ID K6E7T7_9BACI Unreviewed; 531 AA.
AC K6E7T7;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:EKN69376.1};
GN ORFNames=BABA_09961 {ECO:0000313|EMBL:EKN69376.1};
OS Neobacillus bataviensis LMG 21833.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN69376.1, ECO:0000313|Proteomes:UP000006316};
RN [1] {ECO:0000313|EMBL:EKN69376.1, ECO:0000313|Proteomes:UP000006316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX PubMed=23087684;
RA Heylen K., Keltjens J.;
RT "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT reduction in Bacillus.";
RL Front. Microbiol. 3:371-371(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:EKN69376.1}.
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DR EMBL; AJLS01000056; EKN69376.1; -; Genomic_DNA.
DR AlphaFoldDB; K6E7T7; -.
DR STRING; 1117379.BABA_09961; -.
DR PATRIC; fig|1117379.3.peg.2080; -.
DR eggNOG; COG0028; Bacteria.
DR Proteomes; UP000006316; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000006316};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..321
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 379..525
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 531 AA; 58125 MW; 609F8E3D2CB74E2C CRC64;
MEAEMKASDL VVSCLENEGV EFVFGIIGKE VIDLGDSLSA SEKITYIPVR HEQGASFMAD
VYGRISGRPG VCLATLGPGA TNLVTGIACA NLDHSPVIAI TGQKALKDQH KNSHQYINIK
EVYKPVTKWA IQIKDANTIP EIIRKSFRLA FEEKPGAVVI ELPEDIAVEN VTTEPLAVSS
LPKSVPVAES LKIAAQVLNQ SKRPFIIVGN EVIRQDAVLE VLSLIDQLGS PVATSFMAKG
ILSKDHPQNY YTFGFMEKDY VLRGFEEADL LIVIGFDLVE KLPSEWNMKK VPVIHISATA
ADVDEYYPVQ AELVGNLKET MPLLIPTLKP WQPIGGLKRR IQESYSIIEK ASDDSALTIE
KILHVLEKVQ TDEMVLISDV GSHKVAIART YQPKHAKQLI ISNGFASMGI SIPGAIGAKL
AAPEKIVICI TGDGGALMAF AELETAKRLG LSFVIILLND SMLKLEVDTM KKKFGDSYGV
TFTNPDFVQL AESFGARGMR ATNVEEFERM VTEAMNAKNE IVLIDTIMQL R
//
