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Database: UniProt
Entry: A0A1I3KSF6_9BRAD
LinkDB: A0A1I3KSF6_9BRAD
Original site: A0A1I3KSF6_9BRAD 
ID   A0A1I3KSF6_9BRAD        Unreviewed;       541 AA.
AC   A0A1I3KSF6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Acetolactate synthase, large subunit {ECO:0000313|EMBL:SFI75471.1};
GN   ORFNames=SAMN05216525_11377 {ECO:0000313|EMBL:SFI75471.1};
OS   Bradyrhizobium sp. Gha.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1855318 {ECO:0000313|EMBL:SFI75471.1, ECO:0000313|Proteomes:UP000199284};
RN   [1] {ECO:0000313|EMBL:SFI75471.1, ECO:0000313|Proteomes:UP000199284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gha {ECO:0000313|EMBL:SFI75471.1,
RC   ECO:0000313|Proteomes:UP000199284};
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, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; FOQM01000013; SFI75471.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3KSF6; -.
DR   STRING; 1855318.SAMN05216525_11377; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000199284; 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   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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:SF167; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVB2-RELATED; 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          5..122
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          193..317
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          384..522
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   541 AA;  57720 MW;  4AD95644F12F0DD8 CRC64;
     MTTLTGGEAI VSGLVAHGVD TVFGLPGAQV YGLFDAFHQA QLKVIGARHE QACGYMAFGY
     ARSSGKPGVF SVVPGPGVLN ASAALLTAFG CNEPVLCVTG QVPTQFLGKG RGHLHEMPDQ
     LATLRSYVKW ADRIEHPGNA PTTVARAFQE MTSGRRGPAS VEMPWDIFTQ RAETGAAQVL
     APLPAPQPDP DMVKQAAALI KASKAPMIFV GSGAIEAREE ILELAEMIDA PVVAFRSGRG
     IVSNAHELGL TMAAAYKLWP KTDLMIGIGT RLELPTMSRW PYRPDGLKSI RIDIDPVEMR
     RYPSNAAIVA DAKAATADLA AAVSKAGYSK NPGRRAAIRE ASAGALAEIQ RVQPQMAYLN
     ILREVLPANA IVTDELSQFG FASWYGFPVY QPRTFITSGY QGTLGSGFPT ALGAKVANPD
     KPVVAITGDG GFMFGVQELA TAVQFNIGVV TLVFNNNAYG NVRRDQRERF DGRVVASDLV
     NPDFVKLAES FGVASARVTA PDQFKVAMEK ALAHGGPYLI SVEVTRDSEV SPWAFIHPPK
     P
//
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