ID A0A429BSX0_9ACTN Unreviewed; 548 AA.
AC A0A429BSX0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:RSN15725.1};
GN ORFNames=DMB42_02710 {ECO:0000313|EMBL:RSN15725.1};
OS Nonomuraea sp. WAC 01424.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=2203200 {ECO:0000313|EMBL:RSN15725.1, ECO:0000313|Proteomes:UP000286861};
RN [1] {ECO:0000313|EMBL:RSN15725.1, ECO:0000313|Proteomes:UP000286861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC 01424 {ECO:0000313|EMBL:RSN15725.1,
RC ECO:0000313|Proteomes:UP000286861};
RA Waglechner N., Wright G.D.;
RT "Evolution of GPA BGCs.";
RL Submitted (MAY-2018) 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:RSN15725.1}.
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DR EMBL; QHHZ01000001; RSN15725.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A429BSX0; -.
DR OrthoDB; 3203527at2; -.
DR Proteomes; UP000286861; 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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF13; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000286861};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..109
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..322
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 385..529
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 548 AA; 56808 MW; 1DD7FF18EB08B451 CRC64;
MTVTETAAAA VGRVLAAQGV RTAFGVVGSG NFHVTNALVE HGVRFVAARH EGGAATMADA
YARMSGEVGV VTVHQGPGLT NAMTGLTEAA KSRTPMVVLA GEATDARSNF HIDQEALATA
VGAVPMRVTD AGRAGERALE AFRVAARDRR TVLLNLPLDV QSMPSNAPVP VPAVGDAERS
GAPAGVVGGT AELGRLLAAA RRPVFIAGRG ARHARRELEA LADRTGALLA TSAVAKGLFR
GSPWDLDVSG GFATPLAAEL IRGADLVVGW GCALNMWTTR HGSLVPPGAK VAQVDLDPAA
VGAYVPVDLG VIGDVRAVAA ALTGPDGGAP GYRSAELAAR VRAEGRWRAV PYRDESGAGR
IDPRTLTIDL DDLLPIERVV SVDSGNFMGY PSMFLDVPDE GGFCFTQAFQ SIGLGLATAI
GAALARPDRL PVAALGDGGA FMGLAELETV VRLGLPMVVV VYDDEAYGAE VHHFGPHGFP
LDTVRFPPAD LAAIARGHGF AAVTVTDRAD LAGVAEWLKG PRDRPLLVHA KITGERGSWW
LEEAFKGH
//
