ID A0A248VM25_9BURK Unreviewed; 550 AA.
AC A0A248VM25;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:ASW00066.1};
GN ORFNames=CJU94_19095 {ECO:0000313|EMBL:ASW00066.1};
OS Paraburkholderia aromaticivorans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2026199 {ECO:0000313|EMBL:ASW00066.1, ECO:0000313|Proteomes:UP000215158};
RN [1] {ECO:0000313|Proteomes:UP000215158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BN5 {ECO:0000313|Proteomes:UP000215158};
RA Lee Y.;
RT "Identification and genetic characteristics of simultaneous BTEX- and
RT naphthalene-degrading Paraburkholderia sp. BN5 isolated from petroleum-
RT contaminated soil.";
RL Submitted (AUG-2017) 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; CP022989; ASW00066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A248VM25; -.
DR KEGG; parb:CJU94_19095; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000215158; Chromosome 1.
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; cd02010; TPP_ALS; 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:SF129; ACETOLACTATE SYNTHASE; 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 1..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 186..322
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..527
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 143..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 550 AA; 61237 MW; 37AD2153CBA7AAB2 CRC64;
MKASDLFVKS LEAEGIEYVF GIPGEENLDL LESLRRSKIR LILTRHEQAA GFMAATYGRL
TGRIGVCLAT LGPGATNLVT AAAYAQLGGM PMLMVTGQKP IKSSKQGHFQ IVDVVRMMEP
LTKYTRQIVS VSNIPAAVRE AVRQAEEERP GATHLELPED VAHEEGDGKP IPKSYSRRPV
AEEKAVARAV EAITHAKHPL LMIGAGGNRK TTTKMLREFV DQIGIPFFTT QMGKGVIDES
HPMWLGNATL SDGDFVHRAI DHADCIINVG HDVIEKPPFF MRSGDAGEKT VIHVNFLGAE
VDTVYFPQIE VVGDIANAVW QLKESLKARQ EHWDFTRFKE IKAHFEAHLV KGQHDDRFPM
YPVRIVNDVY ETTPVDGIVC LDNGMYKIWF ARYYRAHEPN SLLLDNALAS MGAGLPSAIA
TKIVHPDRKV MAVCGDGGFM MNSQELETAV RLRLDLVILI LRDDAFGMIR WKQENMNFPD
YGMTLSNPDF VAYAQSYGAK GHRIESAAEF APLLRECFVT PGVHVIDLPI DYSDNERVLN
REIKRLSAQL
//
