ID A0A0G1JRQ3_9BACT Unreviewed; 379 AA.
AC A0A0G1JRQ3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=UW70_C0061G0001 {ECO:0000313|EMBL:KKT74246.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWA2_44_7.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619057 {ECO:0000313|EMBL:KKT74246.1, ECO:0000313|Proteomes:UP000034415};
RN [1] {ECO:0000313|EMBL:KKT74246.1, ECO:0000313|Proteomes:UP000034415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKT74246.1}.
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DR EMBL; LCJI01000061; KKT74246.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1JRQ3; -.
DR STRING; 1619057.UW70_C0061G0001; -.
DR Proteomes; UP000034415; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 1.
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 PANTHER; PTHR18968:SF129; ACETOLACTATE SYNTHASE; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 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); 1.
PE 3: Inferred from homology;
FT DOMAIN 37..148
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 222..356
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT NON_TER 379
FT /evidence="ECO:0000313|EMBL:KKT74246.1"
SQ SEQUENCE 379 AA; 41511 MW; D9E449D6212F6BAA CRC64;
MFSKIIKTVS RTGLVGPDRE TPCGGAHEGE TSPSCFNGAQ LLVKALENEG VEYVFGLPGE
EIRDVMVALK NSPIQLVITR HEQGAAFMAD VYGRLTGKAG VCLATLGPGA TNLLTGVADA
HLDHSPLVAI TGQGSLDRLY KESHQVINVV RMFFPVTKWT DRITNPRNIP EMVRKAFKLA
EMEKPGATHI EFSENIAAML VEELPALKKI TVRRSIPEPE TIRRAAELIR QAKKPLILTG
NGAIRTNSSH ILRQWVAQTN IPVVSTFMGK GAVSDREPES LLSVGLGAHP GIVEVLKAAD
LVIAVGYDIA EYGPEKWNAD KHLKIIHIDF AQAEVYEQYI PEVELVGDIS DTLEQLSRQV
TAPVDFPEAR AYRKKIEAR
//
