ID   A0A1I7MCK2_9BRAD        Unreviewed;       515 AA.
AC   A0A1I7MCK2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SFV19666.1};
GN   ORFNames=SAMN05192541_15723 {ECO:0000313|EMBL:SFV19666.1};
OS   Bradyrhizobium arachidis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=858423 {ECO:0000313|EMBL:SFV19666.1, ECO:0000313|Proteomes:UP000199591};
RN   [1] {ECO:0000313|EMBL:SFV19666.1, ECO:0000313|Proteomes:UP000199591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 26795 {ECO:0000313|EMBL:SFV19666.1,
RC   ECO:0000313|Proteomes:UP000199591};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812}.
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DR   EMBL; FPBQ01000057; SFV19666.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I7MCK2; -.
DR   Proteomes; UP000199591; 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; cd02002; TPP_BFDC; 1.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
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:SF86; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVX-RELATED; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
FT   DOMAIN          1..106
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          376..513
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   515 AA;  54249 MW;  CEA735215471BC4B CRC64;
     MNGAESLVRT MVKGGVDVCF TNPGTSEMHF VAALDRVPGM RCVLGLFEGV VTGAADGYFR
     MKGTPASTLL HLGPGLANGL ANLHNAKKAN SGIVNIVGQH AVYHIGYNAP LTSDIEGLAR
     PMSSWVRTSP DSKSVAADGA AAIAAAKSAP PQIATLILPA DTAWNEADGI AEVPAEQQRA
     SYSPQAVERA AKILHGDGEG TLLLMTGSAL SEQGLALAER IAGKTGCTVM GPTFRPKMAR
     GRGRFSIDRI HYVIENALPM LEKFRHIVLV ESDDPVAFFA YPNKPSMLKP QGCEVHRMTS
     WGENSVAALE ALAGAVKASA KDVKPQALAE LVKPTGALTF ATIAQAIACA IPENAIMVDE
     SLTTGRGFFP PTAAAAPHDW LQNMGGSIGF STPLSIGAAI ACPDRKVITM VGDGSAMYTI
     QSLWTQAREN LNIVTIVFAN RIYQILRGEF DNVGAGEPGQ RANDMLRLDR PTLDFVALAK
     GMGVPGRAVT NADEFNKALA EAVAEPGPRL IEVQM
//