ID A0A2T0BFL0_9CLOT Unreviewed; 542 AA.
AC A0A2T0BFL0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Acetolactate synthase isozyme 3 large subunit {ECO:0000313|EMBL:PRR82680.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:PRR82680.1};
GN Name=ilvI {ECO:0000313|EMBL:PRR82680.1};
GN ORFNames=CLLU_28000 {ECO:0000313|EMBL:PRR82680.1};
OS Clostridium luticellarii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1691940 {ECO:0000313|EMBL:PRR82680.1, ECO:0000313|Proteomes:UP000237798};
RN [1] {ECO:0000313|EMBL:PRR82680.1, ECO:0000313|Proteomes:UP000237798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29923 {ECO:0000313|EMBL:PRR82680.1,
RC ECO:0000313|Proteomes:UP000237798};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium luticellarii DSM 29923.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:PRR82680.1}.
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DR EMBL; PVXP01000052; PRR82680.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0BFL0; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000237798; Unassembled WGS sequence.
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; 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, CHLOROPLASTIC; 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:UP000237798};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:PRR82680.1}.
FT DOMAIN 1..113
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 189..320
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 372..518
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 542 AA; 59932 MW; C6ECF3BB0495633C CRC64;
MKVCEKVLEY LKKNDILTAF GIPSATICPI VDAFNDFKDM EYIITKNEVS AAYSACKFAK
VSGKIGLLLV SGSVGIANAM NGIAEAMDSK LPVLIIGGYV DSNLQGLGAA QEVEGERYVS
NFVKYSKVVN NESDILSELQ HAIYEAYTYP RGVVHIGIPL NVQKQEYTGE DFPEVPHSVP
KTNYNSLIDA VSAINESKNG LLFIGGGCRG FGDKIKKLAE RLNWRIIYTP SGKGIVEDNF
HLNMGYYGMP GTDLSVKYVA DTDIDCIVAL GTRLGECSTQ CFTENLKKGK LIHVDADESV
FNKAYNEDVQ VVSHIGDALD YFLKNVQIRN TDNSIKEHIN APAVYKGKGL LLRNVLEKLP
EYVPYNTFYI SDIGSLMLFV ETYLKVPKGG AFECNLNYGA MGSSTGAIGI SRVYPDRPIV
QFVGDGGFFM NVIGELMTYK KYNLRIVCIV VNNHNLRFVD DGHKALFGRS IPGFMDEPVD
ISNIASAFGV KSLRLEHNSE IPNMKKFLAD IDQPLLIELV VDDDEPIPTN RFKSLKNTMN
RD
//