ID A0A370H518_9NOCA Unreviewed; 612 AA.
AC A0A370H518;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=acetolactate synthase {ECO:0000256|ARBA:ARBA00013145};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145};
GN ORFNames=DFR68_107254 {ECO:0000313|EMBL:RDI49126.1};
OS Nocardia mexicana.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=279262 {ECO:0000313|EMBL:RDI49126.1, ECO:0000313|Proteomes:UP000255355};
RN [1] {ECO:0000313|EMBL:RDI49126.1, ECO:0000313|Proteomes:UP000255355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44952 {ECO:0000313|EMBL:RDI49126.1,
RC ECO:0000313|Proteomes:UP000255355};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) 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}.
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:RDI49126.1}.
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DR EMBL; QQAZ01000007; RDI49126.1; -; Genomic_DNA.
DR RefSeq; WP_068013794.1; NZ_QQAZ01000007.1.
DR AlphaFoldDB; A0A370H518; -.
DR STRING; 1210089.GCA_001613165_00744; -.
DR OrthoDB; 3194735at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000255355; Unassembled WGS sequence.
DR GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; 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:0019310; P:inositol catabolic process; 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; 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; IPR030817; Myo_inos_IolD.
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 NCBIfam; TIGR04377; myo_inos_iolD; 1.
DR PANTHER; PTHR18968:SF9; 3D-(3,5_4)-TRIHYDROXYCYCLOHEXANE-1,2-DIONE HYDROLASE; 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 Hydrolase {ECO:0000313|EMBL:RDI49126.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000255355};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..129
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 219..350
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 434..572
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 612 AA; 64803 MW; 5BEECF2C83706085 CRC64;
MRLTTAQALV AWMIAQHSET LDGREVPLFP AVFAIFGHGN VLGLGTALEE RRDVIPVWRG
HTEQGMALAA VGLAKATHRR QVGVATSSIG PGALNMVTAA GVAHANRLPL LLLPGDTFVN
RAPDPVLQQV EHFGDATVTV NDAFRSVSRY FDRITRPEQL LATLPQVARV LTDAAEAGPV
TLALPQDVQA ETSDFPTALF QPVVHRIDRP RPDRESLGEA ARALRAAHRP LLVLGGGVRY
SGAGGRAVEL AERHGIPIAE TTAGRTLVPH DHPLYAGPLG ITGSGSANTV AAEADLVLAV
GTRLQDFTTA SWTVFDPGVR IVAINAARYD AVKHGALSVV ADAGAALEDL APHLSDWRVD
QAWSARASAV RGEWDAYVDK LRAPAAGIPS YAQIVGVVND LSDPADYVMT SSGGMPGELV
GGWRAVGGEP TMDVEYGFSC MGYELSGAWG AAMAHRRGLV TTMLGDGSYL MLNSELFSAA
FAGHPLVAVV CDNDGYAVIA RLQEGQGGNA FNNFYRQCRT NHGRPPRVDF AAHARSLGCA
AFVATDLAEF RAAYAGARAA ALAESRPAVV VVPTQPAAWT ESGAWWEVGV PAHLPGRAAY
DDAKPRQVRY TR
//
