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
//