ID C7ZH60_FUSV7 Unreviewed; 459 AA. AC C7ZH60; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAR-2024, entry version 80. 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=NECHADRAFT_51674 {ECO:0000313|EMBL:EEU36582.1}; OS Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL OS 45880 / 77-13-4) (Fusarium solani subsp. pisi). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium; OC Fusarium solani species complex; Fusarium vanettenii. OX NCBI_TaxID=660122 {ECO:0000313|EMBL:EEU36582.1, ECO:0000313|Proteomes:UP000005206}; RN [1] {ECO:0000313|EMBL:EEU36582.1, ECO:0000313|Proteomes:UP000005206} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4 RC {ECO:0000313|Proteomes:UP000005206}; RX PubMed=19714214; DOI=10.1371/journal.pgen.1000618; RA Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C., RA Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C., RA Freitag M., Ma L.J., Danchin E.G., Henrissat B., Coutinho P.M., RA Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M., RA Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L., RA Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E., RA Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E., RA Vanetten H.D.; RT "The genome of Nectria haematococca: contribution of supernumerary RT chromosomes to gene expansion."; RL PLoS Genet. 5:E1000618-E1000618(2009). 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; GG698927; EEU36582.1; -; Genomic_DNA. DR RefSeq; XP_003042295.1; XM_003042249.1. DR AlphaFoldDB; C7ZH60; -. DR STRING; 660122.C7ZH60; -. DR EnsemblFungi; NechaT51674; NechaP51674; NechaG51674. DR GeneID; 9669783; -. DR KEGG; nhe:NECHADRAFT_51674; -. DR VEuPathDB; FungiDB:NECHADRAFT_51674; -. DR eggNOG; KOG0471; Eukaryota. DR HOGENOM; CLU_006462_7_2_1; -. DR InParanoid; C7ZH60; -. DR OMA; IWWQVYP; -. DR OrthoDB; 3249969at2759; -. DR Proteomes; UP000005206; 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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. 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; 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; 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:UP000005206}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..20 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 21..459 FT /note="Alpha-amylase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002987100" FT DOMAIN 33..371 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" FT ACT_SITE 209 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-1" FT ACT_SITE 233 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-1" FT BINDING 96 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5" FT BINDING 134 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3" FT BINDING 135 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5" FT BINDING 169 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3" FT BINDING 178 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3" FT BINDING 207 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5" FT BINDING 209 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3" FT BINDING 213 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3" FT BINDING 233 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3" FT BINDING 237 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5" FT BINDING 299 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5" FT BINDING 346 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5" FT SITE 299 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR001024-2" FT DISULFID 50..57 FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4" FT DISULFID 158..171 FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4" SQ SEQUENCE 459 AA; 50513 MW; 760D313E929AF4AE CRC64; MKPLYALAAV FASICPTALA ADAAAWKSRN IYFVLTDRIA RSSTDNGGAC SDLGSYCGGT FKGLESKLDY IRGMGFDAIW ITPVVSNTPN GYHGYWADDL YAINSKYGTA EDLKSLVSSA HQKGIYVMVD VVANHMGPNI GGHKPEPLNQ QSSYHSGCEI NYSDQTSIEV CSIAGLPDVK TENSEIRTLY QNWIKWLVKE YQFDGIRIDT VKHVEKDFWP GFQSAAGVYS IGEVFDGNPN YLAGYASVMP GLLNYAIYYP MNRFYQQQGS SQDLVNMHDE ISAKFSDPTV LGTFLDNHDN ARWLNRKNDV SLLKNALAHV ILARGIPIVY YGTEQGYAGG NDPANREDLW RSGFSTNADL YQAISRLSNA RSKAGGLGGN DHKHLFVENN VYAWSRAGGD LVVLTTNRGQ GWSGQYCFFT QKPNKSWNNV FGQGSYTSDN DGRVCVNVTN GEPVVLLAS //