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Database: UniProt
Entry: A0A2U3P5T3_9MYCO
LinkDB: A0A2U3P5T3_9MYCO
Original site: A0A2U3P5T3_9MYCO 
ID   A0A2U3P5T3_9MYCO        Unreviewed;       548 AA.
AC   A0A2U3P5T3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, 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=MNAB215_1293 {ECO:0000313|EMBL:SPM39111.1};
OS   Mycobacterium numidiamassiliense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1841861 {ECO:0000313|EMBL:SPM39111.1, ECO:0000313|Proteomes:UP000240424};
RN   [1] {ECO:0000313|EMBL:SPM39111.1, ECO:0000313|Proteomes:UP000240424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB215 {ECO:0000313|EMBL:SPM39111.1,
RC   ECO:0000313|Proteomes:UP000240424};
RG   Urmite Genomes;
RL   Submitted (JAN-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   -!- 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; FUEZ01000003; SPM39111.1; -; Genomic_DNA.
DR   RefSeq; WP_077077966.1; NZ_FUEZ01000003.1.
DR   AlphaFoldDB; A0A2U3P5T3; -.
DR   STRING; 1841861.GCA_900157365_05496; -.
DR   OrthoDB; 4494979at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000240424; 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; cd02010; TPP_ALS; 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; IPR000399; TPP-bd_CS.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF129; ACETOLACTATE SYNTHASE; 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.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000240424};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          3..117
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          189..322
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          381..525
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   548 AA;  59647 MW;  B22BF90C06C51FF1 CRC64;
     MTKAARLMVE CLENEGVAVV FGLPGEENIR FVQALASSKI RYVLTRHEQA AAFMAEMYGR
     VTGRAAVVSA TLGPGAINMQ LGVADATTNS TPMVAISAQV GQDRQYKESH QYVDLVSMFA
     PITRWAAGVP TVRAIPEMFR KAFKLAETER PAAVYLAVPE HIDADEADYD LSPLPRNVVR
     ADAPAPGQVE RAVDILRAAK RPVVLAGHGA ARSDATAALV RFSERFGVPV ANTFHGKGVM
     PDDHPNSIGT LGFMRHDYVN FGFDNADVII AVGYELQEFD PVRINPQADK KIIHIHRFPA
     EVDAHYSVDV GIIGDISDSL DAVADGLADH TYEAEPEVPG SGLLAEEFAR GQQDSRYPLA
     PARVVADTRE ALGRSDVVLV DTGATKMWMA RLYPTYERNT CLISNGLSTM GFALPGALGV
     KLARPEAKVL AVVGDGAFLM NSQEIETAVR ERIPLVVLIW EDGGYGLIEW KMDLELGEHY
     YVKFGNPDIL QYAESFGAKG YRINSAEELL PTLRAALDDD GVSLICCPVD YSENLRLTDR
     LGELDETL
//
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