ID F2LCB4_BURGS Unreviewed; 534 AA.
AC F2LCB4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Acetolactate synthase large subunit {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=bgla_1g15070 {ECO:0000313|EMBL:AEA60166.1};
OS Burkholderia gladioli (strain BSR3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA60166.1, ECO:0000313|Proteomes:UP000008316};
RN [1] {ECO:0000313|EMBL:AEA60166.1, ECO:0000313|Proteomes:UP000008316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSR3 {ECO:0000313|EMBL:AEA60166.1,
RC ECO:0000313|Proteomes:UP000008316};
RX PubMed=21478339; DOI=10.1128/JB.00420-11;
RA Seo Y.S., Lim J., Choi B.S., Kim H., Goo E., Lee B., Lim J.S., Choi I.Y.,
RA Moon J.S., Kim J., Hwang I.;
RT "Complete genome sequence of Burkholderia gladioli BSR3.";
RL J. Bacteriol. 193:3149-3149(2011).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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DR EMBL; CP002599; AEA60166.1; -; Genomic_DNA.
DR RefSeq; WP_013697506.1; NC_015381.1.
DR AlphaFoldDB; F2LCB4; -.
DR STRING; 999541.bgla_1g15070; -.
DR KEGG; bgd:bgla_1g15070; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_8_0_4; -.
DR Proteomes; UP000008316; Chromosome 1.
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 16..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 392..530
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 534 AA; 55372 MW; 0358067093180A0A CRC64;
MEIPKLEVEV DSEMQNGACV VLKVARDSGV TVCFANPGTT EMPFVGALDQ VAGVRPILGL
FEGVCTGAAD GYGRMTGTPA MTLLHLGLGH ANGIANLHNA RRARTPILNL IGDHTRAHLK
YDAPLTSDIE SLARPVSVWY RSVATEQDLA RDTADAIAAT MGSARGVATL VLPVDLQSIA
VDSSASLAVP VQPPSAPAFD AAHVDEAAAL LRSGERVALL LGGRALSGRG QQAAARIAAA
FDAVCFSETF PARTERGGGL PDIDRLPYFP EPALAALAGR KVLLAGALAP VTYFGYEGIS
SELADPSDLV TLAGPNDSAD EALVALANTL ADRLAADGEP AAAEVAPWPV ESGALTPQAV
GRLLSNALPE HAIVSVEGGT CGYPFVTASS RARHHTILTN TGGAIGQGLP VALGAAVACP
DRRVFALQSD GSAQYTIQSL WTMARERLPI VMLITSNRRY GILQTELSRN GLPVDAPNSS
KLTLLDDPAI DWLALSQGYG VPAERVDTTD GLADALARAL AHTGGPCLIE MCLP
//
