ID AMY_TENMO Reviewed; 471 AA. AC P56634; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 1. DT 22-FEB-2023, entry version 123. DE RecName: Full=Alpha-amylase; DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P04746}; DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase; OS Tenebrio molitor (Yellow mealworm beetle). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia; OC Tenebrionidae; Tenebrio. OX NCBI_TaxID=7067; RN [1] RP PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1. RX PubMed=9199514; DOI=10.1016/s0014-5793(97)00451-1; RA Strobl S., Gomis-Rueth F.-X., Maskos K., Frank G., Huber R., RA Glockshuber R.; RT "The alpha-amylase from the yellow meal worm: complete primary structure, RT crystallization and preliminary X-ray analysis."; RL FEBS Lett. 409:109-114(1997). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-471 IN COMPLEX WITH CALCIUM AND RP CHLORIDE, COFACTOR, SUBUNIT, AND DISULFIDE BONDS. RX PubMed=9600843; DOI=10.1006/jmbi.1998.1667; RA Strobl S., Maskos K., Betz M., Wiegand G., Huber R., Gomis-Rueth F.-X., RA Glockshuber R.; RT "Crystal structure of yellow meal worm alpha-amylase at 1.64-A RT resolution."; RL J. Mol. Biol. 278:617-628(1998). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH CALCIUM AND RP CHLORIDE, DISULFIDE BONDS, COFACTOR, AND PYROGLUTAMATE FORMATION AT GLN-1. RX PubMed=9687373; DOI=10.1016/s0969-2126(98)00092-6; RA Strobl S., Maskos K., Wiegand G., Huber R., Gomis-Rueth F.-X., RA Glockshuber R.; RT "A novel strategy for inhibition of alpha-amylases: yellow meal worm alpha- RT amylase in complex with the Ragi bifunctional inhibitor at 2.5-A RT resolution."; RL Structure 6:911-921(1998). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH CALCIUM AND RP CHLORIDE, DISULFIDE BONDS, AND COFACTOR. RX PubMed=10508777; DOI=10.1016/s0969-2126(99)80175-0; RA Pereira P.J., Lozanov V., Patthy A., Huber R., Bode W., Pongor S., RA Strobl S.; RT "Specific inhibition of insect alpha-amylases: yellow meal worm alpha- RT amylase in complex with the amaranth alpha-amylase inhibitor at 2.0 A RT resolution."; RL Structure 7:1079-1088(1999). 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:0000250|UniProtKB:P04746}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000269|PubMed:10508777, ECO:0000269|PubMed:9600843, CC ECO:0000269|PubMed:9687373, ECO:0007744|PDB:1JAE}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:10508777, CC ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, CC ECO:0007744|PDB:1JAE}; CC -!- COFACTOR: CC Name=chloride; Xref=ChEBI:CHEBI:17996; CC Evidence={ECO:0000269|PubMed:10508777, ECO:0000269|PubMed:9600843, CC ECO:0000269|PubMed:9687373, ECO:0007744|PDB:1JAE}; CC Note=Binds 1 Cl(-) ion per subunit. {ECO:0000269|PubMed:10508777, CC ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, CC ECO:0007744|PDB:1JAE}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9600843}. 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 PIR; S75702; S75702. DR PDB; 1CLV; X-ray; 2.00 A; A=1-471. DR PDB; 1JAE; X-ray; 1.65 A; A=2-471. DR PDB; 1TMQ; X-ray; 2.50 A; A=1-471. DR PDB; 1VIW; X-ray; 3.00 A; A=2-471. DR PDBsum; 1CLV; -. DR PDBsum; 1JAE; -. DR PDBsum; 1TMQ; -. DR PDBsum; 1VIW; -. DR AlphaFoldDB; P56634; -. DR SMR; P56634; -. DR MINT; P56634; -. DR BindingDB; P56634; -. DR ChEMBL; CHEMBL3580521; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR EvolutionaryTrace; P56634; -. DR GO; GO:0004556; F:alpha-amylase activity; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB. DR GO; GO:0031404; F:chloride ion binding; IDA:UniProtKB. DR GO; GO:0016052; P:carbohydrate catabolic process; ISS:UniProtKB. 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; KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase; KW Metal-binding; Pyrrolidone carboxylic acid. FT CHAIN 1..471 FT /note="Alpha-amylase" FT /id="PRO_0000054290" FT REGION 326..346 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 185 FT /note="Nucleophile" FT /evidence="ECO:0000305|PubMed:9600843" FT ACT_SITE 222 FT /note="Proton donor" FT /evidence="ECO:0000305|PubMed:9600843" FT BINDING 98 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:10508777, FT ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, FT ECO:0007744|PDB:1JAE" FT BINDING 146 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:10508777, FT ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, FT ECO:0007744|PDB:1JAE" FT BINDING 155 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:10508777, FT ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, FT ECO:0007744|PDB:1JAE" FT BINDING 183 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /evidence="ECO:0000269|PubMed:10508777, FT ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, FT ECO:0007744|PDB:1JAE" FT BINDING 189 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:10508777, FT ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, FT ECO:0007744|PDB:1JAE" FT BINDING 285 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /evidence="ECO:0000269|PubMed:10508777, FT ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, FT ECO:0007744|PDB:1JAE" FT BINDING 321 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /evidence="ECO:0000269|PubMed:10508777, FT ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, FT ECO:0007744|PDB:1JAE" FT SITE 287 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250|UniProtKB:P04746" FT MOD_RES 1 FT /note="Pyrrolidone carboxylic acid" FT /evidence="ECO:0000269|PubMed:9199514, FT ECO:0000269|PubMed:9687373" FT DISULFID 28..84 FT /evidence="ECO:0000269|PubMed:10508777, FT ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, FT ECO:0007744|PDB:1JAE" FT DISULFID 134..148 FT /evidence="ECO:0000269|PubMed:10508777, FT ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, FT ECO:0007744|PDB:1JAE" FT DISULFID 354..360 FT /evidence="ECO:0000269|PubMed:10508777, FT ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, FT ECO:0007744|PDB:1JAE" FT DISULFID 425..437 FT /evidence="ECO:0000269|PubMed:10508777, FT ECO:0000269|PubMed:9600843, ECO:0000269|PubMed:9687373, FT ECO:0007744|PDB:1JAE" FT STRAND 11..16 FT /evidence="ECO:0007829|PDB:1JAE" FT HELIX 21..30 FT /evidence="ECO:0007829|PDB:1JAE" FT TURN 31..36 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 37..41 FT /evidence="ECO:0007829|PDB:1JAE" FT HELIX 56..60 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 61..63 FT /evidence="ECO:0007829|PDB:1CLV" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:1JAE" FT HELIX 74..86 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 90..95 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:1JAE" FT TURN 115..118 FT /evidence="ECO:0007829|PDB:1JAE" FT TURN 121..124 FT /evidence="ECO:0007829|PDB:1JAE" FT HELIX 127..129 FT /evidence="ECO:0007829|PDB:1JAE" FT HELIX 142..147 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 148..150 FT /evidence="ECO:0007829|PDB:1JAE" FT HELIX 161..176 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 181..184 FT /evidence="ECO:0007829|PDB:1JAE" FT HELIX 187..189 FT /evidence="ECO:0007829|PDB:1JAE" FT HELIX 192..200 FT /evidence="ECO:0007829|PDB:1JAE" FT HELIX 207..209 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 218..222 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 227..230 FT /evidence="ECO:0007829|PDB:1JAE" FT HELIX 233..235 FT /evidence="ECO:0007829|PDB:1JAE" FT TURN 236..238 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 239..243 FT /evidence="ECO:0007829|PDB:1JAE" FT HELIX 245..255 FT /evidence="ECO:0007829|PDB:1JAE" FT TURN 256..258 FT /evidence="ECO:0007829|PDB:1JAE" FT HELIX 261..266 FT /evidence="ECO:0007829|PDB:1JAE" FT HELIX 269..271 FT /evidence="ECO:0007829|PDB:1JAE" FT HELIX 276..278 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 279..281 FT /evidence="ECO:0007829|PDB:1JAE" FT HELIX 288..291 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 292..296 FT /evidence="ECO:0007829|PDB:1CLV" FT HELIX 302..314 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 317..324 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 329..332 FT /evidence="ECO:0007829|PDB:1CLV" FT STRAND 335..337 FT /evidence="ECO:0007829|PDB:1TMQ" FT STRAND 338..340 FT /evidence="ECO:0007829|PDB:1VIW" FT STRAND 347..349 FT /evidence="ECO:0007829|PDB:1TMQ" FT TURN 350..352 FT /evidence="ECO:0007829|PDB:1TMQ" FT STRAND 353..355 FT /evidence="ECO:0007829|PDB:1TMQ" FT HELIX 361..363 FT /evidence="ECO:0007829|PDB:1JAE" FT HELIX 365..376 FT /evidence="ECO:0007829|PDB:1JAE" FT TURN 377..379 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 382..387 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 389..397 FT /evidence="ECO:0007829|PDB:1JAE" FT TURN 398..400 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 401..409 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 411..416 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 421..425 FT /evidence="ECO:0007829|PDB:1JAE" FT TURN 427..429 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 436..439 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 441..444 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 448..454 FT /evidence="ECO:0007829|PDB:1JAE" FT STRAND 461..466 FT /evidence="ECO:0007829|PDB:1JAE" FT HELIX 467..469 FT /evidence="ECO:0007829|PDB:1CLV" SQ SEQUENCE 471 AA; 51240 MW; 9C3D48933D6C24C8 CRC64; QKDANFASGR NSIVHLFEWK WNDIADECER FLQPQGFGGV QISPPNEYLV ADGRPWWERY QPVSYIINTR SGDESAFTDM TRRCNDAGVR IYVDAVINHM TGMNGVGTSG SSADHDGMNY PAVPYGSGDF HSPCEVNNYQ DADNVRNCEL VGLRDLNQGS DYVRGVLIDY MNHMIDLGVA GFRVDAAKHM SPGDLSVIFS GLKNLNTDYG FADGARPFIY QEVIDLGGEA ISKNEYTGFG CVLEFQFGVS LGNAFQGGNQ LKNLANWGPE WGLLEGLDAV VFVDNHDNQR TGGSQILTYK NPKPYKMAIA FMLAHPYGTT RIMSSFDFTD NDQGPPQDGS GNLISPGIND DNTCSNGYVC EHRWRQVYGM VGFRNAVEGT QVENWWSNDD NQIAFSRGSQ GFVAFTNGGD LNQNLNTGLP AGTYCDVISG ELSGGSCTGK SVTVGDNGSA DISLGSAEDD GVLAIHVNAK L //