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Database: UniProt
Entry: A0A162RNP9_9CLOT
LinkDB: A0A162RNP9_9CLOT
Original site: A0A162RNP9_9CLOT 
ID   A0A162RNP9_9CLOT        Unreviewed;       556 AA.
AC   A0A162RNP9;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Acetolactate synthase, catabolic {ECO:0000313|EMBL:KZL90173.1};
DE            EC=2.2.1.6 {ECO:0000313|EMBL:KZL90173.1};
GN   Name=budB {ECO:0000313|EMBL:KZL90173.1};
GN   ORFNames=CLMAG_46670 {ECO:0000313|EMBL:KZL90173.1};
OS   Clostridium magnum DSM 2767.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121326 {ECO:0000313|EMBL:KZL90173.1, ECO:0000313|Proteomes:UP000076603};
RN   [1] {ECO:0000313|EMBL:KZL90173.1, ECO:0000313|Proteomes:UP000076603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2767 {ECO:0000313|EMBL:KZL90173.1,
RC   ECO:0000313|Proteomes:UP000076603};
RA   Poehlein A., Uhlig R., Fischer R., Bahl H., Daniel R.;
RT   "Genome sequence of Clostridium magnum DSM 2767.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:KZL90173.1}.
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DR   EMBL; LWAE01000006; KZL90173.1; -; Genomic_DNA.
DR   RefSeq; WP_066627689.1; NZ_LWAE01000006.1.
DR   AlphaFoldDB; A0A162RNP9; -.
DR   STRING; 1121326.CLMAG_46670; -.
DR   PATRIC; fig|1121326.3.peg.4726; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000076603; 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; cd02010; TPP_ALS; 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: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:UP000076603};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000313|EMBL:KZL90173.1}.
FT   DOMAIN          12..121
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          198..329
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          389..535
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   556 AA;  61476 MW;  D3D23C40BBA386E6 CRC64;
     MSREIKEEVQ LNTAQMLIKC LEAEGVEYIF GIPGEENLEV MNAIADSSIK FITTRHEQGA
     AFMADVYGRL TGNAGVCLAT LGPGATNLVT GVADADSDGA PVVAITGQVG TERMHITSHQ
     FLDLCKMFEP ITKRSKQIVR PDTVNEIVRL AFKYAESEKP GACHIDLPVN IAKMPVSIGE
     KPLEKKIPPK EHADLSTIED AASEIFKAKN PVILAGSGAV RGNTSKAVTE FATKLKIPVI
     NTMMAKGIIP FDNKYSMWTI GIPQKDYVNK IIEEADLVIT VGYDIVEYAP SKWNPKGQTE
     IVHIDARPSH INKLYQPVVE VVGDISDALY NIMRRTSSKA EPVKALEIKA KMLAEHESYA
     EDNGFPMKPQ RILNDVRKVM GREDIVISDV GAHKMWIARH YNCYEPNTCI ISNGFATMGI
     AIPGAIAAKL INPDKKVLAI AGDGGFMMND QELETALRIG TPIVVLVFND NNYGLIKWKQ
     EEQYGKSCYV NFTNPDFVKF AESMHAKGYR VEKAEDLIPT LEEAFKQNVP VVIDCQVDYE
     ENLKLTNHLK EIYGNI
//
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