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}.
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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
//