ID   ILVB_MYCAV              Reviewed;         621 AA.
AC   Q59498;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Acetolactate synthase;
DE            EC=2.2.1.6;
DE   AltName: Full=ALS;
DE   AltName: Full=Acetohydroxy-acid synthase;
GN   Name=ilvB;
OS   Mycobacterium avium.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1764;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8921849; DOI=10.1016/0378-1119(96)00275-2;
RA   Gusberti L., Cantoni R., de Rossi E., Branzoni M., Riccardi G.;
RT   "Cloning and sequencing of the ilvBNC gene cluster from Mycobacterium
RT   avium.";
RL   Gene 177:83-85(1996).
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 1/4.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L49392; AAB38426.1; -; Genomic_DNA.
DR   PIR; JC5164; JC5164.
DR   AlphaFoldDB; Q59498; -.
DR   SMR; Q59498; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
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: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; cd02015; TPP_AHAS; 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-bd_C.
DR   PANTHER; PTHR18968; PTHR18968; 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; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR00118; acolac_lg; 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; FAD;
KW   Flavoprotein; Magnesium; Metal-binding; Thiamine pyrophosphate;
KW   Transferase.
FT   CHAIN           1..621
FT                   /note="Acetolactate synthase"
FT                   /id="PRO_0000090800"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..512
FT                   /note="Thiamine pyrophosphate binding"
FT   COMPBIAS        15..29
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         89
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         296..317
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         339..358
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         483
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         510
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   621 AA;  65913 MW;  F998E18CF893CF96 CRC64;
     MSAPTRRPAP DAPGAAGIAP APPAPAAKPA AGKPKRIGPE QVTGAQSVIR SLEELGVEVI
     FGIPGGAVLP VYDPLFDSKK LRHVLVRHEQ GAGHAASGYA HATGKVGVCM ATSGPGATNL
     VTALADAQMD SIPVVAVTGQ VGRTLIGTDA FQEADISGIT MPITKHNFLV VRQRNPAVLA
     EAFHIAASGR PARCSVDIPK DVLQGQCTFS WPPRIHLPGY KPTTKPHSRQ IRERAKLIAA
     ARKPVLYVGG GVIRGEASEQ LRELAELTGI PVVTTLMARG AFPDSHRQHL GMPGMHGTVA
     AVAALQRSDL LIALGTRFDD RVTGKLDTFA PEAKVIHADI DPAEIGKNRH ADVPIVGDVK
     AVIAELVEIL RHDGAPGNLD IADWWAYLDD VQSTYPLSYG PQSDGSLGPE YVIEKLGQIA
     GPDALYVAGV GHDQMWAAQF ISYEKPRTWL NSGGQGTMGF AIPAAMGAKM GRPEAEVWAI
     DGDGCFQMTN QELATCAVEG IPIKVALINN GNLGMVRQWQ TLFYEERYSQ TDLGHPLAPH
     PDFVKLAEAL GCVGLRCERE EDVVDVINAA RAINDRPVVI AFIVGADAQV WPMVAAGTSN
     DEIQAARGIR PLFDDETEGT P