ID   A0A0Q8QYW3_9BURK        Unreviewed;       582 AA.
AC   A0A0Q8QYW3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KRB87928.1};
GN   ORFNames=ASE07_19430 {ECO:0000313|EMBL:KRB87928.1};
OS   Noviherbaspirillum sp. Root189.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Noviherbaspirillum.
OX   NCBI_TaxID=1736487 {ECO:0000313|EMBL:KRB87928.1, ECO:0000313|Proteomes:UP000051303};
RN   [1] {ECO:0000313|EMBL:KRB87928.1, ECO:0000313|Proteomes:UP000051303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root189 {ECO:0000313|EMBL:KRB87928.1,
RC   ECO:0000313|Proteomes:UP000051303};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB87928.1, ECO:0000313|Proteomes:UP000051303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root189 {ECO:0000313|EMBL:KRB87928.1,
RC   ECO:0000313|Proteomes:UP000051303};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRB87928.1}.
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DR   EMBL; LMHZ01000014; KRB87928.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q8QYW3; -.
DR   STRING; 1736487.ASE07_19430; -.
DR   Proteomes; UP000051303; Unassembled WGS sequence.
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   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:SF166; 2-HYDROXYACYL-COA LYASE 2; 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   Reference proteome {ECO:0000313|Proteomes:UP000051303};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          3..113
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          203..332
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          433..561
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   582 AA;  61328 MW;  FD322883CFB03D8D CRC64;
     MAGLLIAYLE QLGVEQVFGV PGGAIEPIYN ALAQSSRRGG PRPVVARHEA GAAFMADGYT
     RETGALGVVC ATSGPGATNL ITGVACAYDN GIPMLVITGQ PALPGFGRRA LQESSCTGIN
     TVGMFRHCTQ YNSLVSHPQQ LEAKLIAALM RATRTPRGPV HLSIPLDILN SPATVAAPSY
     DLRTLLKPSS MLDQQAVDSL SLMLRDARNP VLLIGGWCGE AIASILRVAE LRQVPFVTTP
     DGKGLVDPRH PLYRGVFGFA GHASAEAALR DRSVDLILAV GTSMNEWTSS GWSDSLLNTR
     LVHVDESDDH LARTPMAKLH VSGRILTVFE KLFAQLDTVA TTTSPDADVA TVTATTTVTA
     CHEALLFTLP AGPAQPPDAK VKPSQLMHDL GRLFPATTRY LADAGNSVAW AVHHLAPQFA
     HPDERSTSSH GGWLRTTMDF APMGWAIGGA VGTALGNPDG PVVCITGDGS LMMNGQELSV
     AVAEGLTVIF VVLNDAALGM VKHGQRLAGA EQIAFALPPT DFAMLARALG AEAHTIRTAA
     DLNALDIDAI CARKGPTLLD VFIDPEEVPP ISVRMRVLGT LL
//