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Database: UniProt
Entry: A0A0U2NW70_9MICC
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ID   A0A0U2NW70_9MICC        Unreviewed;       556 AA.
AC   A0A0U2NW70;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:ALU38445.1};
GN   ORFNames=AS188_00300 {ECO:0000313|EMBL:ALU38445.1};
OS   Kocuria flava.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=446860 {ECO:0000313|EMBL:ALU38445.1, ECO:0000313|Proteomes:UP000057181};
RN   [1] {ECO:0000313|EMBL:ALU38445.1, ECO:0000313|Proteomes:UP000057181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HO-9041 {ECO:0000313|EMBL:ALU38445.1,
RC   ECO:0000313|Proteomes:UP000057181};
RA   Zhou M., Dai J.;
RT   "Complete Genome Sequence of Kocuria flava strain HO-9041.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP013254; ALU38445.1; -; Genomic_DNA.
DR   RefSeq; WP_058857159.1; NZ_CP013254.1.
DR   AlphaFoldDB; A0A0U2NW70; -.
DR   STRING; 446860.AS188_00300; -.
DR   KEGG; kfv:AS188_00300; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000057181; 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, CHLOROPLASTIC; 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:UP000057181};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          4..107
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          188..321
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          388..537
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          163..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   556 AA;  57644 MW;  8050A6B9A845E9B6 CRC64;
     MTGTVAALVA RTLAELGVGH VFGVVGSGNF HLVNALVACG VPFTAARHEN GAATMADAFA
     RTSGQVAVVT THQGCGLTNA TTGIGEAAKS RTPLVVLTAD TQAAAVHSNF RIDQDGLARS
     VGAVAERVHS PASAAADTAR AYRRARNDRR TVVLSVPLDV QAAPAPGHAP VPALPDPPRP
     RPHDDDAARL AGLLASARRP VFVAGRGARG ARAELVALAE RSGALLATSA VAKGLFAGEA
     FDLGISGGFS APLTAELIRR ADLVVGWGCA LNMWTTRHGR LLGPEAAVVQ VDLEEQALGA
     HRDPDRPLAM GVVGDCALTA RDVLARLEGT TAPSSSWRTP GLAARLAREG RWRDVAHEDL
     STPERIDPRA LSRALDEILP AERVVAVDSG NFMGYPSQYL DVPDERGFCF TQAFQSVGLG
     LATAIGAALA QPHRLPVLGT GDGGFLMGVA ELETAVRLGL PLVCVVYDDA AYGAEVHHFA
     GPGAPEVPLD TVVFPDTDLA AVGRGFGAEG AVVRTLGDLE AVRAWVAGPR ERPLVVDAKI
     ASDGGSWWLA EAFRGH
//
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