ID THI4_UROFA STANDARD; PRT; 338 AA. AC Q9UVF8; DT 01-OCT-2000 (Rel. 40, Created) DT 01-OCT-2000 (Rel. 40, Last sequence update) DT 01-OCT-2000 (Rel. 40, Last annotation update) DE THIAZOLE BIOSYNTHETIC ENZYME, MITOCHONDRIAL PRECURSOR. GN THI2. OS Uromyces fabae. OC Eukaryota; Fungi; Basidiomycota; Urediniomycetes; Uredinales; OC Pucciniaceae; Uromyces. OX NCBI_TaxID=55588; RN [1] RP SEQUENCE FROM N.A. RA Sohn J.H., Voegele R.T., Mendgen K., Hahn M.; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: INVOLVED IN BIOSYNTHESIS OF THE THIAMINE PRECURSOR CC THIAZOLE (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL (POTENTIAL). CC -!- SIMILARITY: BELONGS TO THE THI4 FAMILY. 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; AJ250427; CAB59856.1; -. DR InterPro; IPR002922; Thi4. DR Pfam; PF01946; Thi4; 1. KW Thiamine biosynthesis; Mitochondrion; Transit peptide; FAD; NAD. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 338 THIAZOLE BIOSYNTHETIC ENZYME. FT NP_BIND 82 112 FAD OR NAD (POTENTIAL). SQ SEQUENCE 338 AA; 36213 MW; C3F9611094861230 CRC64; MSPVATESMY KPTTINQTAH QQAMDPLKSK QQSNATVNKP AFKPEPAVNL TPIKFAPIKE HQVQRAMVRR YFQDMEERAI SDVIIVGAGS AGLSCAYALG TARPDLKITI LESNVAPGGG CWLGGQLMSA MVCRKPADEF LDQVGVPYED EGNFVVVKHA ALFTSTVLSK VLAMPNVKMF NATACEDLII KPCPINPGVQ RIAGCVTNWT LVSLNHDHQS CMDPSTITAP LVCSFAGHDG PFGAFCVKRV ASAGLSEGLG DMRPLDMERA EDHIANKTRE ILPGLIVGGM ELSEFDGSAR MGPTFGAMLL SGKRAAEVAL QSLDRVKIEE GEVVGLAK //