ID A0A147GRJ1_9BURK Unreviewed; 520 AA.
AC A0A147GRJ1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KTT18716.1};
GN ORFNames=NS331_15885 {ECO:0000313|EMBL:KTT18716.1};
OS Pseudacidovorax intermedius.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Pseudacidovorax.
OX NCBI_TaxID=433924 {ECO:0000313|EMBL:KTT18716.1, ECO:0000313|Proteomes:UP000072741};
RN [1] {ECO:0000313|EMBL:KTT18716.1, ECO:0000313|Proteomes:UP000072741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS331 {ECO:0000313|EMBL:KTT18716.1,
RC ECO:0000313|Proteomes:UP000072741};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
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:KTT18716.1}.
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DR EMBL; LDSL01000100; KTT18716.1; -; Genomic_DNA.
DR RefSeq; WP_058642941.1; NZ_LDSL01000100.1.
DR AlphaFoldDB; A0A147GRJ1; -.
DR PATRIC; fig|433924.3.peg.55; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000072741; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02002; TPP_BFDC; 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; 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; 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:UP000072741}.
FT DOMAIN 5..108
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 382..517
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 520 AA; 53351 MW; 475A343C4BF7A8B4 CRC64;
MTEQTGAQAL WAALSGEGVD TCFANPGTTE LDLVRALEGQ DSIRCVIGLQ ENVCTGAADG
YGRMTGRPAA TLLHLGPGFA NGIANLHNAR RARTPIVNLI GDHTSWHLPF DAPLTSDIES
LARPVSGWVR RIDSTADAPR AAVESVRQSL AGGGQGATLI FPADYQAETL PGTAAPSPTD
ARAAVSSPSA VDLAACAQRL RAARRIVILL GGGGEQGGLG ARAQRAAARL CAALGATAYA
ETFPARAERG QGLPAFDRLP YFPEPARAVL DPADLVLLAG ALPPVTYFGY AGHPSLMVEA
ERLLSLGAPG HPVAEALEQL AEALDAPAFE APVHPLPAAP AGPLTPAAIG AALTRALPEG
AIVSVEGGTC GYPFYAASAA AAPHTALTNT GGAIGQGLPV AVGAAIACPE RQVVGLLSDG
STQYTIQALW TIAHEQLDVV VLIAANHQYA ILRNELRRGG ATLGKRAEAL TALDSPRIDW
VGLAQSYGVP ATRATTAEEL AAQLQDAFGR RGPALIEMAL
//
