ID A0A1I4L5V0_9BACI Unreviewed; 545 AA.
AC A0A1I4L5V0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SFL86418.1};
GN ORFNames=SAMN04487943_104382 {ECO:0000313|EMBL:SFL86418.1};
OS Gracilibacillus orientalis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX NCBI_TaxID=334253 {ECO:0000313|EMBL:SFL86418.1, ECO:0000313|Proteomes:UP000198565};
RN [1] {ECO:0000313|EMBL:SFL86418.1, ECO:0000313|Proteomes:UP000198565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.4250 {ECO:0000313|EMBL:SFL86418.1,
RC ECO:0000313|Proteomes:UP000198565};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; FOTR01000004; SFL86418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4L5V0; -.
DR STRING; 334253.SAMN04487943_104382; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000198565; 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; 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:SF13; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..110
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..325
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 385..531
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 545 AA; 59361 MW; 884B110F8E924307 CRC64;
MKKVSTVLVE NLKRLGISHV FGIPGKAIVP LLVECEIQDL QFVLSRHESG SGFAAAGYAQ
TKGLGVALGT SGPGGTNLLT SAGQAKAYHS PTLFITGQPS AKDTGKAQGQ DSSIFGTDLV
RMFESVTLFS ARVDRGDQLE VFLKHAIEKA TNGVKGPVHL SIPMDVLQEE ISDFIVEIPT
LKSSVISNQI ETVISKLNEA GKPVLLLGKG VHLSKAYKEV RWLVEQWQVP VMTTPGGKGT
FPTNHPLSLG AYGLGGNEKA TKYLKKRVDQ MIVIGSKLSD MSLAGFSEAV YPKHLIHFDL
DPTFIQKSIP IPTLYIQGDI KANLVEIQRK TKLDRIDIKR VSLFSEENEN LDDIQESETY
LSAKVAIKEL RKYLPNDAVL FGDDGSHTFY AIKYYDIYEP GTFYFDDVFG TMGHAIGYSI
GAKVASPDKT VVCLTGDGCT FMHGTEIATA VDQNLPVIFI VFNNVALDMV DKGMKKMLGH
SIGATYQHAL DVKLFASSLG AASYRCRKTE DIENAIGQAL KNYTGPTVIE IMVDPEEIPP
ILNRV
//
