ID A0A0M2ZM92_9MYCO Unreviewed; 570 AA.
AC A0A0M2ZM92; A0A1A0R1T5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=acetolactate synthase {ECO:0000256|ARBA:ARBA00013145};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145};
GN ORFNames=BST23_01575 {ECO:0000313|EMBL:ORA69366.1};
OS Mycolicibacterium elephantis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=81858 {ECO:0000313|EMBL:ORA69366.1, ECO:0000313|Proteomes:UP000192772};
RN [1] {ECO:0000313|EMBL:ORA69366.1, ECO:0000313|Proteomes:UP000192772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FI-09383 {ECO:0000313|EMBL:ORA69366.1,
RC ECO:0000313|Proteomes:UP000192772};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (FEB-2017) 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 -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:ORA69366.1}.
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DR EMBL; MVHP01000001; ORA69366.1; -; Genomic_DNA.
DR RefSeq; WP_046749963.1; NZ_MVHP01000001.1.
DR AlphaFoldDB; A0A0M2ZM92; -.
DR STRING; 81858.BST23_01575; -.
DR OrthoDB; 4494979at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000192772; 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; cd02004; TPP_BZL_OCoD_HPCL; 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:SF166; 2-HYDROXYACYL-COA LYASE 2; 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 6..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..330
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 399..544
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 570 AA; 62384 MW; 3E194C4330F39837 CRC64;
MGVPVYKRIL DLFEAEGVNT LFGIPDPNFV HMFAEAEARG WSVVAPHHEL SAGFMAEAAS
RMTGKPGLCI GTLGPGMANI AGAIQCALVE NSPVIFLGGQ RARITERRVR RGRIQFVQQE
PLFEASVKYS SSIEYADQTD EIIHEAIRRS MSGTPGPSYV EFPSHVILEE LDVADPPPPN
RYRLVNQGAG AREVAEAAKL IREAKSPILL VGHGVHTSRT QQEVKELAEL MACPVIQTSG
GTSYIPGLQD RTFPYLFSPA ANEAVEESDL CVALGTELGE PMHYGRTQHW AANDANRRWV
YVEQDPAAIG VNRSFDVPLV GDLRGVVPQL VEALRDTPRE PSANLDKLVK ADAEELAQLA
ENAPSGRTPI HPARFVVEAT KAFNELEDGI MVRDGGATVI FQWTYSQSKP RDVIWNQNFG
HLGTGLPYAV GASIAEGRKR PVMLLTSDSS FLFHIAELET AAREGVPLVC VVGVDHQWGL
EVGVYKRTFP QPSPQPGVHW SKDVRMDKIA VGFGCHGEYV EKDDELGPAI ARAYASGKVG
VVHVCIDPKA NSEEMPKYDR FRTWYAEGTQ
//