ID U5N848_9BURK Unreviewed; 585 AA.
AC U5N848;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:AGX87485.1};
GN ORFNames=Cenrod_1398 {ECO:0000313|EMBL:AGX87485.1};
OS Candidatus Symbiobacter mobilis CR.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=946483 {ECO:0000313|EMBL:AGX87485.1, ECO:0000313|Proteomes:UP000017184};
RN [1] {ECO:0000313|EMBL:AGX87485.1, ECO:0000313|Proteomes:UP000017184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR {ECO:0000313|EMBL:AGX87485.1};
RX PubMed=24267588; DOI=10.1186/gb-2013-14-11-r127;
RA Liu Z., Muller J., Li T., Alvey R.M., Vogl K., Frigaard N.U.,
RA Rockwell N.C., Boyd E.S., Tomsho L.P., Schuster S.C., Henke P., Rohde M.,
RA Overmann J., Bryant D.A.;
RT "Genomic analysis reveals key aspects of prokaryotic symbiosis in the
RT phototrophic consortium "Chlorochromatium aggregatum".";
RL Genome Biol. 14:R127-R127(2013).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP004885; AGX87485.1; -; Genomic_DNA.
DR RefSeq; WP_022772870.1; NC_022576.1.
DR AlphaFoldDB; U5N848; -.
DR STRING; 946483.Cenrod_1398; -.
DR KEGG; cbx:Cenrod_1398; -.
DR PATRIC; fig|946483.4.peg.1409; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_1_3_4; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000017184; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd00568; TPP_enzymes; 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:SF142; ACETOLACTATE SYNTHASE; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000017184};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..332
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 391..537
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 585 AA; 63545 MW; EA55E253A4B349A9 CRC64;
MKYSDLLAKW LRNMGYTHCF FVPGGNVMHL VASCSAHFRM VGVVHEVAAG IAAEYFNEAH
PQEKAFALVT AGPGLTNVVT ALAGAFLESR ELLVLGGQVK TADLRDLWLR QRGIQEIDGV
RIAEPVCCVA RRLDAPVSLA SFQRWVGNVG SPRPGPVFLE LPLDVQARSV DEASLERADP
AEGLHPVIPL AGASVKTALV ERIRAAERPV LLLGGGVSRK TMRTVYAQLE AMGIPLMTTW
NGADRVGAEH PLYFGRPNTW GQRYANVLLQ KCDLLVALGT RLGLQQTGFR WQEFVPEGEV
LQVEIDPAEL SKGHPHVEWP VLGDANDVLR HLAGSHLGDH TAWVRCCSKV RDALPLVEPN
HTGAGYVSPY RFYEEIAGWC RAEDVVIPCS SGCAYTVAMQ VFAQRWGQTI ITNKGLASMG
YGLSGAIGAA LAHPDRRTIL FEGDGGFAQN LQELGTVVAN RLSLKIFLFD DQGYASIRMT
QQSYFAGRFV GCEVQGGLGL PPWDKLFAAY GIPVLRIDGP VADCPGFAEA FEAPGPCAFV
LAIDPAQTYF PKITSRVAAD GTMQSNPLHR MTPEVPDIDW AAYCK
//
