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Database: UniProt
Entry: A0A0N1C2D2_9SPHN
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ID   A0A0N1C2D2_9SPHN        Unreviewed;       582 AA.
AC   A0A0N1C2D2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=IP83_05765 {ECO:0000313|EMBL:KPF88362.1};
OS   Novosphingobium sp. AAP93.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1523427 {ECO:0000313|EMBL:KPF88362.1, ECO:0000313|Proteomes:UP000037906};
RN   [1] {ECO:0000313|EMBL:KPF88362.1, ECO:0000313|Proteomes:UP000037906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP93 {ECO:0000313|EMBL:KPF88362.1,
RC   ECO:0000313|Proteomes:UP000037906};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-2015) 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}.
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:KPF88362.1}.
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DR   EMBL; LJHZ01000027; KPF88362.1; -; Genomic_DNA.
DR   RefSeq; WP_054121260.1; NZ_LJHZ01000027.1.
DR   AlphaFoldDB; A0A0N1C2D2; -.
DR   STRING; 1523427.IP83_05765; -.
DR   PATRIC; fig|1523427.4.peg.1802; -.
DR   OrthoDB; 4494979at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000037906; 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   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591}.
FT   DOMAIN          6..121
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          195..332
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          395..542
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   582 AA;  62996 MW;  6EC1E6E86774E4CF CRC64;
     MKNERSGAEI LVESLVAQGV ECVFGYPGGA VLPIYDALFG DERIRHILVR HEAGAAHAAE
     GYARATGKPG VVLVTSGPGA TNAVTGIADA FMDSIPLVVL TGQVPTALIG SDAFQECDTV
     GITRHCTKHN YLVKDPAQLG EVVEEAFRIA TEGRPGPVVI DIPKDVQIGL APWTGKPARI
     RTRYNPQIEG SREDIAQAVQ MIAAAQAPIF YTGGGVINSG PEATALLREL QALTGAPVTS
     TLMGLGAFPA DHPAWLGMLG MHGTYEANMA MNRADLIVAI GARFDDRVTG RLDAFSPNSK
     RIHIDIDRAS INKTVRADLP IVGDCAKVLR QLIDAWHAAH HEAADLAEWY ARIDGWRARQ
     SLAYPHRKEA IMPQYAVERL YELTRRHDPI ITTEVGQHQM WAAQYFHFSG PNKWLTSGGL
     GTMGYGLPAA IGAQVGFPDA LVIDIAGDAS IQMNIQELGT ATQYRLPVKI FVLNNEWMGM
     VRQWQELTYE SRYSNSYSDS LPDFVKLAEA YGWKGIRITD ESELDAGIQA MIDHPGPVFV
     DCLVAKEVNC FPMIPSGAAH TDMILYGDSV AGTMDDAAKA LV
//
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