 FT /evidence="ECO:0007829|PDB:3VM5" FT TURN 142..145 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 148..150 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 153..155 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 159..162 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 169..174 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 175..177 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 180..183 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 188..204 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 208..211 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 214..216 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 219..226 FT /evidence="ECO:0007829|PDB:3VM5" FT TURN 234..236 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 244..247 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 259..261 FT /evidence="ECO:0007829|PDB:3VM5" FT TURN 262..265 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 266..269 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 271..282 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 284..286 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 289..294 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 297..299 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 304..306 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 307..309 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 316..318 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 324..326 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 333..345 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 348..354 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 363..368 FT /evidence="ECO:0007829|PDB:3VM5" FT TURN 369..372 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 375..377 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 401..403 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 405..417 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 422..427 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 429..437 FT /evidence="ECO:0007829|PDB:3VM5" FT TURN 438..440 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 441..446 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 448..450 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 452..457 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 462..466 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 477..480 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 482..485 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 489..495 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 499..501 FT /evidence="ECO:0007829|PDB:3VM5" FT STRAND 503..507 FT /evidence="ECO:0007829|PDB:3VM5" FT HELIX 508..510 FT /evidence="ECO:0007829|PDB:3VM5" SQ SEQUENCE 512 AA; 57167 MW; FFDA8EFC8F527D02 CRC64; MKLFVLIALF GLGFAQHNPN TRDGRTAIVH LFEWRWADIA AECERFLGPK GFAGVQISPP NEHILVSSPW RPWWQRYQPI SYNLCSRSGG ENELRDMITR CNNVGVNVYV DAVINHMCGA GGGEGTHSSC GSWFNANNKD FPSVPYSNLD FNDGKCKTGS GNIENYGDPY QVRDCRLVGL LDLALEKDYV RGKVADFMNK LIDMGVAGFR VDACKHMWPG DLDNVYRRLN NLNTKWFPGG SRPFIFQEVI DLGGEPITTG EYVGLGRVTE FKYGARLGEL FRKWNGQKLS YTKNWGEGWG FMADGNAVVF TDNHDNQRGH GAGGASILTF WDPRLYKMAV GYMLAHPYGF TRVMSSYSWD RNFVNGKDEN DWIGPPSNGD GSTKPVPINP DQTCGDGWVC EHRWRQIMNM VQFRNVVNGQ PHANWWDNGN NQVAFGRGNR GFIVFNNDDW ALDVTLNTGL PGGTYCDVIS GNKDGGSCTG KQITVGGDGR AHFYINNSEE DPFIAIHADS KL //