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Database: UniProt
Entry: A0A172TRN3_9BACT
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Original site: A0A172TRN3_9BACT 
ID   A0A172TRN3_9BACT        Unreviewed;       581 AA.
AC   A0A172TRN3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, 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=SY85_03440 {ECO:0000313|EMBL:ANE49690.1};
OS   Flavisolibacter tropicus.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Flavisolibacter.
OX   NCBI_TaxID=1492898 {ECO:0000313|EMBL:ANE49690.1, ECO:0000313|Proteomes:UP000077177};
RN   [1] {ECO:0000313|Proteomes:UP000077177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCS9 {ECO:0000313|Proteomes:UP000077177};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Flavisolibacter sp./LCS9/ whole genome sequencing.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ANE49690.1, ECO:0000313|Proteomes:UP000077177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCS9 {ECO:0000313|EMBL:ANE49690.1,
RC   ECO:0000313|Proteomes:UP000077177};
RX   PubMed=27259556; DOI=10.1099/ijsem.0.001207;
RA   Lee J.J., Kang M.S., Kim G.S., Lee C.S., Lim S., Lee J., Roh S.H., Kang H.,
RA   Ha J.M., Bae S., Jung H.Y., Kim M.K.;
RT   "Flavisolibacter tropicus sp. nov., isolated from tropical soil.";
RL   Int. J. Syst. Evol. Microbiol. 66:3413-3419(2016).
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; CP011390; ANE49690.1; -; Genomic_DNA.
DR   RefSeq; WP_066401824.1; NZ_CP011390.1.
DR   AlphaFoldDB; A0A172TRN3; -.
DR   STRING; 1492898.SY85_03440; -.
DR   KEGG; fla:SY85_03440; -.
DR   PATRIC; fig|1492898.3.peg.749; -.
DR   OrthoDB; 4494979at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000077177; Chromosome.
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:UP000077177};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591, ECO:0000313|EMBL:ANE49690.1}.
FT   DOMAIN          23..138
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          214..347
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          410..557
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   581 AA;  63636 MW;  187827B6E5C10401 CRC64;
     MQTFDTVKAG SLEQVSLKTE SISGSEAVLD AFLHEGVTTI FGYPGGAIMP IYDALYDYQD
     KLEHILVRHE QGAIHAAQGF ARTSGKTGVV FATSGPGATN LVTGLADAMI DSTPLVCITG
     QVFAHLLGTD AFQETDIINI TTPITKWNYQ ITDATEIPTV LAKAFFIACS GRPGPVLIDI
     SKNAQLQKFD YKGYQKCEFI RSYRPKPFVR QEYVEQAADL INKAKKPLVV FGQGVILGKA
     EKEFQDFIEK AGLPAAWTIM GLSALPSGHP LNVGMLGMHG NYAPNVLTNE CDVLIAVGMR
     FDDRVTGRLD KYAKQAKIIH LDIDPAEIDK NVKTTVSVWG DCKETLPLLI QLLNHNQHPE
     WLQTFKALEQ KEIDACIQNE LHPTGEQMTM GEVIDVLNEL TEGKAVIVTD VGQHQMVACR
     YAQFNQSKSN ITSGGLGTMG FALPAAIGAK FGAPNQTVIA IMGDGGVQMT IQELGTIMQS
     QVDVKLLILN NQFLGMVRQW QELFHGKRYS FVDIESPDFV QVAKGYGIPG QRVTARENLK
     EALKAMLEYK GAYLLEVMVG KENNVFPMVE AGTSVSEIRL K
//
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