ID A0A1G4WLW6_9MYCO Unreviewed; 570 AA.
AC A0A1G4WLW6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=acetolactate synthase {ECO:0000256|ARBA:ARBA00013145};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145};
GN ORFNames=SAMN02799620_03860 {ECO:0000313|EMBL:SCX25462.1};
OS Mycolicibacterium fluoranthenivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=258505 {ECO:0000313|EMBL:SCX25462.1, ECO:0000313|Proteomes:UP000199707};
RN [1] {ECO:0000313|Proteomes:UP000199707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UNC267MFSha1.1M11 {ECO:0000313|Proteomes:UP000199707};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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|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; FMUB01000008; SCX25462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4WLW6; -.
DR STRING; 1502745.SAMN02799620_03860; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000199707; Unassembled WGS sequence.
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 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 10..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..294
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 399..546
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 570 AA; 59115 MW; 4A831C31798AF9CB CRC64;
MSNGQTSRRR VVDHIVDRLA AHGVRHIFGV DGANIEDLYD AAHFRADLTA VLAKHEFSAA
TMADGYRRSG APLGVVAATS GGGSLNLVAA LGESLTSRVP VLALVGQPPT AMDGRGSFQD
TSGLGGSLDA EALFSAVSVY CRRVVDPGLI ETALSEALAA SHRGPAVLLL PKDVQQGFFE
GAAGAGLPLA VPIGDPDPIA EQLRRVRGPV TIIAGEQVAR DDARDELERL RAILRARVAT
VPDAKDVSGA PGPGSSSALG VTGVMGHPGV AEALTASGVC LLVGTRLPAT ARAGLDAALA
ALPVLSLGSE PPYLSSLHVH TDDLRRSLTM LNAALSGSGR VGSGPQSLRS CPPDGVTVPD
RIPYTELTPP VHEGNGIRYR AAMAALDAAL PDGTDIVVDA GNTGASAIHY LPVRRGGRFV
VALGMGGMGY SFGAGIGMCF ARGHRTVIIA GDGSFFMHGM ELHTAIQYRL PVTVVLFNNN
AHAMCVTREQ LFYRDLYSYN RFTPSKLGAG LAAMFPGLPA VDVAEIGALP HALQTALDEE
GPSVVSIECS ADEIPPFAPF LETKEAHVHV
//
