ID   A0A261STY1_9BORD        Unreviewed;       514 AA.
AC   A0A261STY1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:OZI40477.1};
GN   ORFNames=CEG14_01535 {ECO:0000313|EMBL:OZI40477.1};
OS   Bordetella genomosp. 1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1395607 {ECO:0000313|EMBL:OZI40477.1, ECO:0000313|Proteomes:UP000217005};
RN   [1] {ECO:0000313|EMBL:OZI40477.1, ECO:0000313|Proteomes:UP000217005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU17610 {ECO:0000313|EMBL:OZI40477.1,
RC   ECO:0000313|Proteomes:UP000217005};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812}.
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:OZI40477.1}.
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DR   EMBL; NEVL01000001; OZI40477.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261STY1; -.
DR   OrthoDB; 2254214at2; -.
DR   Proteomes; UP000217005; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; 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; 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.
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          369..511
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          320..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   514 AA;  54142 MW;  F0FA92D9093CD2DB CRC64;
     MNGAKSLVQT LLASGVDTCF ANPGTSEMHF VAALDQIPGM KCVLGLQENV VTGMADGYFR
     IARKPACTLL HCGPGLANGM GNLHNARRAR SGIVNIVGDQ AIYHRPYDAP LTADTTGMAQ
     TVSQWVRTGT SAGQLGRDAA EAVSAARTFP GQIATLILPA DVSWNEGGAV GAPIAPAAPP
     AIDHNAVENA ARTLRQHGRD TLILLAGPAV QADAQRLVWR VAQATGAALL ADYVNGHVAR
     GRGRLPLERV PYTMEAATRA LQDYRHIILV NAKPPVGFFG YPGMPSIQYA ADAQLQVLSR
     PDQDPLEALD ALVRALDAPQ AEIPDPGPRP EAARGAPSPE GLAQTVAALM PDHAIVSDES
     VSYGRGFYKF THAAPPNDWL HLAGGAIGDG LPVATGAAIA AQRQRRVISL QADGSAMYSL
     QSLWTQARER LPVTTIILNN SKYNILIGEY KNVGAVPGET AMSMLDLGNP GISWTGLANA
     MGVEAARATT LEQCADLLRA SFTKDAPFLI ELMV
//