ID A1CWV2_NEOFI Unreviewed; 422 AA. AC A1CWV2; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 100. DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134}; DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134}; GN ORFNames=NFIA_105920 {ECO:0000313|EMBL:EAW25104.1}; OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW25104.1, ECO:0000313|Proteomes:UP000006702}; RN [1] {ECO:0000313|Proteomes:UP000006702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702}; RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046; RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M., RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.; RT "Genomic islands in the pathogenic filamentous fungus Aspergillus RT fumigatus."; RL PLoS Genet. 4:E1000046-E1000046(2008). 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:0000256|ARBA:ARBA00000548, CC ECO:0000256|RuleBase:RU361134}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|ARBA:ARBA00001913}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}. 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 EMBL; DS027685; EAW25104.1; -; Genomic_DNA. DR RefSeq; XP_001267001.1; XM_001267000.1. DR AlphaFoldDB; A1CWV2; -. DR STRING; 331117.A1CWV2; -. DR EnsemblFungi; EAW25104; EAW25104; NFIA_105920. DR GeneID; 4593921; -. DR KEGG; nfi:NFIA_105920; -. DR VEuPathDB; FungiDB:NFIA_105920; -. DR eggNOG; KOG0471; Eukaryota. DR HOGENOM; CLU_006462_7_2_1; -. DR OMA; AHNWLFT; -. DR OrthoDB; 3249969at2759; -. DR Proteomes; UP000006702; Unassembled WGS sequence. DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule. 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; 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; PTHR10357:SF212; ALPHA-AMYLASE; 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 PRINTS; PR00110; ALPHAAMYLASE. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|PIRSR:PIRSR001024-3}; KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134}; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR001024-4}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001024-3}; KW Reference proteome {ECO:0000313|Proteomes:UP000006702}. FT DOMAIN 1..315 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" FT ACT_SITE 152 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-1" FT ACT_SITE 176 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-1" FT BINDING 29 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5" FT BINDING 67 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3" FT BINDING 68 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5" FT BINDING 108 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3" FT BINDING 121 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3" FT BINDING 150 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5" FT BINDING 152 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3" FT BINDING 156 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3" FT BINDING 176 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3" FT BINDING 180 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5" FT BINDING 243 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5" FT BINDING 290 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5" FT SITE 243 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-2" FT DISULFID 96..110 FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4" FT DISULFID 186..229 FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4" FT DISULFID 386..421 FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4" SQ SEQUENCE 422 AA; 45982 MW; 46BE39CF05067B0E CRC64; MGFTAIWITP VTEQLPQDTS EGTAYHGYWQ QDIYSVNSNY GTADDLKALA SALHDRGMYL MVDVVANHMG YAGAGDSVDY SVFKPFNSQA YFHPLCFISN YDNQKDVEDC WLGDNVVPLP DLNTTNSDVQ KIWYNWVTSL VSNYSIDGLR IDTVKHVQND FWPGFNDAAG VYCIGEVFDG DPAYTCPYQE VLDGVLNYPI YYPLLKAFQS TSGSMSGLYD MINTVKSQCA DSTLLGTFVE NHDTPRFASY TNDMALAKNA AAFIILSDGI PIIYAGQEQH YSGGTDPANR EAVWLSGYSK TSELYKLIAT ANAIRNHAIS KDPGYMTYKN NPIYKDTSTI AMRKGSDGAQ VITVLSNLGA SGSSYTLSLS GTGYEAGQQL TEVFSCTTVT VGSDGKVPVP MASGLPRVFY PTAGLDGSTI CT //