ID A0A1E1FB83_9AGAM Unreviewed; 71 AA. AC A0A1E1FB83; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 24-JAN-2024, entry version 12. DE SubName: Full=Ilv2 protein {ECO:0000313|EMBL:BAV67762.1}; DE Flags: Fragment; GN Name=Ilv2 {ECO:0000313|EMBL:BAV67762.1}; OS Strobilomyces aff. strobilaceus L23-s438. OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC Agaricomycetidae; Boletales; Boletineae; Boletaceae; Boletoideae; OC Strobilomyces. OX NCBI_TaxID=1712139 {ECO:0000313|EMBL:BAV67762.1}; RN [1] {ECO:0000313|EMBL:BAV67762.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=L23-s438 {ECO:0000313|EMBL:BAV67762.1}; RC TISSUE=Fruit body {ECO:0000313|EMBL:BAV67762.1}; RA Sato H., Tanabe S.A., Toju H.; RT "Host shifts enhance diversification of ectomycorrhizal fungi: RT diversification rate analysis of the ectomycorrhizal fungal genera RT Strobilomyces and Afroboletus with 80-gene phylogeny."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- SIMILARITY: Belongs to the TPP enzyme family. CC {ECO:0000256|ARBA:ARBA00007812}. 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; LC083102; BAV67762.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1E1FB83; -. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR000399; TPP-bd_CS. DR InterPro; IPR045229; TPP_enz. DR InterPro; IPR011766; TPP_enzyme_TPP-bd. DR PANTHER; PTHR18968:SF169; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 1. DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1. DR Pfam; PF02775; TPP_enzyme_C; 1. DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1. DR PROSITE; PS00187; TPP_ENZYMES; 1. PE 3: Inferred from homology; FT DOMAIN 1..71 FT /note="Thiamine pyrophosphate enzyme TPP-binding" FT /evidence="ECO:0000259|Pfam:PF02775" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:BAV67762.1" FT NON_TER 71 FT /evidence="ECO:0000313|EMBL:BAV67762.1" SQ SEQUENCE 71 AA; 7391 MW; D2FB0E490C2DD09F CRC64; AQHYRWRTPR SMVTSGGLGT MGFGLPAAIG AKVAAPHKTV VDIDGDASFS MTAMELATAA QFDIGVKVLV L //