ID A0A0H1AL02_9GAMM Unreviewed; 548 AA.
AC A0A0H1AL02;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KLI99754.1};
GN ORFNames=WQ56_11430 {ECO:0000313|EMBL:KLI99754.1};
OS Luteimonas sp. FCS-9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Luteimonas.
OX NCBI_TaxID=1547516 {ECO:0000313|EMBL:KLI99754.1, ECO:0000313|Proteomes:UP000035397};
RN [1] {ECO:0000313|EMBL:KLI99754.1, ECO:0000313|Proteomes:UP000035397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FCS-9 {ECO:0000313|EMBL:KLI99754.1,
RC ECO:0000313|Proteomes:UP000035397};
RA Bala M., Kumar A., Kaur N., Mathan Kumar R., Kaur G., Singh N.K.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Luteimonas oceanisediminis
RT sp. nov., a novel gammaproteobacteria isolated from a marine sediment.";
RL Submitted (APR-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:KLI99754.1}.
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DR EMBL; LASZ01000012; KLI99754.1; -; Genomic_DNA.
DR RefSeq; WP_047137248.1; NZ_LASZ01000012.1.
DR AlphaFoldDB; A0A0H1AL02; -.
DR STRING; 1547516.WQ56_11430; -.
DR PATRIC; fig|1547516.3.peg.2409; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000035397; 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 GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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:UP000035397};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 187..320
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 379..525
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 548 AA; 59368 MW; 982CCBF184A6BB1B CRC64;
MTKASDLFVS ALEAEGVTHV FGVPGEENLD LLESLRASKI ELVLTRHEQA AGFMAATCGR
LTGKAGVCLA TLGPGATNLV TAAAYAQLGA MPMLMVTGQK PIRSSRQGHF QIVDIVDTMR
PLTKTTRQLV SADGIPARVR DAFRLAEEER PGAAHLELPQ DVAGDDTDAQ LLPAAYGRRP
LAEPKAIARA AEAVAAARHP LLMIGAGANR KTTARTLRAF VERLGIPFFS TQMGKGVLDE
TGPLWLGTAA LSEGDFVHRA IDAADCIVNI GHDVIEKPPF SMHRGRRTVI HVNYASAAID
QVYFPQIEVV GDIANAVWQL GEALAPQPHW DFAFFDRVRE ALCTHIDGLA RDDRFPLRIP
HLVAEVRAAL GPRDIACLDN GLYKLWFARH YRCHAPNTLL LDNALATMGA GLPSAIAART
IHPDRRVVAI CGDGGFMMNS QELETAVRRR LDLVVLVLRD DAYGMIKWKQ AHEDYPAFGM
DYGNPDFVAY ARSYGARGHR PDSAAGFGAL LRTALDTPGV DLIEVPVDYT DDDTLLNEDI
PRLSAAVA
//