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Database: UniProt
Entry: A0A0U2UCT5_9BACL
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ID   A0A0U2UCT5_9BACL        Unreviewed;       579 AA.
AC   A0A0U2UCT5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Acetolactate synthase {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
DE            EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
GN   ORFNames=IJ22_37340 {ECO:0000313|EMBL:ALS24072.1}, PN4B1_21950
GN   {ECO:0000313|EMBL:GCL72290.1};
OS   Paenibacillus naphthalenovorans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=162209 {ECO:0000313|EMBL:ALS24072.1, ECO:0000313|Proteomes:UP000061660};
RN   [1] {ECO:0000313|Proteomes:UP000061660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=32O-Y {ECO:0000313|Proteomes:UP000061660};
RA   Butler R.III., Wang J., Stark B.C., Pombert J.-F.;
RT   "Complete genome sequences of two moderately thermophilic Paenibacillus
RT   species.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALS24072.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=32O-Y {ECO:0000313|EMBL:ALS24072.1};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ALS24072.1, ECO:0000313|Proteomes:UP000061660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=32O-Y {ECO:0000313|EMBL:ALS24072.1,
RC   ECO:0000313|Proteomes:UP000061660};
RX   PubMed=26868401;
RA   Butler R.R.III., Wang J., Stark B.C., Pombert J.F.;
RT   "Complete Genome Sequences of Two Interactive Moderate Thermophiles,
RT   Paenibacillus napthalenovorans 32O-Y and Paenibacillus sp. 32O-W.";
RL   Genome Announc. 4:e01717-15(2016).
RN   [4] {ECO:0000313|EMBL:GCL72290.1, ECO:0000313|Proteomes:UP000299945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B1 {ECO:0000313|EMBL:GCL72290.1,
RC   ECO:0000313|Proteomes:UP000299945};
RA   Ha-Thanh L.T., Ngoc-Thi T.V., Shintani M., Moriuchi R., Dohra H.,
RA   Hoang-Loc N., Kimbara K.;
RT   "Isolation and characterization of a moderate thermophilic Paenibacillus
RT   naphthalenovorans strain 4B1 capable of degrading dibenzofuran from dioxin-
RT   contaminated soil in Vietnam.";
RL   Submitted (MAR-2019) 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         ECO:0000256|RuleBase:RU003591};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU003591};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU003591};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|RuleBase:RU003591};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000256|RuleBase:RU003591};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004974, ECO:0000256|RuleBase:RU003591}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025,
CC       ECO:0000256|RuleBase:RU003591}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU003591}.
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DR   EMBL; CP013652; ALS24072.1; -; Genomic_DNA.
DR   EMBL; BJCS01000005; GCL72290.1; -; Genomic_DNA.
DR   RefSeq; WP_062409841.1; NZ_FNDY01000042.1.
DR   AlphaFoldDB; A0A0U2UCT5; -.
DR   STRING; 162209.IJ22_37340; -.
DR   KEGG; pnp:IJ22_37340; -.
DR   PATRIC; fig|162209.4.peg.3977; -.
DR   OrthoDB; 4494979at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000061660; Chromosome.
DR   Proteomes; UP000299945; Unassembled WGS sequence.
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:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
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   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; 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_TPP-bd.
DR   NCBIfam; TIGR00118; acolac_lg; 1.
DR   PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE, CHLOROPLASTIC; 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   ECO:0000256|RuleBase:RU003591};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|RuleBase:RU003591}; FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061660};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591}.
FT   DOMAIN          24..138
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          213..347
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          405..553
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   579 AA;  63352 MW;  C796500C0FC2F9E5 CRC64;
     MIVQTKQKSK EQLREELLKP DVITGSEMLL RSLLLEDVDC VFGYPGGAVL YIYDAMHGNP
     DFRHLLTRHE QGAIHAADGY ARSTGKVGVC IATSGPGATN LVTGIATAYM DSVPLVVITG
     NVATTVIGTD AFQEADITGI TMPITKHSYL VRDVKDLPRI IKEAFHIAST GRKGPVLIDI
     PKDVSNDTAP FYYPEKVDIR GYHPTVQPHK LQVDRMLEAI AESERPVIIA GGGVVYADAS
     KELIEFVEKT RIPVATTLLG LGGFPSAHEL WLGMPGMHGT YAANHALQNC DLLIGIGARF
     DDRVTMKVNG FAPKAKKIVH IDVDPAEIGK IVETAIPVVG DVKKVLQLAN LKAKPSQSKD
     WIAWNQENKK NFPLTYQDSD TELKPQYVIE MINETTKGEA IITTDVGQHQ MWTAQYYKFN
     HPRSWITSGG LGTMGFGFPS AIGAQVAHPD RLVISINGDG GMQMCSQELA ICAINQIPVK
     IVVINNQVLG MVRQWQEIIY DNRYSHIDLA GSPDFVKLAE AYGVKGLRAA NKEDARRVWQ
     EALDTPGPVL VEFIVPKGEN VFPMVTQGST IDQMIMGDS
//
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