ID A0A0A2VHB1_9BACI Unreviewed; 558 AA.
AC A0A0A2VHB1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KGP93010.1};
GN ORFNames=N780_11805 {ECO:0000313|EMBL:KGP93010.1};
OS Pontibacillus chungwhensis BH030062.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385513 {ECO:0000313|EMBL:KGP93010.1, ECO:0000313|Proteomes:UP000030153};
RN [1] {ECO:0000313|EMBL:KGP93010.1, ECO:0000313|Proteomes:UP000030153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH030062 {ECO:0000313|EMBL:KGP93010.1,
RC ECO:0000313|Proteomes:UP000030153};
RA Wang Q., Wang G.;
RT "Genome of Pontibacillus chungwhensis.";
RL Submitted (AUG-2013) 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:KGP93010.1}.
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DR EMBL; AVBG01000001; KGP93010.1; -; Genomic_DNA.
DR RefSeq; WP_036779084.1; NZ_AVBG01000001.1.
DR AlphaFoldDB; A0A0A2VHB1; -.
DR STRING; 1385513.N780_11805; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000030153; 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:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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:UP000030153};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 14..126
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 203..334
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 391..537
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 558 AA; 61777 MW; 6635C9A99F49DD50 CRC64;
MIEKSLRPIK RTLTSAHAIV ECMKIEGVKH VFCVPGESYL PIMDAIHDEP SIKLISARHE
GGASFMAEGY AKSSGKPGVL MATRGVGGSN LTIGVHTAHQ DSTPMVVFLG QVHSQFRGRE
GFQEVDLDQY FRHIAKWTVE IRDAKRVPEL VQRAFRVAQT GRPGPVVVSL PEDLLIKESV
MAFGPPVRRP TPSPSSDEVG DVEKLLQSSE SPLIIAGGGV KASEAEGALK QFAEKYKIPV
MASFRRHDVM PNDHPLYLGH LGLGTHKSIL ETVQQSDVIL AFGTRLSEVT TQDYSIITDE
KKLVHVDIEY DSIGKIYQPD IGIVADLKEG LHALLSINLL SSWEDWAVTR RRVYENVTSL
TNKDVDNHNF HTQIIQTLQA QLPKNAILTN DAGNFAGWLH TFFQFTERNT YVGPTSGAMG
YGMPAALGTK LAHPHRTVLS LSGDGGFMMT MQEIETAVRY NIPIISIVFN NKMYGTIRMH
QEMHYPFKPI GTELGSVPFT ELAQSIGANG YFVRTIKEFE LAIERAVKSD KPVVIEIESD
PNQISVSSTI EEIRNQHK
//
