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Database: UniProt
Entry: W8PU41_9PSED
LinkDB: W8PU41_9PSED
Original site: W8PU41_9PSED 
ID   W8PU41_9PSED            Unreviewed;       513 AA.
AC   W8PU41;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:AHL34557.1};
GN   ORFNames=CD58_17350 {ECO:0000313|EMBL:AHL34557.1};
OS   Pseudomonas brassicacearum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=930166 {ECO:0000313|EMBL:AHL34557.1, ECO:0000313|Proteomes:UP000019521};
RN   [1] {ECO:0000313|EMBL:AHL34557.1, ECO:0000313|Proteomes:UP000019521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DF41 {ECO:0000313|EMBL:AHL34557.1,
RC   ECO:0000313|Proteomes:UP000019521};
RX   PubMed=24812222;
RA   Loewen P.C., Switala J., Fernando W.G., de Kievit T.;
RT   "Genome Sequence of Pseudomonas brassicacearum DF41.";
RL   Genome Announc. 2:e00390-14(2014).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812}.
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DR   EMBL; CP007410; AHL34557.1; -; Genomic_DNA.
DR   RefSeq; WP_025214143.1; NZ_CP007410.1.
DR   AlphaFoldDB; W8PU41; -.
DR   KEGG; pbc:CD58_17350; -.
DR   PATRIC; fig|930166.5.peg.3382; -.
DR   eggNOG; COG0028; Bacteria.
DR   OrthoDB; 9785953at2; -.
DR   Proteomes; UP000019521; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd02002; TPP_BFDC; 1.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF86; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVX-RELATED; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
FT   DOMAIN          1..106
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          374..510
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   513 AA;  54056 MW;  AF59DCC9B6C66BBA CRC64;
     MNGAQLIVKA AVASGIEYCF ANPGTTEIPL VAAMASAPAL KPVLSMFEGV CTGAADGYGR
     IAGKPAMTLT HLGPGFANGI ANLHNARRAN TPIVNVIGDH ASWHVNYDPP LASDIQALAG
     SVSGWVRTSR TASGIGDDFQ EAVRAAWQAK GQIASLILPM DLQANPVERE SAFTTLQAPV
     RRFAGDRIEA VAQALRNGQR LVFIVGDQGL SVAGLEAAGR LAQLPGVRMF AETFPRLSYR
     GGGLPDLDRL PYFPEVAIEI LDQYDVVVCA GVPDPISYFG YEGIPSRLAE RDRLLCLAEV
     GDDVAGALTA LANELEAPAF VPTSMGVELP IAEAELTPQS IGQVLAASLP DDCIVSVEGG
     TCGYPFFTAS AHAARHRVLT NTGGAIGQGI PVGFGAALAE RGNRVFCLQS DGSAQYTIQT
     LWSIAREQLP VVILIAANHR YAILQNELRR FGMTELGPEA LSLTVLDRPR IDWKALAKGY
     GLPASTVHTN AELQRALANA KADGGPCLIE MAL
//
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