AMY_ORYLA
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 03-AUG-2022, entry version 75.
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; ENSORLP00000024837; ENSORLG00000020006.
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; 665362at2759; -.
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 tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1180; -; 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 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; SSF51445; 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
