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
//