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
//