ID A0A1X1YN71_9MYCO Unreviewed; 588 AA.
AC A0A1X1YN71;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=acetolactate synthase {ECO:0000256|ARBA:ARBA00013145};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145};
GN ORFNames=AWC15_15035 {ECO:0000313|EMBL:ORW12566.1}, MLAC_34180
GN {ECO:0000313|EMBL:BBX98124.1};
OS Mycobacterium lacus.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=169765 {ECO:0000313|EMBL:BBX98124.1, ECO:0000313|Proteomes:UP000466396};
RN [1] {ECO:0000313|EMBL:ORW12566.1, ECO:0000313|Proteomes:UP000193202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44577 {ECO:0000313|EMBL:ORW12566.1,
RC ECO:0000313|Proteomes:UP000193202};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BBX98124.1, ECO:0000313|Proteomes:UP000466396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15657 {ECO:0000313|EMBL:BBX98124.1,
RC ECO:0000313|Proteomes:UP000466396};
RX PubMed=31287781;
RA Matsumoto Y., Kinjo T., Motooka D., Nabeya D., Jung N., Uechi K., Horii T.,
RA Iida T., Fujita J., Nakamura S.;
RT "Comprehensive subspecies identification of 175 nontuberculous mycobacteria
RT species based on 7547 genomic profiles.";
RL Emerg. Microbes Infect. 8:1043-1053(2019).
RN [3] {ECO:0000313|EMBL:BBX98124.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 15657 {ECO:0000313|EMBL:BBX98124.1};
RA Matsumoto Y., Motooka D., Nakamura S.;
RL Submitted (FEB-2020) 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|ARBA:ARBA00000673};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004974}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; AP022581; BBX98124.1; -; Genomic_DNA.
DR EMBL; LQPF01000025; ORW12566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1YN71; -.
DR STRING; 169765.AWC15_15035; -.
DR KEGG; mlj:MLAC_34180; -.
DR OrthoDB; 2254214at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000193202; Unassembled WGS sequence.
DR Proteomes; UP000466396; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00568; TPP_enzymes; 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; 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 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000466396};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 205..306
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 393..547
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 588 AA; 60347 MW; B3E8B8CC0CC439C2 CRC64;
MPRTHRVVDH IVEHLAALGV DHIFGVDGAN IEDLYDAAHF QSDITAVLAK HEFSAATMAD
GYSRSGAGLG SGLGVVASTS GGGALNLVAG LGESLASRVP VLALVGQAPT TMDGRGSFQD
MSGCNGALNA QAVFSAVSLS CERVVTPSDI VSALPRAVAA ARTGGPAVLL LPKDIQQGYV
DVNWGGYRAS RTTQDLRPIG NPHPIAQVLR HANGPVTIIV GEQVARDDAR AELEALRAVL
RARVATVPDA KDVAGTPGCG SSSALGVTGV MGNPGVAQAV AASAVCLVVG TRLSVTARTG
LDDALAAVRT VSIGSATPYV PCTHVHTDDL RGSLRMLTHA LSGPGRPTGL RVPDVVHRTE
LTPPPLVGAG VRYRDAMAVL DGALPDGTDI VVDAGNTGAS AVHYLPARRG GRFAVALGMG
GMGYSFGAGI GMAFGRANTG RPAGRTVVVA GDGAFFMHGM EIHTAVQYRL PVTFVLLNNN
AHAMCVTREQ LFYDDLYSYN RFRSSRLGAG LAAMFPGLTS VDVTDLDGFA AAVRAALEVD
GPAVVSVECA ADEIPPFAPF LAKTSIKAPA TDEIPAAKES RTNVTASA
//
