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Database: UniProt
Entry: F4CQY9_PSEUX
LinkDB: F4CQY9_PSEUX
Original site: F4CQY9_PSEUX 
ID   F4CQY9_PSEUX            Unreviewed;       578 AA.
AC   F4CQY9;
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:AEA23688.1};
DE            EC=2.2.1.6 {ECO:0000313|EMBL:AEA23688.1};
GN   OrderedLocusNames=Psed_1449 {ECO:0000313|EMBL:AEA23688.1};
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:AEA23688.1, ECO:0000313|Proteomes:UP000007809};
RN   [1] {ECO:0000313|EMBL:AEA23688.1, 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; AEA23688.1; -; Genomic_DNA.
DR   RefSeq; WP_013673623.1; NC_015312.1.
DR   AlphaFoldDB; F4CQY9; -.
DR   STRING; 675635.Psed_1449; -.
DR   KEGG; pdx:Psed_1449; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_3_11; -.
DR   OMA; PGPYGCL; -.
DR   OrthoDB; 4494979at2; -.
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; cd02004; TPP_BZL_OCoD_HPCL; 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; 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:SF166; 2-HYDROXYACYL-COA LYASE 2; 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:AEA23688.1}.
FT   DOMAIN          1..117
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          222..348
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          419..564
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   578 AA;  59789 MW;  AFB8953B0C64832D CRC64;
     MHGGDQVADV LSAQGVHALF TLCGGHISPI LVGAKARGIR IVDTRHEATA VFAADAVARL
     TGRPGVAAVT AGPGLTNTVT AVKNAQLAQS PVVLLGGAAP TVLQGRGALQ DIDQMALLRP
     HVKWSYAVRR VRDIGPAVEE AFRSALSGVP GPVFVELPID LLYDEVVVRQ WYGAARSGRS
     LGERAVQAYL KARVARMFSG AGRNRPGPAV DVPAPVPAPD RVAAAAAALA KATRPVILVG
     SQAMVAPGAA DRLVPALERI GAPVFLSGTA RGLLGADHPL QARHKRRESL KAADLVVLAG
     VPADFRLDYG NHVRRGATLV SANRSSGDLR RNRRPDVAIL GDAALALAGV AAALPARDDD
     AAPSRWPEWM DVVRGRDAER EADIATQAEA GTDDGVGPVR MCVEVAAALP AGAIIVGDGG
     DIVATASYVL RPDGPLRWLD PGVFGTLGVG AGFALGAATV HPDAPLWIVF GDGSVGYSLS
     EFDTFVRHGI GVVAVVGNDA SWSQIAREQV ELLRDDVATV LAPTRYDQVA AGFGAVGLHV
     DDAAELPAAL AKAKAADGPV LVDVRLGRSD FRKGSISM
//
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