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Database: UniProt
Entry: A0A168W1N3_9BACI
LinkDB: A0A168W1N3_9BACI
Original site: A0A168W1N3_9BACI 
ID   A0A168W1N3_9BACI        Unreviewed;       543 AA.
AC   A0A168W1N3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:ANC77445.1};
GN   ORFNames=ABE65_011800 {ECO:0000313|EMBL:ANC77445.1};
OS   Fictibacillus phosphorivorans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX   NCBI_TaxID=1221500 {ECO:0000313|EMBL:ANC77445.1, ECO:0000313|Proteomes:UP000076623};
RN   [1] {ECO:0000313|EMBL:ANC77445.1, ECO:0000313|Proteomes:UP000076623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G25-29 {ECO:0000313|EMBL:ANC77445.1,
RC   ECO:0000313|Proteomes:UP000076623};
RA   Zheng Z.;
RT   "Complete genome sequence of Fictibacillus phosphorivorans G25-29, a strain
RT   toxic to nematodes.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP015378; ANC77445.1; -; Genomic_DNA.
DR   RefSeq; WP_066395081.1; NZ_CP015378.1.
DR   AlphaFoldDB; A0A168W1N3; -.
DR   STRING; 1221500.ABE65_011800; -.
DR   KEGG; fpn:ABE65_011800; -.
DR   Proteomes; UP000076623; Chromosome.
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:SF169; 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..111
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          192..327
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          383..529
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   543 AA;  58854 MW;  94F91DE03DC3A39B CRC64;
     MKKIADVLVM NLKNLGVEHT FGIPGKAVVP ILLELDRQGI PFNLTRHEGG AGYIASGYSL
     MNKTIGVAIG TSGPGGTNLL TAAAQAKAWH LPVLFLTGQP SSKDIGKPFG QDSTSFGTDL
     IKMFEPVTKF SARVDRAESF QSYFTHAIEK ALHGVKGPVH LSIPMDVLLE EIEPFLLQPK
     EAPQMVATKE SLQEALTSIH NAKRPVMILG KGVHASHAYE EVIQLAEAFS IPVMTTPGGK
     GTFPTTHELS LDGFGLGGSD RSADYLTQRS DLVIVIGSKL SDMSIVGLDP SRYPETIIHF
     DYDHTFIGKS IPAITHHILG DAASNVRSLL SLWNGENARP RPQILKETSV EEGSTTERML
     SKDIILTLRE SLPSETVFFG DDGSHSFYAI KHLSLPVPGS FYFDDVFGAM GHAIGYSIGA
     KVSRPEKPIV CLAGDGCFFM HGNEISTAVD LGAATLFVIF NNGRLDMVDK GMSKNVGKAV
     GTRFKQELDV EKFSEAMGAR AFKCWKLEEL RTAVKSGLNH HEGPTVIEVM VDQEEIPPTL
     QRG
//
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