ID   R9JUH1_9FIRM            Unreviewed;       593 AA.
AC   R9JUH1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Acetolactate synthase I/II/III large subunit {ECO:0008006|Google:ProtNLM};
GN   ORFNames=C808_03595 {ECO:0000313|EMBL:EOS37616.1};
OS   Lachnospiraceae bacterium M18-1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1235792 {ECO:0000313|EMBL:EOS37616.1, ECO:0000313|Proteomes:UP000014090};
RN   [1] {ECO:0000313|EMBL:EOS37616.1, ECO:0000313|Proteomes:UP000014090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M18-1 {ECO:0000313|EMBL:EOS37616.1,
RC   ECO:0000313|Proteomes:UP000014090};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium M18-1.";
RL   Submitted (APR-2013) 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:EOS37616.1}.
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DR   EMBL; ASSV01000027; EOS37616.1; -; Genomic_DNA.
DR   AlphaFoldDB; R9JUH1; -.
DR   STRING; 1235792.C808_03595; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_1_3_9; -.
DR   Proteomes; UP000014090; 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; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF142; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000014090};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          1..105
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          200..333
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          392..544
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   593 AA;  65749 MW;  98924FF2A3A85D43 CRC64;
     MRVCDYIADE IYKAGAKDVF LVTGGGMMFL TDGLASHPKI NAIPCHHEQA AAMAAVGYAK
     YNGFGSAFVT TGCGGTNTVT GVLHAYQDST PCVFVSGQCA TNEIIQSAPA PLRQFGMQEA
     DIVSIVKPIT KYAVTLKETE SVVYEIEKAL YLAKEGRPGP VWIDVPLDIQ QAELEGIAQR
     HFPIPDQDKP LCTDDELCSI AESLKNAERP LIIAGQGIRL SGAVELFGRF IEEYQIPFVY
     SRLGFDVYPN GKDLSIGCIG IRGTRAGNFA VANADFILVL GSRLSINSTG YNSDLFAREA
     RVCVVDVDEN EHKKNTIRID QFICSDVKYF LEHIPALDRG KYSEWVSICK NWKNKYPACT
     AECYDDRHGI SLYAFTNEMS KYLDEDAAVV TDAGSTCYVV PQSMKFLYDG QRYMPSGAQA
     EMGYTLPAAL GTCFARGKKS TIGIVGDGSL QMNIQELQTV KHHDLPIKLF VWNNDGYMSI
     RGAQKGRFSG RYLGSGRASG VTLPSLDKIC YAYGIDYVRL ENLAQIDEIM KRVMRVTHPI
     ICEVMCRPDE WILCTWSRRT LENGDVIRMP NEDMAPLLDR EEFYNNMIVK PVS
//