ID Q2NQA3_SODGM Unreviewed; 548 AA.
AC Q2NQA3;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 24-JAN-2024, entry version 120.
DE RecName: Full=Acetolactate synthase {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
GN Name=ilvG {ECO:0000313|EMBL:CRL46764.1};
GN OrderedLocusNames=SG2397 {ECO:0000313|EMBL:BAE75672.1};
GN ORFNames=SGGMMB4_05635 {ECO:0000313|EMBL:CRL46764.1};
OS Sodalis glossinidius (strain morsitans).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=343509 {ECO:0000313|EMBL:BAE75672.1, ECO:0000313|Proteomes:UP000001932};
RN [1] {ECO:0000313|EMBL:BAE75672.1, ECO:0000313|Proteomes:UP000001932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Morsitans {ECO:0000313|EMBL:BAE75672.1}, and morsitans
RC {ECO:0000313|Proteomes:UP000001932};
RX PubMed=16365377; DOI=10.1101/gr.4106106;
RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA Aksoy S.;
RT "Massive genome erosion and functional adaptations provide insights into
RT the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL Genome Res. 16:149-156(2006).
RN [2] {ECO:0000313|EMBL:CRL46764.1, ECO:0000313|Proteomes:UP000245838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:CRL46764.1}, and morsitans
RC {ECO:0000313|Proteomes:UP000245838};
RA Goodhead I.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2;
CC Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
CC Evidence={ECO:0000256|RuleBase:RU003591};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU003591};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU003591};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|RuleBase:RU003591};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000256|RuleBase:RU003591};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004974, ECO:0000256|RuleBase:RU003591}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025,
CC ECO:0000256|RuleBase:RU003591}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU003591}.
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DR EMBL; AP008232; BAE75672.1; -; Genomic_DNA.
DR EMBL; LN854557; CRL46764.1; -; Genomic_DNA.
DR RefSeq; WP_011412203.1; NZ_LN854557.1.
DR STRING; 343509.SG2397; -.
DR KEGG; sgl:SG2397; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_1_2_6; -.
DR OMA; YMGMIGM; -.
DR OrthoDB; 9785953at2; -.
DR BioCyc; SGLO343509:SGP1_RS21740-MONOMER; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000001932; Chromosome.
DR Proteomes; UP000245838; Chromosome sggmmb4_Chromosome.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02015; TPP_AHAS; 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; IPR012846; Acetolactate_synth_lsu.
DR InterPro; IPR039368; AHAS_TPP.
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 NCBIfam; TIGR00118; acolac_lg; 1.
DR PANTHER; PTHR18968:SF142; ACETOLACTATE SYNTHASE; 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU003591};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|RuleBase:RU003591}; Magnesium {ECO:0000256|RuleBase:RU003591};
KW Metal-binding {ECO:0000256|RuleBase:RU003591};
KW Reference proteome {ECO:0000313|Proteomes:UP000001932};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591}.
FT DOMAIN 1..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 189..321
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 374..522
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 548 AA; 58443 MW; 929F89ABBAE24677 CRC64;
MNGAQWVIQA LRAQGVDMVF GYPGGAIMPV YDALFDGGVE HLLCRHEQGA AIAAIGYARA
TGKVGVCIAT SGPGATNLIT GLADALLDSV PVVAITGQVG SAFIGTDAFQ EIDVLGLSLA
CTKHSFLVES LDALPGIITE AFAIATSGRT GPVLIDIPKD IQLADGDLTP HLLSLDDQAS
SIQGDLDGAR RLMRQATRPI LYVGGGVGMA GAVPALRQLI TQTGLPAVAT LKGLGAPDVD
DACYLGMLGM HGNQAANLAV QACDLLIAVG ARFDDRVTGR LNAFAPHAKV IHLDIDPAEL
GKLRQAHIAL LGDLNHLLPA LAQPLSIDAW RVETQALKAE YRWRYDNPGA GIYAPALLRA
ISDRAPDEAV VTTDVGQHQM WAAQHMRFSR PENFITSSGL GTMGFGIPAA IGAQIARLED
TVICISGDGS FMMNVQELTT IKRKRLPLKI VLLDNQRLGM VRQWQQLFFD KRYSETTLTD
NPDFLTLASA FNIPGLHITR KDQIPQALDS LFNQPGPFLL HVSIDELENV WPLVPPGAGN
ETMLEKSL
//