ID   A0A0Q7AVN4_9BURK        Unreviewed;       587 AA.
AC   A0A0Q7AVN4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Acetohydroxyacid synthase large subunit {ECO:0000313|EMBL:KQW38297.1};
GN   ORFNames=ASC76_09715 {ECO:0000313|EMBL:KQW38297.1};
OS   Rhizobacter sp. Root404.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX   NCBI_TaxID=1736528 {ECO:0000313|EMBL:KQW38297.1, ECO:0000313|Proteomes:UP000051611};
RN   [1] {ECO:0000313|EMBL:KQW38297.1, ECO:0000313|Proteomes:UP000051611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root404 {ECO:0000313|EMBL:KQW38297.1,
RC   ECO:0000313|Proteomes:UP000051611};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQW38297.1, ECO:0000313|Proteomes:UP000051611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root404 {ECO:0000313|EMBL:KQW38297.1,
RC   ECO:0000313|Proteomes:UP000051611};
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   -!- 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:KQW38297.1}.
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; LMDS01000004; KQW38297.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q7AVN4; -.
DR   STRING; 1736528.ASC76_09715; -.
DR   OrthoDB; 2254214at2; -.
DR   Proteomes; UP000051611; 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:SF129; ACETOLACTATE SYNTHASE; 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:UP000051611};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          6..115
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          200..335
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          403..555
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   587 AA;  63375 MW;  CAFFFEE37EDD13D6 CRC64;
     MKQMISKQLV KYLEDRGVEY LFGLCGHTNI AVLTELEGST VKFVNTRHEQ IAAHMADGYA
     RAKHTTAVLL SHLGPGLTNA ATGVANAALD SIPMVVIAGD IPSHYYGKHP HQEVNLHSDA
     SQSEIYRPFV KRVWRVERPD LFPEILEKAF QLAESGRPGP VLVSVPMDIF SMEVDTALFE
     RLALHTKALN KPSMDDPTAE KIVRALLEAK NPVIYAGGGI LGADAAAELA EFATHLQIPV
     AHSLMGKGAL PDDHPLTLGM TGFWGTKFVN EKCRTADWVI GLGTRFAEAD CSSWDNEFTF
     SFPPTKLIHI DIDPSEIGRN YPAEIGVVTD LKQALIVLNR VAKKLAPTAR RNEKLQNEIA
     DYRAEFIAGN RPLTVAPGFP MQPERILAVV REALPRDAII TTDVGWNKNG VGQQFPIYTP
     GSILTPGGYA TMGFGAPAAL GAKLACPEKV VLALVGDGGF GQNPAMLATA VEMGIPVIWV
     VMNNFAYGTI AGLQMAHYGT TVGVLFRKDG KPYSPDFAAV ARAYGAEGVK IESADQFKGV
     LAEAIASNKP FVIDVAMLNN PVPTAGHWNI NDIYSPGKRD VSHVSIP
//