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Database: UniProt
Entry: F4CPQ9_PSEUX
LinkDB: F4CPQ9_PSEUX
Original site: F4CPQ9_PSEUX 
ID   F4CPQ9_PSEUX            Unreviewed;       549 AA.
AC   F4CPQ9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:AEA26092.1};
DE            EC=2.2.1.6 {ECO:0000313|EMBL:AEA26092.1};
GN   OrderedLocusNames=Psed_3925 {ECO:0000313|EMBL:AEA26092.1};
OS   Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS   CB1190).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA26092.1, ECO:0000313|Proteomes:UP000007809};
RN   [1] {ECO:0000313|EMBL:AEA26092.1, ECO:0000313|Proteomes:UP000007809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC   {ECO:0000313|Proteomes:UP000007809};
RX   PubMed=21725009; DOI=10.1128/JB.00415-11;
RA   Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA   Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA   Alvarez-Cohen L.;
RT   "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT   strain CB1190.";
RL   J. Bacteriol. 193:4549-4550(2011).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP002593; AEA26092.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4CPQ9; -.
DR   STRING; 675635.Psed_3925; -.
DR   KEGG; pdx:Psed_3925; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_1_11; -.
DR   OMA; CVNGSHE; -.
DR   Proteomes; UP000007809; Chromosome.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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: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   Reference proteome {ECO:0000313|Proteomes:UP000007809};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000313|EMBL:AEA26092.1}.
FT   DOMAIN          6..106
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          186..320
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          388..535
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   549 AA;  58350 MW;  9F54200CFE21C850 CRC64;
     MNAAVNVAQA AAEVLRREGV EHLFAYPLNP LIDAAAAVGI RPVVVRQERV GIHMADAVSR
     LGDTVGVFCM QAGPGVENSF GAVAQAFAEG IPLVVIPGGA PRAQTWVQPA FNAALNFQHV
     TKWAEQVTTG AGLVPALRRA FTQARNGRPG PVLLEIPGDV WAEDAPGVEE YVPSRRARST
     PDADAVDAAA AALVAAERPL IYAGQGVHHA RAWTGLRELA ELLEAPVTTS LEGKSAFPET
     HPLALGSGGV AMPRAVFEHV RDADVVFGVG ASFTATGFGI RFPTAGRTFV HNTVDAVDLD
     KNVPAAHALV GDAGLTLATL TDAVRDRLRG RARGRADEVA ARIRAQNDPW LAGWRPHLDS
     DAVPLSPYRV IRDLMATVDV ARTIITHDAG SPRDELSPFW RTEAPHTYLG WGKSTQLGYG
     LGLAMGAKLA RPDMLCVNVW GDAAIGMTGM DLETCARVGI PILSVLFNNF AMAMEDRIMA
     VSRERYASTD ISGDYAAMAR AFGLHGERVT APSDIVPALR RARTAVDGGT PALVEFVTTR
     DKCYSTFQS
//
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