ID H8IQV4_MYCIA Unreviewed; 605 AA.
AC H8IQV4;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=acetolactate synthase {ECO:0000256|ARBA:ARBA00013145};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145};
GN OrderedLocusNames=OCU_42910 {ECO:0000313|EMBL:AFC45510.1};
OS Mycobacterium intracellulare (strain ATCC 13950 / DSM 43223 / JCM 6384 /
OS NCTC 13025 / 3600).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=487521 {ECO:0000313|EMBL:AFC45510.1, ECO:0000313|Proteomes:UP000008004};
RN [1] {ECO:0000313|EMBL:AFC45510.1, ECO:0000313|Proteomes:UP000008004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13950 / DSM 43223 / JCM 6384 / NCTC 13025 / 3600
RC {ECO:0000313|Proteomes:UP000008004};
RX PubMed=22535933; DOI=10.1128/JB.00295-12;
RA Kim B.J., Choi B.S., Lim J.S., Choi I.Y., Lee J.H., Chun J., Kook Y.H.,
RA Kim B.J.;
RT "Complete genome sequence of Mycobacterium intracellulare strain ATCC
RT 13950T.";
RL J. Bacteriol. 194:2750-2750(2012).
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; CP003322; AFC45510.1; -; Genomic_DNA.
DR AlphaFoldDB; H8IQV4; -.
DR KEGG; mia:OCU_42910; -.
DR PATRIC; fig|487521.10.peg.4299; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_11; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000008004; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 32..142
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 234..334
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 410..564
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 359..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 605 AA; 62571 MW; 6602BBF2A54ED62D CRC64;
MAAGERFMYW IWTTMNRPGR YLVSSGMLGR HRVVDHIVGH LAAIGVDHIF GVDGANIEDV
YDAAHFCPDI DAVLAKHEFS AATMADGYSR SGAGVGVVAA TSGGGALNLV AGLGESLASR
VPVLALVGQP ARTMDGRGSF QDTSGANGSL NAEALFSAVS VFCERLLTPA DIVSLLPRAI
AAARIGGPAV LLLPKDIQQA HLDAGRDDND ADGMRAAIGN PHPIVAELRR VQGRVTILAG
EQVARDDARA ELEELRALLH ARVATVPDAK DVAAADGGPA ALGVTGVMGH RNVAEAVATS
AVCLIVGTRL AVTARGGLDE ALAAVRTVSI GSAPPYLPCT HVHTDDLRGS LRALTHAVRH
RGRPAGPRIP GAGRPAEMTP PPFTGPGVRY REAMAVLDDV VPDGSDIVVD AGNTGAAAIH
YLPVRRGGRF AVALGMGGMG YSFGAGIGMT LGRANTGRPA GRTVVIAGDG AFFMHGMEVH
TAVQYRLPMT FVLFNNNAHA MCVTREQLFY DDLYSYNRFR PSRLGAGLAA MFPGLAAVDV
SDADGFAAAM GAALDIDGPA VVSVECAADE IPPFAPFLTA APAKGRGVDQ ISLAEENLTN
VAASA
//
