ID   A0A1M6QXB0_9RHOB        Unreviewed;       557 AA.
AC   A0A1M6QXB0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SAMN05444000_12352 {ECO:0000313|EMBL:SHK24909.1};
OS   Shimia gijangensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae.
OX   NCBI_TaxID=1470563 {ECO:0000313|EMBL:SHK24909.1, ECO:0000313|Proteomes:UP000183982};
RN   [1] {ECO:0000313|Proteomes:UP000183982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100564 {ECO:0000313|Proteomes:UP000183982};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-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; FQZQ01000023; SHK24909.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6QXB0; -.
DR   STRING; 1470563.SAMN05444000_12352; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000183982; 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; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000183982};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          3..104
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          186..320
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          397..534
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   557 AA;  60312 MW;  7F355901CB13CB8C CRC64;
     MIGADLIAGI LKKEGVEYIP AFPHSDIIDS GAKIGIVPLI VRQERHSLHI ADGYTRMHGG
     RKVCCTTVQY GPGSENAVGA VAQCYADNVP VLHMPGGYAR ADQGIAPNFN GARNMQLVNK
     WCEMVLQADR IPQMMQNAFA MMKNGRPGPV TLEIPIDIFT EEVDPALLDS YKVQRRSAPH
     ADPADISEMA DILLAAKNPV IIAGQGILYA EAWDELVALA ELTDTPVIST LNGKSCFPED
     HPLSVGCAGG ARPDGVNRAL ERADVYIGLG TSFTTSDYIT PFPKANRTFV QLTNWEGDIS
     KDYPIDLGVI GDAKPSIAAL VEAVKAKTDG KGVDRPEVIE TVAAEKQAFL DKWMPMLTSD
     EQPISPYRVV WDLMNTVDRS KTVMTHEAGS PRDQTTPFWE SIVPHGYMGW GKTTQLGMSL
     GLMQGAKLAK PDWTCVHVMG DAAIGMTGMD FETAVRLKLG TITIILKNSI MGGYTKHHPN
     ASEKYQIEAL GGDYAAMAEA FGGYAETITD PADLIPAYKR AIEKADQGIP VLLQIITKEE
     LRMAKDLPEG VGPHVQV
//