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Database: UniProt
Entry: A0A124HBX3_9ACTN
LinkDB: A0A124HBX3_9ACTN
Original site: A0A124HBX3_9ACTN 
ID   A0A124HBX3_9ACTN        Unreviewed;       583 AA.
AC   A0A124HBX3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KUM92631.1};
GN   ORFNames=AQI88_31195 {ECO:0000313|EMBL:KUM92631.1};
OS   Streptomyces cellostaticus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67285 {ECO:0000313|EMBL:KUM92631.1, ECO:0000313|Proteomes:UP000054241};
RN   [1] {ECO:0000313|EMBL:KUM92631.1, ECO:0000313|Proteomes:UP000054241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40189 {ECO:0000313|EMBL:KUM92631.1,
RC   ECO:0000313|Proteomes:UP000054241};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces cellostaticus DSM 40189, type strain
RT   for the species Streptomyces cellostaticus.";
RL   Submitted (OCT-2015) 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:KUM92631.1}.
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DR   EMBL; LMWL01000061; KUM92631.1; -; Genomic_DNA.
DR   RefSeq; WP_067005540.1; NZ_KQ948035.1.
DR   AlphaFoldDB; A0A124HBX3; -.
DR   STRING; 67285.AQI88_31195; -.
DR   OrthoDB; 2254214at2; -.
DR   Proteomes; UP000054241; 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: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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054241};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          16..125
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          215..311
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          400..548
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   583 AA;  59963 MW;  19482AC86C7146AC CRC64;
     MTTTTSELRE AETVRLVDYL AGELARAGVT HVFGVGGANI EDLYDAVHRG GAVRGVVAKH
     EFSAVTMADG YARTTRRLGV VAATSGGGAM NLVPGLAEAY ASRVPVLALV GQPPTGQEGH
     GAFQDSSGKA GSFDAREVFA PVSRFCARVD DADALPELLP RAVAAAQADP RGPAVLLLPK
     DVQQARIKVP ARDTAPAPGG PATASAARLD TAAVTAVSDA LRGAGRVLVI AGEDVAAADA
     RADLAELARC LGAWVAVTPD AKDVFDNRDP RFAGVAGVMG HANVEDCLRR ADLCLLVGTR
     LPLLARGGLD RALAATDVVC LGPEPPFVAG TALGGNLRDA LRAVTARLPS HPRPCPPHAG
     PLPTPMPGPL FHARERTVPH AQAVAAVAAA LPQDAHVFVD AGNAGASAVH LLPAPRHGRF
     VVAVGMGGMG YTFGAGIGAA LATGRRTYVL AGDGAFFMHG MEVHTAVEYA APVTFVIFNN
     NAHAMCALRE EFLQGGVRSD DLFTRTDLAA GVTAAFPSLQ ATEATDAAHL RTALLRSNAG
     DGPAFVAVAC DPREIPPFLP FQSFTEATKS KEGSDERGVV HVG
//
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