ID A0A1U7CPW8_9BACT Unreviewed; 589 AA.
AC A0A1U7CPW8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
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:APW60946.1};
GN ORFNames=BSF38_02440 {ECO:0000313|EMBL:APW60946.1};
OS Paludisphaera borealis.
OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC Paludisphaera.
OX NCBI_TaxID=1387353 {ECO:0000313|EMBL:APW60946.1, ECO:0000313|Proteomes:UP000186309};
RN [1] {ECO:0000313|Proteomes:UP000186309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX4 {ECO:0000313|Proteomes:UP000186309};
RA Ivanova A.;
RT "Comparative genomics of four Isosphaeraceae planctomycetes: a common pool
RT of plasmids and glycoside hydrolase genes.";
RL Submitted (DEC-2016) 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; CP019082; APW60946.1; -; Genomic_DNA.
DR RefSeq; WP_076345937.1; NZ_CP019082.1.
DR AlphaFoldDB; A0A1U7CPW8; -.
DR STRING; 1387353.BSF38_02440; -.
DR KEGG; pbor:BSF38_02440; -.
DR OrthoDB; 4494979at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000186309; 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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR00118; acolac_lg; 1.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
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:UP000186309};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591, ECO:0000313|EMBL:APW60946.1}.
FT DOMAIN 17..128
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 208..342
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 399..565
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 589 AA; 64206 MW; 73A711BE8506221C CRC64;
MSAIENCKVQ TAARPTTGAD VLVESLARHG VDVVFAYPGG ASMPMHQALT RYRDRIRTIL
PRHEQGGIFA AEGFARASGR PGVVMATSGP GALNLVTGLA DAKMDSIPLI AITGQVPTHV
IGTDAFQETP TVEVCRAICK HAYLVQNARD IARIMKEAFY LATTGRPGPV LIDMPKDIQN
TIVANPDYDV EMDLPGYVLP PEPTPAKIRE VLAAIKESQR PIIYCGGGVL ASNAGDELRE
FASKAGIPVA MTVHGLGSMP SDHYLSLDML GMHGTVYANL AVSQADLLLA FGVRFDDRVT
GKLSEFAKHG KIVHVDIDAS EINKNKLAHI PVHSDVKSFL KAINPQVVSG DYGAWRHQID
EWRASDPMTY DQRDDVILPQ YVLDEFSKLT KGEFIMSTGV GQHQMWAAQW TKFNRLRSWI
TSGGLGSMGY GLPAAMGAQA AFPDALVVDI DGDGSFLMNI QELATVFCED LPVKVIVLNN
QHLGMVVQWE DRFHQGNRAH TYLGPIHHPE AIGQGAGEQP DELYPDFIQI AKGFGVKARQ
IRRKEEVGEA LLEMINHKGP YVLDVLVPYQ EHVLPMIPSG GTVRDVIKT
//
