ID A0A0F2J0V4_9BACT Unreviewed; 577 AA.
AC A0A0F2J0V4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=MCHI_001168 {ECO:0000313|EMBL:KJR42931.1};
OS Candidatus Magnetoovum chiemensis.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Magnetoovum.
OX NCBI_TaxID=1609970 {ECO:0000313|EMBL:KJR42931.1, ECO:0000313|Proteomes:UP000033718};
RN [1] {ECO:0000313|EMBL:KJR42931.1, ECO:0000313|Proteomes:UP000033718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS-04 {ECO:0000313|EMBL:KJR42931.1,
RC ECO:0000313|Proteomes:UP000033718};
RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT conserved set of magnetosome genes.";
RL Submitted (FEB-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}.
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:KJR42931.1}.
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DR EMBL; JZJI01000305; KJR42931.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2J0V4; -.
DR PATRIC; fig|1609970.3.peg.1291; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000033718; 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:UP000033718};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591}.
FT DOMAIN 4..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 392..538
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 577 AA; 63882 MW; AB677D2C910C80C6 CRC64;
MKISGSEIIL ESLKREGVKH IFGYPGGVVL HLFDFIYDDK DIQLILTRHE QGATHAADGY
SRSTGKVGVA LVTSGPGATN TVTGLATAAM DSIPIIVLTG QVATTLIGND AFQEADTVGI
TRPCTKYNYL VKSVDDLAYT IKEAFYIATS GRPGPVVIDL PKDVTAAKSK FEWPETINIR
SYNPTLEGNK WMIERACEKI TKSRKPIIIA GGGVILSGAS EELRELAEFT SIPVITTLMG
IGSFPSSHPL YLGMPGMHGT YYANMAIQNC DLLIAAGMRF DDRVTGKLDA FAPHAEIIHI
DIDPTSIRKN VEVDIPIVGD CNRILTTLNT IIKSQEAQQW DEIRNAWLKQ LQEWKKLRPM
QYNYSDTIIK PQFVIEKLCE IAGDDVIITT EVGQNQMWAA QFYKFKKPRT FLTSGGLGTM
GYGFPAALGA QVANPDKTVI DIAGDGSIQM NIQELATATI YNLPVKVAIL NNRYLGMVRQ
WQEMFFNERY SHSHLDVVPD FVKLAEAYNA VGLRAEKPSD VEPVIREALK VKKPVLMDFV
IDWKEKVYPM VPAGAPIDNM LFDDEPEKEE KKLKAVK
//
