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
//