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
//