ID   A0A318M0Y8_9PSEU        Unreviewed;       557 AA.
AC   A0A318M0Y8;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BA062_12215 {ECO:0000313|EMBL:PXY36195.1};
OS   Prauserella flavalba.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Prauserella.
OX   NCBI_TaxID=1477506 {ECO:0000313|EMBL:PXY36195.1, ECO:0000313|Proteomes:UP000247892};
RN   [1] {ECO:0000313|EMBL:PXY36195.1, ECO:0000313|Proteomes:UP000247892}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 121212 {ECO:0000313|EMBL:PXY36195.1,
RC   ECO:0000313|Proteomes:UP000247892};
RA   Ruckert C., Albersmeier A., Jiang C.-L., Jiang Y., Kalinowski J.,
RA   Schneider O., Winkler A., Zotchev S.B.;
RT   "Draft genome sequence of Prauserella sp. YIM 121212, isolated from
RT   alkaline soil.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:PXY36195.1}.
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DR   EMBL; MASU01000005; PXY36195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A318M0Y8; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000247892; 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; IPR000399; TPP-bd_CS.
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.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000247892};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          9..120
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          192..325
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          398..539
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   557 AA;  58519 MW;  BE988C03B83D92F5 CRC64;
     MSSDTPRLGA GLVADTLAAE GITHVFGLPG TTVMELIDAL GEHGTVRYLS TRHEQVAGFM
     ADGFSRAGGL GVCLASRGPG AANLAIAVQN AHDESVPLLA LIGQVPRSIT HRRSFEDMDV
     VSAFRPMCKW AVEITEPDRI PELLQRAVRT AVGGRPGPVV VSLPLDVLQA PAHASIGPRV
     RTYPPAPDPA GIAEAARLLA GARRPAVIVG GGGAGDPEAV LALAETAGAP VVSTWLRKNA
     LPGGHPAFLG SLGYGAHDVT DQLVRDADVV VALGCRFSEF TTKRWTLLPP AAKLVHADVD
     PEELGRVHPP AVGLVSDAAA AARALTRALT PLIAADRARA ASRTARRVAL RKAFEEAAAL
     PVTPASEGTV SSSALVRAVQ GLADRDGVVL VQDVHTFGPW VQRYVHVERP RSYYGSAGGA
     MAWGFPAAMG MALARPGERM VTLSGDGSFW MVAQDFETCV REGIDVVTVV VNNHAYGNTR
     DRQRFAHDGR YHGVFLGNPD FAEYARILGG HGIRVTSDAE LGPAIEEALA QEGPCIVDVV
     QDRMEGLPSG LTPPRAR
//