ID A0A0W8JEF0_9VIBR Unreviewed; 513 AA.
AC A0A0W8JEF0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KUI98592.1};
GN ORFNames=VRK_24600 {ECO:0000313|EMBL:KUI98592.1};
OS Vibrio sp. MEBiC08052.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1761910 {ECO:0000313|EMBL:KUI98592.1, ECO:0000313|Proteomes:UP000054473};
RN [1] {ECO:0000313|EMBL:KUI98592.1, ECO:0000313|Proteomes:UP000054473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEBiC08052 {ECO:0000313|EMBL:KUI98592.1,
RC ECO:0000313|Proteomes:UP000054473};
RA Kim Y.J., Lee J.-H., Kwon K.K.;
RT "Genome sequence of Vibrio sp. MEBiC08052.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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:KUI98592.1}.
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DR EMBL; LQIY01000021; KUI98592.1; -; Genomic_DNA.
DR RefSeq; WP_059121537.1; NZ_KQ947475.1.
DR AlphaFoldDB; A0A0W8JEF0; -.
DR STRING; 1761910.VRK_24600; -.
DR PATRIC; fig|1761910.3.peg.2488; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000054473; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR CDD; cd02002; TPP_BFDC; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF86; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVX-RELATED; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
FT DOMAIN 1..106
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 377..510
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 513 AA; 54713 MW; DA50D8DDA458DC48 CRC64;
MNGAEAIVKA AVESGVEYCF ANPGTTEMPF VAAMDSEPKF RPVLSMFEGV CTGAADGYGR
VSGRPALTLT HLGPGFANGI ANLHNARRAN SPIVNLVGDH ASWHVNYDPP LASDIESLAR
PVSAFFRTSK SVDRMVEDFG AAMRAAWQPC GAISTLVLPM DLQAKALSGD MPKMSILPPK
RHFKADNVEA VAERIKAGKR LVFIVGDNGL DEKGLTAAGR IGQLPGIKMF AETFPRISHR
GGGLPDLDRL PYFPEKAIAE LEQYDEVVCA GVVEPIAYFG YEGMPSRLAE TDRLVTLADV
GDDVSGALEA LAELLNAPAH KDLVGTIELP AANEALTPQS IGKIVSSILP DNCIVSVEGG
TCGYPFFTES ALASRHRVLT NTGGAIGQGI PAGFGAALAE PGNTVVCLQS DGSAQYTIQT
LWSIARENLP VVILIAANHK YSILQNELRR YGVTEFGQNS LALTELDRPR VDWQALSKAY
GVDSVCVTNN AELMREFKAA CDAKAPRLIE MSL
//