ID Q39P46_BURL3 Unreviewed; 564 AA. AC Q39P46; DT 22-NOV-2005, integrated into UniProtKB/TrEMBL. DT 22-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 88. DE SubName: Full=Acetolactate synthase, large subunit {ECO:0000313|EMBL:ABB05770.1}; DE EC=2.2.1.6 {ECO:0000313|EMBL:ABB05770.1}; GN OrderedLocusNames=Bcep18194_C6721 {ECO:0000313|EMBL:ABB05770.1}; OS Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / OS R18194 / 383). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=482957 {ECO:0000313|EMBL:ABB05770.1, ECO:0000313|Proteomes:UP000002705}; RN [1] {ECO:0000313|Proteomes:UP000002705} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383 RC {ECO:0000313|Proteomes:UP000002705}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., RA Richardson P.; RT "Complete sequence of chromosome 3 of Burkholderia sp. 383."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the TPP enzyme family. CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}. 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; CP000150; ABB05770.1; -; Genomic_DNA. DR AlphaFoldDB; Q39P46; -. DR KEGG; bur:Bcep18194_C6721; -. DR PATRIC; fig|482957.22.peg.7238; -. DR HOGENOM; CLU_013748_3_1_4; -. DR Proteomes; UP000002705; Chromosome 3. DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR CDD; cd00568; TPP_enzymes; 1. DR CDD; cd07035; TPP_PYR_POX_like; 1. DR Gene3D; 3.40.50.970; -; 2. DR Gene3D; 3.40.50.1220; TPP-binding domain; 1. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom. DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom. DR InterPro; IPR000399; TPP-bd_CS. DR InterPro; IPR045229; TPP_enz. DR InterPro; IPR011766; TPP_enzyme_TPP-bd. DR PANTHER; PTHR18968:SF167; 2-KETOARGININE DECARBOXYLASE ARUI-RELATED; 1. DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1. DR Pfam; PF02775; TPP_enzyme_C; 1. DR Pfam; PF00205; TPP_enzyme_M; 1. DR Pfam; PF02776; TPP_enzyme_N; 1. DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1. DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2. DR PROSITE; PS00187; TPP_ENZYMES; 1. PE 3: Inferred from homology; KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}; KW Transferase {ECO:0000313|EMBL:ABB05770.1}. FT DOMAIN 27..137 FT /note="Thiamine pyrophosphate enzyme N-terminal TPP- FT binding" FT /evidence="ECO:0000259|Pfam:PF02776" FT DOMAIN 216..348 FT /note="Thiamine pyrophosphate enzyme central" FT /evidence="ECO:0000259|Pfam:PF00205" FT DOMAIN 419..553 FT /note="Thiamine pyrophosphate enzyme TPP-binding" FT /evidence="ECO:0000259|Pfam:PF02775" SQ SEQUENCE 564 AA; 58456 MW; E97B79E1BBDE9F7D CRC64; MNHPATVSSI AGARKATAAP CHARPRTCGE ALVDLLERHG VECVFGIPGV HTVELYRGLA ASSIRHVTPR HEQGAGFMAD GYARVTGRPG VCFIITGPGM TNIATAMAQA YADSIPMLVI SSVNARRELG SGDGRLHELP SQRDVFAGLT AFSHTLLDAA DLPQVLARAF AVFASARPRP VHIEIPLDVI VMPAPALSDA PPALPARPAP DANALAAAAD LLAHARRPLI LAGGGAIHAA AELRELAERL HAPVALTINA KGLLPAGHPL LIGSTQSLPA TRAAIRDADV VLAVGTELGE TDYDVTFDGG FAIDGRLIRI DIDAQQLMRN ARAEIAIAGD SQLALGALST RLHETPAPTP DAGWGAPRVA AVRAAIAATH DSAAQSQALL IDTIVATLPG AIIAGDSTSP VYVGNFTHDA PAPRSWFNSS TGYGTLGYGL PAAIGAKLAA PARPVVCLIG DGGLQFTLPE LASAVEARLP VIVIVWNNHG YGEIRKYMVA RDITPVGVDP YTPDFQVLAR GFGCAAHTAA TPGALAAALR DAAARAIPTV IEIDEATWFG QVQR //