ID A0A0B5DC99_9ACTN Unreviewed; 573 AA.
AC A0A0B5DC99;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:MBB4789613.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:MBB4789613.1};
DE SubName: Full=Thiamine pyrophosphate-binding protein {ECO:0000313|EMBL:AJE38840.1};
GN ORFNames=BJY54_000225 {ECO:0000313|EMBL:MBB4789613.1}, CP978_01535
GN {ECO:0000313|EMBL:QEV37420.1}, SNOD_01185
GN {ECO:0000313|EMBL:AJE38840.1};
OS Streptomyces nodosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=40318 {ECO:0000313|EMBL:AJE38840.1, ECO:0000313|Proteomes:UP000031526};
RN [1] {ECO:0000313|Proteomes:UP000031526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|Proteomes:UP000031526};
RA Sweeney P., Stephens N., Murphy C., Caffrey P.;
RT "Sequence of the Streptomyces nodosus genome.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AJE38840.1, ECO:0000313|Proteomes:UP000031526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|EMBL:AJE38840.1,
RC ECO:0000313|Proteomes:UP000031526};
RX PubMed=26497174;
RA Sweeney P., Murphy C.D., Caffrey P.;
RT "Exploiting the genome sequence of Streptomyces nodosus for enhanced
RT antibiotic production.";
RL Appl. Microbiol. Biotechnol. 100:1285-1295(2016).
RN [3] {ECO:0000313|EMBL:QEV37420.1, ECO:0000313|Proteomes:UP000325763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|EMBL:QEV37420.1,
RC ECO:0000313|Proteomes:UP000325763};
RA Lee N., Cho B.-K.;
RT "Streptomyces genome completion.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:MBB4789613.1, ECO:0000313|Proteomes:UP000544950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40109 {ECO:0000313|EMBL:MBB4789613.1,
RC ECO:0000313|Proteomes:UP000544950};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) 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; CP009313; AJE38840.1; -; Genomic_DNA.
DR EMBL; JACHMR010000001; MBB4789613.1; -; Genomic_DNA.
DR EMBL; CP023747; QEV37420.1; -; Genomic_DNA.
DR RefSeq; WP_043436922.1; NZ_JACHMR010000001.1.
DR STRING; 40318.SNOD_01185; -.
DR KEGG; snq:CP978_01535; -.
DR HOGENOM; CLU_013748_4_0_11; -.
DR OrthoDB; 2443624at2; -.
DR Proteomes; UP000031526; Chromosome.
DR Proteomes; UP000325763; Chromosome.
DR Proteomes; UP000544950; 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; cd02002; TPP_BFDC; 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:SF164; PYRUVATE DECARBOXYLASE; 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:UP000031526};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:MBB4789613.1}.
FT DOMAIN 11..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 213..318
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 415..569
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 573 AA; 61178 MW; 27C7BA4D04F777BF CRC64;
MTDTKAVRGP DGGDALVAAF NAVGADYLFC SSGSEWAPVW ESLARRHRDG EPAPEYLDLT
HETVAVGMAT GYGLLTRRPQ GVLLHAAPGL LQGSMAVHGA LLAGVPMVVA SSESTTYGDG
PGQDPGGQWY RNLSVVGGPH HVAQPFTKWA NEAASLHTLP TMVTRAAELA WRAPAGPAYL
NIPLEILLED WDGREAKPVV PPGSTHSSPE EADAVARLIR ESHNPVIVTE TAGREAGGFE
ALVAFAEAWN IPVVEPDSAV CGNFPRTHPL HAGSDVGPWI DEADLILLVN CRAPFYPPSR
RPAKARVVVI DEVPQRPHVV YQVLFADQYL EGGVVNTLRQ LTKRAKDLDG DAVTVRRTAQ
QRCHAAESNA IASAEAKAAT GTAEAGGVDP VLVAATLRRL LDGQDAVVVD ETITHSRIVK
RHLQQVDPDS YFYVQGGLGQ GIAVALGVKL AARERPVVLT IGDGAFTYNP VIPSYDASKT
YGLPVLIVVF NNRVYRSMNL NHRRFYPDGA AAQTGEWLGT DLHRLPRLAA FAEPFGMHTE
TVDTPAGLAP ALERALKAVS DGTTAVVDVL VTR
//
