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
//