ID   A0A0S8DNZ6_9BACT        Unreviewed;       290 AA.
AC   A0A0S8DNZ6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Acetolactate synthase catalytic subunit {ECO:0000313|EMBL:KPK37960.1};
DE            EC=2.2.1.6 {ECO:0000313|EMBL:KPK37960.1};
DE   Flags: Fragment;
GN   ORFNames=AMJ78_10750 {ECO:0000313|EMBL:KPK37960.1};
OS   Omnitrophica WOR_2 bacterium SM23_29.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1703776 {ECO:0000313|EMBL:KPK37960.1, ECO:0000313|Proteomes:UP000050824};
RN   [1] {ECO:0000313|EMBL:KPK37960.1, ECO:0000313|Proteomes:UP000050824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_29 {ECO:0000313|EMBL:KPK37960.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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}.
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:KPK37960.1}.
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DR   EMBL; LJUB01000167; KPK37960.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8DNZ6; -.
DR   PATRIC; fig|1703776.3.peg.156; -.
DR   Proteomes; UP000050824; Unassembled WGS sequence.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd02015; TPP_AHAS; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR039368; AHAS_TPP.
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   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   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Transferase {ECO:0000313|EMBL:KPK37960.1}.
FT   DOMAIN          1..62
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          117..263
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KPK37960.1"
SQ   SEQUENCE   290 AA;  32559 MW;  5E397959727CFA1E CRC64;
     IQNSDLIIAI GARFDDRVTG KIDEFAPHAR IVHIDIDPAA ISKNVRVDIP IVGDVKNVLT
     ELLKIVHKPD TKEWLERIKQ WREKHPLEYK NDNKLKPQYV IQQIYEATKG EAIIATDVGQ
     NQMWAAQWYT YTRPRSFISS GGLGTMGFGL PAAIGAKVGR PDEQVFVIAG DGSFQMNIQE
     LATAVVNGIH VKVAILNNSY LGMVRQWQEL FYKKRYSHTH LVNPDFVKIA EAYGAVGIRV
     AKKEEVRPAI EKALHTKNVV VMDFIVEEEE NVFPMVPVGK AIDQMIGSMA
//