ID A0A0G3BSL8_9BURK Unreviewed; 599 AA.
AC A0A0G3BSL8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:AKJ29545.1};
GN ORFNames=AAW51_2854 {ECO:0000313|EMBL:AKJ29545.1};
OS Caldimonas brevitalea.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Caldimonas.
OX NCBI_TaxID=413882 {ECO:0000313|EMBL:AKJ29545.1, ECO:0000313|Proteomes:UP000035352};
RN [1] {ECO:0000313|EMBL:AKJ29545.1, ECO:0000313|Proteomes:UP000035352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7029 {ECO:0000313|EMBL:AKJ29545.1,
RC ECO:0000313|Proteomes:UP000035352};
RA Tang B., Yu Y.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP011371; AKJ29545.1; -; Genomic_DNA.
DR RefSeq; WP_053013573.1; NZ_CP011371.1.
DR AlphaFoldDB; A0A0G3BSL8; -.
DR STRING; 413882.AAW51_2854; -.
DR KEGG; pbh:AAW51_2854; -.
DR PATRIC; fig|413882.6.peg.2978; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000035352; 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; 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:UP000035352};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..114
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 203..299
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 394..538
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 599 AA; 63576 MW; D1A41B0E906BA86E CRC64;
MKLCDAMVHA LLALEVRYLF GVSGANIEHL HDAVHRANDP RLRSVLAKHE SGAAFMADGY
ARASGTLGVC CATSGGGMLN LAAGVAEAQA SAVPLLALVG QPPLLTEGQG GFQDSSGKGH
NVDALQLWRA VTGYAAKISR PELFWPALEE CLQHALHGRQ GASALLLPRD LMDAEVGPPP
SWLHQVDGPG ATRAPVVSER QCQRTWDLLR AARRPVLVLG EAAARQGVGE ALQSFIAATG
IGVVTTLGNI AAFPHRHPQY LGCIGVAGHP SAHRYLAEQA DLVIAAGTQL DAMTLGPLGH
TLRRLPLLMV NRSLTDVPRE LEPDLLLEMA PAVLFEALNP LLRSRALRFE APAGYRLSRH
PPSPAPAADR PLLTSEAVQT ISRHLPQDVH LVFDAGNCAA AAAHYLDAPL GTHASIALGM
GGMGYGVASA IGVQLARRHR YAGARRPTVV LCGDGAFLMN GAEVHTAVEL GLPVLWIVFN
NASHGMCATR QRLYFGNRVE ASVFGIEPSI ESMSRGFGPR QRLWVERAET SGQLARALCC
YFDESAHLPG VLELHLPVEQ LPPFAPFIAA QEALQATAAL KLGGHELQVG ARVAASTIR
//
