ID A0A2U8E7V6_9BACT Unreviewed; 570 AA.
AC A0A2U8E7V6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=ilvB {ECO:0000313|EMBL:AWI10702.1};
GN ORFNames=CKA38_13760 {ECO:0000313|EMBL:AWI10702.1};
OS Ereboglobus luteus.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC Ereboglobus.
OX NCBI_TaxID=1796921 {ECO:0000313|EMBL:AWI10702.1, ECO:0000313|Proteomes:UP000244896};
RN [1] {ECO:0000313|EMBL:AWI10702.1, ECO:0000313|Proteomes:UP000244896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ho45 {ECO:0000313|EMBL:AWI10702.1,
RC ECO:0000313|Proteomes:UP000244896};
RX PubMed=29295750; DOI=10.1016/j.syapm.2017.10.005;
RA Tegtmeier D., Belitz A., Radek R., Heimerl T., Brune A.;
RT "Ereboglobus luteus gen. nov. sp. nov. from cockroach guts, and new
RT insights into the oxygen relationship of the genera Opitutus and
RT Didymococcus (Verrucomicrobia: Opitutaceae).";
RL Syst. Appl. Microbiol. 41:101-112(2018).
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; CP023004; AWI10702.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U8E7V6; -.
DR OrthoDB; 4494979at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000244896; 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:SF171; ACETOLACTATE SYNTHASE ISOZYME 1 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 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:UP000244896};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591}.
FT DOMAIN 7..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 195..330
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 393..542
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 570 AA; 60144 MW; 52D8A807B83F5974 CRC64;
MTKKKYTGAT LLTALLERQG IRQMPGIPGG AILPFYDALH TSPIQHILAR HEQGAGFIAQ
GMARVTGRAA ACVATSGPGA TNLITAIADA RLDSIPLVAI TGQVAQSLIG TDAFQEVDFY
GLTVPITKHN YLVRDVRELL HIVPEAFTLA ESGRPGPVVI DIPKDVQIAA IELSDDELPA
PGGCRPTPPA KDAEIDALAR MLAKAQRPVL YLGGGIIAAN ASALAHELAK RLDAPAVSTL
NALGAIPADS PHNMGMLGMH GTRATHTLLD ECDLIIAIGA RFDDRATGKV AEFCPRAAIA
HIDIDRAEFG KIKRPHLSIE ADAAEVLQRL LAHPLLHAEP GTPRASGWLA RATALRDAHP
LRHPSRETAP LHPVNICRFL AETLPSDAII ATDVGQHQMW VAQAYPFRSP RTLLTSGGLG
TMGFGLPNAI GAAFAAPGKR IACVSGDGSL LMNIQELATL ADHELSVAVL VFNNAHLGLV
RQQQELFYGR RYEASRFETT PDFAALARAF GIRGHSIAAN SADPLGDIAA ALAQPGPCLI
DIPIIATENV LPMVPPGAAN NQSIEHAGAM
//
