AMY_TENMO
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 03-AUG-2022, entry version 120.
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}.
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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 PRIDE; P56634; -.
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 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;
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
