ID A2GAK8_TRIV3 Unreviewed; 607 AA. AC A2GAK8; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 82. 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=TVAG_537410 {ECO:0000313|EMBL:EAX85812.1}; OS Trichomonas vaginalis (strain ATCC PRA-98 / G3). OC Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae; OC Trichomonas. OX NCBI_TaxID=412133 {ECO:0000313|EMBL:EAX85812.1, ECO:0000313|Proteomes:UP000001542}; RN [1] {ECO:0000313|EMBL:EAX85812.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=G3 {ECO:0000313|EMBL:EAX85812.1}; RA Amadeo P., Zhao Q., Wortman J., Fraser-Liggett C., Carlton J.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:EAX85812.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G3 {ECO:0000313|EMBL:EAX85812.1}; RX PubMed=17218520; DOI=10.1126/science.1132894; RA Carlton J.M., Hirt R.P., Silva J.C., Delcher A.L., Schatz M., Zhao Q., RA Wortman J.R., Bidwell S.L., Alsmark U.C.M., Besteiro S., RA Sicheritz-Ponten T., Noel C.J., Dacks J.B., Foster P.G., Simillion C., RA Van de Peer Y., Miranda-Saavedra D., Barton G.J., Westrop G.D., Mueller S., RA Dessi D., Fiori P.L., Ren Q., Paulsen I., Zhang H., Bastida-Corcuera F.D., RA Simoes-Barbosa A., Brown M.T., Hayes R.D., Mukherjee M., Okumura C.Y., RA Schneider R., Smith A.J., Vanacova S., Villalvazo M., Haas B.J., Pertea M., RA Feldblyum T.V., Utterback T.R., Shu C.L., Osoegawa K., de Jong P.J., RA Hrdy I., Horvathova L., Zubacova Z., Dolezal P., Malik S.B., RA Logsdon J.M. Jr., Henze K., Gupta A., Wang C.C., Dunne R.L., Upcroft J.A., RA Upcroft P., White O., Salzberg S.L., Tang P., Chiu C.-H., Lee Y.-S., RA Embley T.M., Coombs G.H., Mottram J.C., Tachezy J., Fraser-Liggett C.M., RA Johnson P.J.; RT "Draft genome sequence of the sexually transmitted pathogen Trichomonas RT vaginalis."; RL Science 315:207-212(2007). 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; DS114826; EAX85812.1; -; Genomic_DNA. DR RefSeq; XP_001298742.1; XM_001298741.1. DR AlphaFoldDB; A2GAK8; -. DR STRING; 5722.A2GAK8; -. DR GeneID; 4743455; -. DR KEGG; tva:TVAG_2v0790270; -. DR VEuPathDB; TrichDB:TVAG_537410; -. DR VEuPathDB; TrichDB:TVAGG3_0790270; -. DR eggNOG; KOG2212; Eukaryota. DR InParanoid; A2GAK8; -. DR OMA; RTHRDIQ; -. DR Proteomes; UP000001542; Unassembled WGS sequence. DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0043169; F:cation binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR006046; Alpha_amylase. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. 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 PRINTS; PR00110; ALPHAAMYLASE. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134}; KW Reference proteome {ECO:0000313|Proteomes:UP000001542}. FT DOMAIN 161..605 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" FT REGION 463..493 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 471..488 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 607 AA; 67968 MW; 50CCA42F30793DE2 CRC64; MLISFAVNGR FGAANQYDPL PNCNIHPQMS CAGSSGDIDP KWFGNLWNTP KRGKENWKPG FQDMSDLTGY AQLKYASGRQ SCTVNIITKT SKDLDLTFYF DGVAQKTNSK TFDSSFNKLL KVKVVAATGE SLILDDIDFV RNVAPLGQRS NDQRYRNGQK GAIIELFGWP DADIEQECKF IADAGYLGVK VFPHQEQVMS SQTFEKELNP WYFMYQPVSY RLQGRMGTRD QLRNMINTCR RYGVRVYADA VVNHMTGNGN DLSNHRNPSA GCTKWGNKTS SAYELGSPYY TPAYTYETNP NTGRGTNVLE FPAVPYGPED FHCDKALGSW SDPNILNTGW LSGLSDLDTS KDYVRQRIAD FMIDLISIGF SGYRIDAAKH IHPKDLAAIF GKVKQGLGGS LPDDFISWLE VLTGGEAYLL VQGDGDYSFT GGLTKFLKQN GLNDDEILKI KIWWCGYPTE PGNDNGSIDP HRKVIQNDDH DQQNDGSSSR DMHDAGCVLV KGCDPAKHRE YEKRLFKNPA GFESNNKDAA PIRLVLSSYY WGDNNVHSIP DGESDCKKCT LSCESCHTRE YIKAYNPSAT SYPGGKGYTY VHRDSEIIQE MNNWMNL //