ID   W1SM13_9BACI            Unreviewed;       580 AA.
AC   W1SM13;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Acetolactate synthase catalytic subunit {ECO:0000313|EMBL:ETI69039.1};
GN   ORFNames=BAVI_09766 {ECO:0000313|EMBL:ETI69039.1};
OS   Neobacillus vireti LMG 21834.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI69039.1, ECO:0000313|Proteomes:UP000018877};
RN   [1] {ECO:0000313|EMBL:ETI69039.1, ECO:0000313|Proteomes:UP000018877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI69039.1,
RC   ECO:0000313|Proteomes:UP000018877};
RX   PubMed=24708037; DOI=10.1111/1462-2920.12478;
RA   Mania D., Heylen K., van Spanning R.J., Frostegard A.;
RT   "The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti is a
RT   potent source and sink for nitric and nitrous oxide under high nitrate
RT   conditions.";
RL   Environ. Microbiol. 16:3196-3210(2014).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:ETI69039.1}.
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DR   EMBL; ALAN01000059; ETI69039.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1SM13; -.
DR   STRING; 220686.AA980_20785; -.
DR   PATRIC; fig|1131730.3.peg.2036; -.
DR   eggNOG; COG0028; Bacteria.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000018877; 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; 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:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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:UP000018877};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          21..131
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          208..347
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          417..560
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   580 AA;  63010 MW;  22CA112EC28E5827 CRC64;
     MNNLTETHKE TDDSIKELTN AQRFALALKR NSVKYIFGQS NPQTIMLACA DLGIEQIGFR
     QENAGSYMAQ AYAMCSGSVP VVAAQNGPAA TLLVPGLAEC LKASHPVVAL VDDVPISEEE
     KNSFQDLDHI KLFSGVAKWV KKIPLEARIE DYVDMAFTAA ASGRPGPAVL LCPKDLTFDT
     KKNPVRTERK ASLGNYPLDR TTADSERIEE AAKLLVNAER PFIYAGGGVI SSRATDVLRQ
     IQEECSIPVA TTTMGKGSVD EEHALTMGPI GYYMGKGGAT KYLKPMVQTA DVILLVGNRT
     NQNGTDSWSL FSKDASIIHI DIDPMEVGRN YESLRLVGDA KLTLTALKNA LLRNSLDKRT
     KARPSIEETI EKARVAHIEE AKTIQNTDVS PIKVERFLAE LEKQLSDDHI IVADASFSSI
     WLANYIKAKG NRKFIFPRGL AGLGWGLPLA MGAKVAQPDR KVFCLAGDGG FAHVWSELET
     CKRHGIEVVV AVINNEVLAY QKLAELARWG RNTSACDLTA VDHSKVAEAC GVKGIRVDSS
     EKIAGALKEA FETKGSVVLD LISDPTSIPP LPFMSVLQNV
//