ID Q2KVX8_BORA1 Unreviewed; 569 AA.
AC Q2KVX8;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Acetolactate synthase isozyme I large subunit {ECO:0000313|EMBL:CAJ48513.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:CAJ48513.1};
GN Name=ilvB {ECO:0000313|EMBL:CAJ48513.1};
GN OrderedLocusNames=BAV0902 {ECO:0000313|EMBL:CAJ48513.1};
OS Bordetella avium (strain 197N).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ48513.1, ECO:0000313|Proteomes:UP000001977};
RN [1] {ECO:0000313|EMBL:CAJ48513.1, ECO:0000313|Proteomes:UP000001977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N {ECO:0000313|EMBL:CAJ48513.1,
RC ECO:0000313|Proteomes:UP000001977};
RX PubMed=16885469; DOI=10.1128/JB.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; AM167904; CAJ48513.1; -; Genomic_DNA.
DR RefSeq; WP_012416592.1; NC_010645.1.
DR AlphaFoldDB; Q2KVX8; -.
DR STRING; 360910.BAV0902; -.
DR GeneID; 41392813; -.
DR KEGG; bav:BAV0902; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_4_4; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000001977; Chromosome.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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 Reference proteome {ECO:0000313|Proteomes:UP000001977};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:CAJ48513.1}.
FT DOMAIN 17..129
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 201..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 398..544
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 569 AA; 60943 MW; 3F33BF5C6AAFA0BC CRC64;
MTLSSSPSSP PPASRIGGHI LVDQLAAHGV KHVFCVPGES YLAVLDGLHD ARIEVTVCRQ
EGGAAMMADA HGKLTGEPGI CMVTRGPGAS NALAGVHIAK QDSTPMILFV GQVERGMRER
EAFQEMDYRA VFGSQAKWVT EIDQVERIPE LISRAFHVAT SGRPGPVVIA LPEDMLVETA
EVADAPHYEV IDAAPGAGQM ETLAQALASA RKPVAILGGT RWSAEAVAQF ADFAKTHALP
VAVSFRRQML FPADHPCYSG DVGLGINPAL LARLSEADLI LLVGGRMSEI PSQTYSLLDI
PVPRQKLMHV HPDSAELARV YRPNLAINVS PVSFSAALAA LPAPSAAPVW ATDTDAMHQS
YLAWSDPKTI QTPGRLQLGE VMAYLEARLP ADAIMTNGAG NYATWLHRFH RFTRYGTQLA
PTSGSMGYGL PAAVGAKRVW PDKTVVCFAG DGCFLMHGQE FATAVQYDLP LVVVLIDNGM
YGTIRMHQEK HYPGRISATQ LKNPDFADYA RAFGGHGERV ETSAEFGPAF ERALASGKPA
ILHCLIDPET ISPSTTLEKI RAAALKAHA
//
