ID A0A096AKB6_9FIRM Unreviewed; 577 AA.
AC A0A096AKB6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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 ORFNames=HMPREF0872_05205 {ECO:0000313|EMBL:KGF47250.1};
OS Veillonella montpellierensis DNF00314.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=1401067 {ECO:0000313|EMBL:KGF47250.1, ECO:0000313|Proteomes:UP000029628};
RN [1] {ECO:0000313|EMBL:KGF47250.1, ECO:0000313|Proteomes:UP000029628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00314 {ECO:0000313|EMBL:KGF47250.1,
RC ECO:0000313|Proteomes:UP000029628};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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}.
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:KGF47250.1}.
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DR EMBL; JRNT01000014; KGF47250.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A096AKB6; -.
DR eggNOG; COG0028; Bacteria.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000029628; Unassembled WGS sequence.
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:UP000029628};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591}.
FT DOMAIN 7..126
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 205..340
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 397..545
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 577 AA; 63523 MW; 8FC52999D1B1158B CRC64;
MRADKINGAH IVLETLYRLG VRHMFGYPGG AVIPIYDELY KYNEEDVKLH HYFVRHEQGA
AHAADGYARV SGKVGVCLAT SGPGATNLVT GIMTAYVDSI PLLAITGQVG RSLLGKDSFQ
EADTVGITMP ITKNNYLVKD IMDLPRIIKS AYFIASTGRP GPVLIDIPKD IQLQTIPMDV
YDKLYDEPIT VEGYDPTYKG HIGQIKKAAA LLKTAKKPLI IAGGGVLKAS AWQELRELAE
RTQTPVANTL VGLGCFPEDH PLSLGMLGMH GTVAANYATE AADVVIAAGI RFHDRITGDP
NHFCPHAKII HIDIDPAEID KNVKIHVPIV GDLKHVLTEL NTCIEDATHE EWWNQIHEWQ
ETYPMVVPPH DESVLYPQEV LSEVDRIVNG EAIIVTDVGQ HQMWAAQFLT FKHPHTMVTS
GGAGTMGYGV PAAMGAAIAA PDTTVVLVVG DGGFQMTFEE LMMMKQYHLN VKVLILNNQY
LGMVRQWQEL FNQRRYSFVD LHVSPDFVKL AEAFDLPAMR ISTRKELDAH LRDILTSDTG
IVIDCRVAEE VNVFPMIPAG ARVSNMVGKK GVSLHDE
//
