ID Q0RZD0_RHOJR Unreviewed; 597 AA.
AC Q0RZD0;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:ABG99356.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:ABG99356.1};
GN Name=ilvB6 {ECO:0000313|EMBL:ABG99356.1};
GN OrderedLocusNames=RHA1_ro08312 {ECO:0000313|EMBL:ABG99356.1};
OS Rhodococcus jostii (strain RHA1).
OG Plasmid pRHL1 {ECO:0000313|EMBL:ABG99356.1,
OG ECO:0000313|Proteomes:UP000008710}.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG99356.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP000432; ABG99356.1; -; Genomic_DNA.
DR RefSeq; WP_007296731.1; NC_008269.1.
DR AlphaFoldDB; Q0RZD0; -.
DR KEGG; rha:RHA1_ro08312; -.
DR PATRIC; fig|101510.16.peg.7656; -.
DR HOGENOM; CLU_013748_3_0_11; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000008710; Plasmid pRHL1.
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; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 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; IPR047211; POXB-like.
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; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 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 Plasmid {ECO:0000313|EMBL:ABG99356.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:ABG99356.1}.
FT DOMAIN 5..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 200..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 389..544
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 597 AA; 64865 MW; D51F5677F4DF1565 CRC64;
MASQNVADYL LERLRAWGIE HVFAYAGDGI NAILAAWARA DNRPQFVQAR HEEMCAFEAV
GYAKFTGRVG VCMATSGPGA VHLLNGLYDA KLDHVPVVAI VGQTNRTAMG GSYQQEIDLL
SLYKDVASDY VQMVTVPQQL PNVLDRAIRV ALTQRAPTAL IIPADVQELD YSPPTHEFKM
VPSSIGIDWP TTTPDDQAIM RAAEILNAGS KVAMLVGQGA RGAHEEIAQV ADLLGAGAAK
ALLGKDVLSD ELTWVTGSIG LLGTRPSYEL MTGCDTLLTI GSSFPYSQFL PEYGQARGVQ
IDIDGRMIGI RYPNEVNLVA DATTALRALI PHLIRKDDRS WREEIEANVA RWWETMDMQA
QVDGDPVNPL RLFGELSPRL PDDAIVTADS GSSANWYARQ LRFRGNMRGS LSGTLATMGP
GVPYGIGAKF AHPGRPVIVF AGDGAMQMNG LAELITVKHY WRQWDDPRLI IAILHNNDLN
QVTWEMRAMS GSPKFAESQT LPDVDYAGFA ASLGLHGDTV TGPDQLAGVW ETALSADRPT
VLDVHTDPNM PPIPPHATWE QFKSATAAVL GGDEDSWGFI KTGIKTKAQE FLPHKNT
//
