ID A0A0L6CS70_9RHOB Unreviewed; 561 AA.
AC A0A0L6CS70;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Acetolactate synthase isozyme 2 large subunit {ECO:0000313|EMBL:KNX40556.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:KNX40556.1};
GN Name=ilvG {ECO:0000313|EMBL:KNX40556.1};
GN ORFNames=ROTO_28980 {ECO:0000313|EMBL:KNX40556.1};
OS Roseovarius tolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=74031 {ECO:0000313|EMBL:KNX40556.1, ECO:0000313|Proteomes:UP000037046};
RN [1] {ECO:0000313|Proteomes:UP000037046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EL-164 {ECO:0000313|Proteomes:UP000037046};
RA Voget S., Bruns H., Wagner-Doebler I., Schulz S., Daniel R.;
RT "Draft Genome Sequence of Roseovarius tolerans EL-164, a producer of N-
RT Acylated Alanine Methyl Esters (NAMEs).";
RL Submitted (JUL-2015) 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:KNX40556.1}.
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DR EMBL; LGVV01000048; KNX40556.1; -; Genomic_DNA.
DR RefSeq; WP_050663763.1; NZ_LGVV01000048.1.
DR AlphaFoldDB; A0A0L6CS70; -.
DR STRING; 74031.SAMN04488077_104161; -.
DR PATRIC; fig|74031.6.peg.2952; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000037046; 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 GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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 Reference proteome {ECO:0000313|Proteomes:UP000037046};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:KNX40556.1}.
FT DOMAIN 7..122
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 195..332
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..532
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 561 AA; 59701 MW; 581189150C761E95 CRC64;
MTHDTRNGGQ LLVDCLVALG ARHSFGVPGE SYLAVLDALH DMAGQLDFTI CRQEGGAAYM
AAAYGKLTGR PGIAWVTRGP GATNASIGVH TAMQDSAPML LFVGQVGTDM KGREAFQELD
YRAVFGSMVK WAVEIDDVDR IPEITARAWK TALTGRPGPV VVALPEDMLT ATSTKPALTG
PGHYPEAEPS AEAIARTRNM LGAAKRPLIL YGGCNWTSAG RAALHSFAEG SDIPVVSVFR
YQDKFDNHSP CFCGEAGVGM MPHVRALITG ADVILAINNR FGENSTDGYT ALTVPQPAQR
LIHVHASDLE LGKVYQPELG VQAGANAFIR ALDAGGPLRG DWSDWRAGGR KSYEAAFDLP
DQPPPVDMGR VTAHLREVLP EDAIITNGAG NFAIWSGRFL KYGPNMRLLA PQSGSMGYGI
PAAIAAKIVH PDRRVVCFAG DGDFQMNCQE LATAAQAGAQ PVILILNNGI YGTIRAHQER
NYPERVSGTT MVNPDFPALA RAYGFHAERV ETTEGFAPAF ARACASSTGA VLDLAISPEA
LTPRMTLSQM RAAGLEKATK G
//