ID M6ZZ00_9ACTN Unreviewed; 524 AA.
AC M6ZZ00;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=acetolactate synthase {ECO:0000256|ARBA:ARBA00013145};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145};
GN ORFNames=ISGA_2072 {ECO:0000313|EMBL:EMP11668.1};
OS Gordonia sp. NB41Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=875808 {ECO:0000313|EMBL:EMP11668.1, ECO:0000313|Proteomes:UP000011989};
RN [1] {ECO:0000313|EMBL:EMP11668.1, ECO:0000313|Proteomes:UP000011989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB4-1Y {ECO:0000313|EMBL:EMP11668.1,
RC ECO:0000313|Proteomes:UP000011989};
RX PubMed=23744905; DOI=10.1099/mic.0.068932-0;
RA Van Hamme J.D., Bottos E.M., Bilbey N.J., Brewer S.E.;
RT "Genomic and proteomic characterization of Gordonia sp. NB4-1Y in relation
RT to 6 : 2 fluorotelomer sulfonate biodegradation.";
RL Microbiology 159:1618-1628(2013).
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:EMP11668.1}.
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DR EMBL; APHK02000061; EMP11668.1; -; Genomic_DNA.
DR AlphaFoldDB; M6ZZ00; -.
DR STRING; 1241906.ISGA_2072; -.
DR PATRIC; fig|1241906.3.peg.3364; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000011989; 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; 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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF167; 2-KETOARGININE DECARBOXYLASE ARUI-RELATED; 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:UP000011989};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 191..318
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 384..518
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 524 AA; 54049 MW; 82D768D06DA8F84F CRC64;
MITTGGEALV RALAAQGADT VFGIPGTHNL GAYSALERVG LRHVLVRHEQ GAGYAADGYA
RSTGRPGVVL TTTGPAILNA VSSAAQAYSD SVPVFFVSPG MPSNHPGFGN GLLHEIRDQT
ASMAAVVHRA VRVSQVSEIP AAVAQLWGEM IDGRPRPVYL EIPLDLFDVT AEIDDYPRAV
TAQHVAADDA IERAAAAITA AQSPIVVVGG GAGSASEQVT ALAERIGAPV LTTTNGKGAV
ADDHPLLVGA GVQHACVRAL VESSDLLVAI GTELAPADWW YGQPTISSMV RLDIDPAGIH
ANRAADVAVL GDIADSAPRL ARRLPARDTA TTIDEIRATI TAEARATGAT WGPLVDALVA
ATPRETVIAA DNAMAVYYGT LSNWPLHRAR SFLFPTGAGT LGFGLPAGIG AKVADPDAPV
IVIQGDGGTM FTVAELATAA ELRLPLPIIV VDNGGYGEIR NEMADRDEPV HAVDLGHPDF
VALARSVGCH GVGAQEPDDV AAAVVEALKA DRPTVIHVRE GARA
//
