ID   A0A0R3N9W0_9BRAD        Unreviewed;       599 AA.
AC   A0A0R3N9W0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KRR26797.1};
GN   ORFNames=CQ14_20705 {ECO:0000313|EMBL:KRR26797.1};
OS   Bradyrhizobium lablabi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=722472 {ECO:0000313|EMBL:KRR26797.1, ECO:0000313|Proteomes:UP000051660};
RN   [1] {ECO:0000313|EMBL:KRR26797.1, ECO:0000313|Proteomes:UP000051660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCBAU 23086 {ECO:0000313|EMBL:KRR26797.1,
RC   ECO:0000313|Proteomes:UP000051660};
RA   Duran D., Rey L., Navarro A., Busquets A., Imperial J., Ruiz-Argueso T.;
RT   "Bradyrhizobium valentinum sp. nov., isolated from effective nodules of
RT   Lupinus mariae-josephae, a lupine endemic of basic-lime soils in Eastern
RT   Spain.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:KRR26797.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LLYB01000043; KRR26797.1; -; Genomic_DNA.
DR   RefSeq; WP_057856883.1; NZ_LLYB01000043.1.
DR   AlphaFoldDB; A0A0R3N9W0; -.
DR   STRING; 722472.SAMN05444321_4135; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000051660; 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; 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   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          7..119
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          206..342
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          411..566
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   599 AA;  65005 MW;  0DFC670F4B8EE6A3 CRC64;
     MSRNMLNGAQ VIVDYLIQEK VPQVFGLCGH GNIQFIDALY ERSHDIKTIS VHHESVAGFM
     ADVYYRVSGR PTATFTSCGP GSANLPISLA NAFLDSVPFM AVTGNVPTSQ FNRGAFQEMY
     RHHQADFPST VRTICKKVFQ PTRGEMVPLA VRQAWKTMTS GRPGPVVLDV PFDVFVESAA
     EEAPNAIEWN ANISSRCGAD PEGVVKAVDM LLGAERPTII VGQGVRYGGA AEELRRLAER
     LQIPVAASAS GLGALDCNHP LALGLVARAG HYQANHATRQ ADVLLAMGMR FDDRTSSSWI
     PGYSFTIPPT RLIHVDIDPE EIGRNYPVAL GLMADVRTFL RQVHAELDRR GDLSKKADAR
     KKWLSQIDGY RKEWDKFVAP GFSDDTTPIN PQRAALEIDK ALPEDAILVS DIGVHHNWLL
     GFCKPRRPDS LIGSMGFGPM GFGVAGVMGA KFAAPDRPCV SVCGDGAFFM HANVLGTAVE
     YNLPVVWVVW NNYAYASIRG LQRGYLGGRE LATDFHDPNT GERYNPDFAA MARSCGVEGV
     RVDRAGDLGE AIRKGIAANK PYLIDVDIAA DINPVGAGVW ELPGLGQSKA GIGTRYQPA
//