ID C3GEU0_BACTU Unreviewed; 562 AA.
AC C3GEU0;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:EEM79304.1};
GN ORFNames=bthur0010_7590 {ECO:0000313|EMBL:EEM79304.1};
OS Bacillus thuringiensis serovar pondicheriensis BGSC 4BA1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=527029 {ECO:0000313|EMBL:EEM79304.1};
RN [1] {ECO:0000313|EMBL:EEM79304.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 4BA1 {ECO:0000313|EMBL:EEM79304.1};
RX PubMed=22645259; DOI=10.1101/gr.134437.111;
RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT "Genomic characterization of the Bacillus cereus sensu lato species:
RT Backdrop to the evolution of Bacillus anthracis.";
RL Genome Res. 22:1512-1524(2012).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:EEM79304.1}.
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DR EMBL; ACNH01000019; EEM79304.1; -; Genomic_DNA.
DR RefSeq; WP_000103511.1; NZ_CM000755.1.
DR AlphaFoldDB; C3GEU0; -.
DR GeneID; 45020933; -.
DR HOGENOM; CLU_013748_3_2_9; -.
DR Proteomes; UP000006660; Chromosome.
DR GO; GO:0003984; F:acetolactate synthase 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:0034077; P:butanediol metabolic process; 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; IPR012782; Acetolactate_synth_catblc.
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 NCBIfam; TIGR02418; acolac_catab; 1.
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 15..129
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 201..333
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 396..542
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 562 AA; 60970 MW; 5567D1EEC2D12273 CRC64;
MSTGVKANDV KTKTKGADLV VDCLIKQGVT HVFGIPGAKI DSVFDVLQER GPELIVCRHE
QNAAFMAAAI GRLTGKPGVC LVTSGPGTSN LATGLVTANA ESDPVVALAG AVPRTDRLKR
THQSMDNAAL FEPITKYSVE VEHPDNVPEA LSNAFRSATS TNPGATLVSL PQDVMTAETT
VESIGALSKP QLGIAPTHDI TYVVEKIKAA KLPVILLGMR ASTNEVTKAV RALIADTELP
VVETYQAAGA ISRELEDHFF GRVGLFRNQP GDILLEEADL VISIGYDPIE YDPKFWNKLG
DRTIIHLDDH QADIDHDYQP ERELIGDIAL TVNSIAERLP KLVLSTKSEA VLERLRAKLS
EQAEVPNRDS EGVTHPLQVI RTLRSLISDD TTVTCDIGSH SIWMARCFRS YEPRRLLFSN
GMQTLGVALP WAIAATLVEP GKKVVSVSGD GGFLFSAMEL ETAVRLNSPI VHLVWRDGTY
DMVAFQQMMK YGRTSATEFG DVDLVKYAES FGATGLRVNT PDELEGVLKS ALAADGPVII
DIPIDYRDNI KLSEKLLPNQ LN
//
