ID A0A085FKV0_9BURK Unreviewed; 567 AA.
AC A0A085FKV0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Acetolactate synthase isozyme 2 large subunit IlvG {ECO:0000313|EMBL:KFC72095.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:KFC72095.1};
GN Name=ilvG {ECO:0000313|EMBL:KFC72095.1};
GN ORFNames=FG94_02128 {ECO:0000313|EMBL:KFC72095.1};
OS Massilia sp. LC238.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1502852 {ECO:0000313|EMBL:KFC72095.1, ECO:0000313|Proteomes:UP000028601};
RN [1] {ECO:0000313|EMBL:KFC72095.1, ECO:0000313|Proteomes:UP000028601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC238 {ECO:0000313|EMBL:KFC72095.1,
RC ECO:0000313|Proteomes:UP000028601};
RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT isolate.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:KFC72095.1}.
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DR EMBL; JNNN01000038; KFC72095.1; -; Genomic_DNA.
DR RefSeq; WP_036210817.1; NZ_JNNN01000038.1.
DR AlphaFoldDB; A0A085FKV0; -.
DR STRING; 1502852.FG94_02128; -.
DR PATRIC; fig|1502852.3.peg.2074; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000028601; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
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:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:KFC72095.1}.
FT DOMAIN 7..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..327
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..539
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 567 AA; 61376 MW; 9896A9964E4361C7 CRC64;
MTHPSRTGGQ ILVDALHTHG VDTAFGVPGE SYLDVLDALH DSDIRFVINR QEGGAAFMAE
AYGKMTGKPG ICFVTRGPGA TNASIGVHTA FQDSTPMILF IGQVGSDFID REAFQEIDYR
RMFGQMAKWV TQIDRADRIP EYIARAFQVA TSGRPGPVVL ALPEDMLVNK AEVPDARRYQ
PVQAAPSTEQ VAQLRAMLAE SQRPIVLLGG GSWSDQACAD LARFAEANRL PVGCTFRFQD
LMDNAHPNYV GDVGIGINPK LAARVKEADL VIAIGPRLGE MTTSGYSLLS SPVPRQRLVH
IHADPEELGS VYQADLMIAS GAPQVCAMLA AMEPVDSSAW ANTVEEARAD LTAWQAQPPI
FRDGAAPLDL WQVVQELMRQ SPRDTIITNG AGNYATWAHR FYRYGGKRTQ LAPTNGAMGY
AVPAGVAAKI IDPQRTVVTF AGDGEFMMTG QELATAVQYG AGVIILVFNN SMFGTIRMHQ
ERDYPGRVSG TSLHNPDFAA LARAYGGHGE VVEKTEEFAP ALQRALAHAN ERKLPAVIEL
RYDGNLITPN ATLETIRKTA EAAKAGR
//
