ID A0A060LTB7_9BACI Unreviewed; 587 AA.
AC A0A060LTB7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:AIC93377.1};
GN ORFNames=BleG1_0769 {ECO:0000313|EMBL:AIC93377.1};
OS Shouchella lehensis G1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX NCBI_TaxID=1246626 {ECO:0000313|EMBL:AIC93377.1, ECO:0000313|Proteomes:UP000027142};
RN [1] {ECO:0000313|EMBL:AIC93377.1, ECO:0000313|Proteomes:UP000027142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G1 {ECO:0000313|EMBL:AIC93377.1,
RC ECO:0000313|Proteomes:UP000027142};
RX PubMed=24811681; DOI=10.1016/j.gene.2014.05.012;
RA Noor Y.M., Samsulrizal N.H., Jema'on N.A., Low K.O., Ramli A.N.,
RA Alias N.I., Damis S.I., Fuzi S.F., Isa M.N., Murad A.M., Raih M.F.,
RA Bakar F.D., Najimudin N., Mahadi N.M., Illias R.M.;
RT "A comparative genomic analysis of the alkalitolerant soil bacterium
RT Bacillus lehensis G1.";
RL Gene 545:253-261(2014).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP003923; AIC93377.1; -; Genomic_DNA.
DR RefSeq; WP_038477371.1; NZ_CP003923.1.
DR AlphaFoldDB; A0A060LTB7; -.
DR STRING; 1246626.BleG1_0769; -.
DR KEGG; ble:BleG1_0769; -.
DR PATRIC; fig|1246626.3.peg.767; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_9; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000027142; Chromosome.
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; 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:SF169; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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:UP000027142};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 200..338
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 404..556
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 587 AA; 64471 MW; F6A1ABDBBB84EC5F CRC64;
MKKLVSEQLV TYLESRGVEY VFGLCGHTNI AVLAELDKSP ITFINVRHEQ IASHAADGYA
RAKRKTSVVL SHLGPGLTNA ATGVANAALD SIPMVVIAGD VPSHYYGKHP HQEVNMHADG
AQWEIYRPFV KRAWRVDRED LFPEIIQKAF QLAESGRPGP VLVSVPMDIF SKEVDEEKFA
LLKHHTQVVE KPALDEETAE RIVETLANAE RPVIYAGGGV VLSQAEEELR EFVEHMNIPV
AHSLMGKGVL PDDHPLTVGM TGFWGTTFIN DQTKNADYLF GVGTRFSEAD SSSWYQNVTF
NFPKTKLIHI DIDPSEIGRN YPVEIGAVAD LKRALVALNR VAKQLYPNGM DRNEKLKEEI
QEYRKSLRAS IHENVTSDAF PMKPERILAD VREVLPRDAY ITTDVGWNKN GVGQQFPIYT
PGSILTPGGY ATMGFGSAAA LGAKLAQPNK VVVSLIGDGG FGQNPSVLAT AVEENIPVVW
VVMNNSAYGT IAGLEMAHYD TTYGTLFKKD GESYTPNFAE IAKGFGVKGV KITSAAEFKH
ELKAAIEANE PVVLDVAMRN EPVPTDGQWN INDIYSPYSK KSHVSIP
//