ID AMYA_ASPNG Reviewed; 484 AA. AC P56271; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 27-MAR-2024, entry version 114. DE RecName: Full=Acid alpha-amylase; DE EC=3.2.1.1 {ECO:0000269|PubMed:2207069}; DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase; OS Aspergillus niger. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=5061; RN [1] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, RP CATALYTIC ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION, AND DISULFIDE BONDS. RX PubMed=2207069; DOI=10.1021/bi00478a019; RA Boel E., Brady L., Brzozowski A.M., Derewenda Z., Dodson G.G., Jensen V.J., RA Petersen S.B., Swift H., Thim L., Woldike H.F.; RT "Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A RT resolution of two enzymes from Aspergillus."; RL Biochemistry 29:6244-6249(1990). 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:2207069}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000269|PubMed:2207069}; CC Note=Binds 2 calcium ions per subunit. Calcium is inhibitory at high CC concentrations. {ECO:0000269|PubMed:2207069}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:2207069}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2207069}. 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; A35282; A35282. DR PDB; 2AAA; X-ray; 2.10 A; A=1-484. DR PDBsum; 2AAA; -. DR AlphaFoldDB; P56271; -. DR SMR; P56271; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR PaxDb; 5061-CADANGAP00008517; -. DR VEuPathDB; FungiDB:An11g03340; -. DR VEuPathDB; FungiDB:ASPNIDRAFT2_1147022; -. DR VEuPathDB; FungiDB:ATCC64974_89550; -. DR VEuPathDB; FungiDB:M747DRAFT_340768; -. DR eggNOG; KOG0471; Eukaryota. DR EvolutionaryTrace; P56271; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro. DR CDD; cd11319; AmyAc_euk_AmyA; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR InterPro; IPR013777; A-amylase-like. DR InterPro; IPR015340; A_amylase_C_dom. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1. DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1. DR Pfam; PF09260; A_amylase_dom_C; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR PIRSF; PIRSF001024; Alph-amyl_fung; 1. 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; Calcium; Carbohydrate metabolism; Disulfide bond; KW Glycoprotein; Glycosidase; Hydrolase; Metal-binding; Secreted. FT CHAIN 1..484 FT /note="Acid alpha-amylase" FT /id="PRO_0000054289" FT ACT_SITE 206 FT /note="Nucleophile" FT /evidence="ECO:0000269|PubMed:2207069" FT ACT_SITE 230 FT /note="Proton donor" FT /evidence="ECO:0000269|PubMed:2207069" FT BINDING 83 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0C1B3" FT BINDING 121 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:2207069, FT ECO:0007744|PDB:2AAA" FT BINDING 122 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0C1B3" FT BINDING 162 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:2207069, FT ECO:0007744|PDB:2AAA" FT BINDING 175 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:2207069, FT ECO:0007744|PDB:2AAA" FT BINDING 204 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0C1B3" FT BINDING 206 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:2207069, FT ECO:0007744|PDB:2AAA" FT BINDING 209..210 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0C1B3" FT BINDING 210 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:2207069, FT ECO:0007744|PDB:2AAA" FT BINDING 230 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:2207069, FT ECO:0007744|PDB:2AAA" FT BINDING 234 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0C1B3" FT BINDING 297 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0C1B3" FT BINDING 344 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0C1B3" FT SITE 297 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250|UniProtKB:P0C1B3" FT CARBOHYD 24 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 157 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 197 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 30..38 FT /evidence="ECO:0000269|PubMed:2207069, FT ECO:0007744|PDB:2AAA" FT DISULFID 150..164 FT /evidence="ECO:0000269|PubMed:2207069, FT ECO:0007744|PDB:2AAA" FT DISULFID 240..283 FT /evidence="ECO:0000269|PubMed:2207069, FT ECO:0007744|PDB:2AAA" FT DISULFID 440..475 FT /evidence="ECO:0000269|PubMed:2207069, FT ECO:0007744|PDB:2AAA" FT HELIX 3..6 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 11..13 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 16..19 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 32..34 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 42..47 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 49..53 FT /evidence="ECO:0007829|PDB:2AAA" FT TURN 54..56 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 59..62 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 66..68 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 83..90 FT /evidence="ECO:0007829|PDB:2AAA" FT TURN 92..94 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 97..108 FT /evidence="ECO:0007829|PDB:2AAA" FT TURN 109..111 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 113..118 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 125..127 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 129..131 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 134..136 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 143..145 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 158..163 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 164..167 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 169..173 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 181..198 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 202..206 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 213..215 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 216..223 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 225..229 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 236..239 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 240..244 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 246..250 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 252..262 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 269..282 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 286..288 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 289..291 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 301..303 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 308..320 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 321..328 FT /evidence="ECO:0007829|PDB:2AAA" FT TURN 329..334 FT /evidence="ECO:0007829|PDB:2AAA" FT TURN 339..343 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 347..350 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 357..375 FT /evidence="ECO:0007829|PDB:2AAA" FT TURN 377..381 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 385..390 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 393..400 FT /evidence="ECO:0007829|PDB:2AAA" FT TURN 401..403 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 405..410 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 419..423 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 433..436 FT /evidence="ECO:0007829|PDB:2AAA" FT TURN 437..440 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 441..444 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 451..455 FT /evidence="ECO:0007829|PDB:2AAA" FT STRAND 461..465 FT /evidence="ECO:0007829|PDB:2AAA" FT HELIX 466..469 FT /evidence="ECO:0007829|PDB:2AAA" SQ SEQUENCE 484 AA; 52935 MW; 04D596E34680656D CRC64; LSAASWRTQS IYFLLTDRFG RTDNSTTATC NTGNEIYCGG SWQGIIDHLD YIEGMGFTAI WISPITEQLP QDTADGEAYH GYWQQKIYDV NSNFGTADNL KSLSDALHAR GMYLMVDVVP DHMGYAGNGN DVDYSVFDPF DSSSYFHPYC LITDWDNLTM VEDCWEGDTI VSLPDLDTTE TAVRTIWYDW VADLVSNYSV DGLRIDSVLE VQPDFFPGYN KASGVYCVGE IDNGNPASDC PYQKVLDGVL NYPIYWQLLY AFESSSGSIS NLYNMIKSVA SDCSDPTLLG NFIENHDNPR FAKYTSDYSQ AKNVLSYIFL SDGIPIVYAG EEQHYAGGKV PYNREATWLS GYDTSAELYT WIATTNAIRK LAIAADSAYI TYANDAFYTD SNTIAMAKGT SGSQVITVLS NKGSSGSSYT LTLSGSGYTS GTKLIEAYTC TSVTVDSSGD IPVPMASGLP RVLLPASVVD SSSLCGGSGR LYVE //