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Database: UniProt
Entry: U3TR91_9ENTR
LinkDB: U3TR91_9ENTR
Original site: U3TR91_9ENTR 
ID   U3TR91_9ENTR            Unreviewed;       574 AA.
AC   U3TR91;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
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=E05_01930 {ECO:0000313|EMBL:BAN94959.1};
OS   Plautia stali symbiont.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae.
OX   NCBI_TaxID=891974 {ECO:0000313|EMBL:BAN94959.1, ECO:0000313|Proteomes:UP000016901};
RN   [1] {ECO:0000313|EMBL:BAN94959.1, ECO:0000313|Proteomes:UP000016901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21470838; DOI=10.1016/j.micres.2011.03.001;
RA   Kobayashi H., Kawasaki K., Takeishi K., Noda H.;
RT   "Symbiont of the stink bug Plautia stali synthesizes rough-type
RT   lipopolysaccharide.";
RL   Microbiol. Res. 167:48-54(2011).
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; AP012551; BAN94959.1; -; Genomic_DNA.
DR   AlphaFoldDB; U3TR91; -.
DR   KEGG; psts:E05_01930; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_1_2_6; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000016901; 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:UP000016901};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591}.
FT   DOMAIN          5..119
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          196..330
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          394..545
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   574 AA;  62737 MW;  0750585E592F55AF CRC64;
     MEMLSGAEMV VRSLIDQGVK QVFGYPGGAV LDIYDALQTV GGIDHVLVRH EQGAVHMADG
     LARATGEVGV VLVTSGPGAT NAITGIATAY MDSIPLVILS GQVLSSLIGY DAFQECDMVG
     ISRPVVKHSF LVKSTEEIPT VLKKAFWLAA SGRPGPVVID LPKDILNPAN KLPYVWPETV
     SMRSYNPTLQ GHKGQIKRAL QTLLAAHKPV IYVGGGAITS GCEAELLQLA EQLNIPVTTS
     LMGLGAFPGT HRQCVGMLGM HGTYEANMTM HNADLIFGIG VRFDDRTTNN LAKYCPNATV
     MHIDVDPTSI SKTVSADIPI VGDARQTLTQ MLELLAQSEA KQELDSLRDW WQSIEGWRSR
     KCLEFDRTSD KIKPQAVIET IRRLTHGEAY VTSDVGQHQM FAALYYQFDK PRRWINSGGL
     GTMGFGLPAA LGVKMALPQE TVICVTGDGS IQMNIQELST ALQYDLPVLV LNLNNRFLGM
     VKQWQDMIYS GRHSQSYMES LPDFVRLAEA YGHVGIAIKH PAELEEKLQL ALDTLAKGRL
     VFVDVTVDGS EHVYPMQIRG GAMDEMWLSK TERT
//
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