ID   Q8L209_STRTR            Unreviewed;       477 AA.
AC   Q8L209;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   SubName: Full=Alpha-acetolactate synthase {ECO:0000313|EMBL:AAL68398.1};
DE            EC=4.1.3.18 {ECO:0000313|EMBL:AAL68398.1};
DE   Flags: Fragment;
GN   Name=aldS {ECO:0000313|EMBL:AAL68398.1};
OS   Streptococcus thermophilus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1308 {ECO:0000313|EMBL:AAL68398.1};
RN   [1] {ECO:0000313|EMBL:AAL68398.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CNRZ 385 {ECO:0000313|EMBL:AAL68398.1};
RX   PubMed=12753249; DOI=10.1046/j.1472-765X.2003.01326.x;
RA   Monnet C., Nardi M., Hols P., Gulea M., Corrieu G., Monnet V.;
RT   "Regulation of branched-chain amino acid biosynthesis by alpha-acetolactate
RT   decarboxylase in Streptococcus thermophilus.";
RL   Lett. Appl. Microbiol. 36:399-405(2003).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812}.
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DR   EMBL; AY072795; AAL68398.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8L209; -.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0034077; P:butanediol metabolic process; IEA:InterPro.
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; IPR012782; Acetolactate_synth_catblc.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   NCBIfam; TIGR02418; acolac_catab; 1.
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   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   Lyase {ECO:0000313|EMBL:AAL68398.1}.
FT   DOMAIN          113..246
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          309..457
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAL68398.1"
SQ   SEQUENCE   477 AA;  52321 MW;  5303E85CE30AD201 CRC64;
     SNLATGLVTA TDEGDPVLAI GGQVKRADLL KRAHQSMNNV AMLEPITKYA AEVHDANTLS
     ETVANAYRHA KSGKPGASFI SIPQDVTDAP VSVKAIKPMT DPKLGSASVS DINYLAQAIK
     NAVLPVFLLG NGASSEAVTY SIRQILKHVK LPVVETFQGA GIVSRDLEED TFFGRVGLFR
     NQPGDMLLKK SDLVIAIGYD PIEYEARNWN AEISARIIVI DVEPAEVDTY FQPERELIGN
     VEASLNLLLP AIQGYKLPEG SVEYLKGLKN NVVEDVKFDR QPDEGTVHPL DLIEVLQEQT
     DDDMTVTVDV GSHYIWMARY FKSYEPRHLL FSNGMQTLGV ALPWAISAAL VRPKTKVISV
     SGDGGFLFSA QELETAVRLK LPIVHIIWND GHYNMVEFQE EMKYGRSSGV DFGPVDFVKY
     AESFGAKGYR ATSKAAFASL LQEALTQAVD GPVLIDVPID YKDNIKLGET ILPDEFY
//