ID A0A106BJ42_THIDE Unreviewed; 553 AA.
AC A0A106BJ42;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KVW93411.1};
GN ORFNames=ABW22_14920 {ECO:0000313|EMBL:KVW93411.1};
OS Thiobacillus denitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=36861 {ECO:0000313|EMBL:KVW93411.1, ECO:0000313|Proteomes:UP000064243};
RN [1] {ECO:0000313|EMBL:KVW93411.1, ECO:0000313|Proteomes:UP000064243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RG {ECO:0000313|EMBL:KVW93411.1,
RC ECO:0000313|Proteomes:UP000064243};
RX PubMed=26712544;
RA Harrold Z.R., Skidmore M.L., Hamilton T.L., Desch L., Amada K.,
RA van Gelder W., Glover K., Roden E.E., Boyd E.S.;
RT "Aerobic and Anaerobic Thiosulfate Oxidation by a Cold-Adapted, Subglacial
RT Chemoautotroph.";
RL Appl. Environ. Microbiol. 82:1486-1495(2015).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KVW93411.1}.
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DR EMBL; LDUG01000048; KVW93411.1; -; Genomic_DNA.
DR RefSeq; WP_059758532.1; NZ_LDUG01000048.1.
DR AlphaFoldDB; A0A106BJ42; -.
DR STRING; 1123392.GCA_000376425_01490; -.
DR PATRIC; fig|36861.3.peg.2807; -.
DR OrthoDB; 2254214at2; -.
DR Proteomes; UP000064243; Unassembled WGS sequence.
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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000064243};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..113
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..332
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 399..529
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 553 AA; 60153 MW; 68DA0319F5C4ECA1 CRC64;
MNISVSELIV RYLERLGIDH IFGMPGAHVL PIYDCLHDSK VKSVLVKHEQ GAAFMAGGLA
RVSHRPAACI ATAGPGATNL ITGIANAYAE RLPVLAITGE TSTYIFGRGG LQESSGEGGA
IDQGALFASI TRYHKLVERT DYLGQVLNQA TQALLGREPG PVLLSIPYNV QKEMIDEDVI
EQIHFPGKAA IRHTTPTAEF TELLRAAHHP VIVAGYGCIQ AGARDVVAAF SERFNIPVTT
SLKAKGVVAE GTPLSLGCLG VTSNGEAYRY LVDHADLLIF LGAGFNERTS YLWDAKLLRG
KKIAQVDRDA AQIGRVFQPD VSICGDILAV MEDVFDVLEA DDMPPKSRDL LDGHQAAVSQ
PADDSAAQAQ PFRLMQAFFR GLAQRFPHNA LVFDDNIIFA QSYFDVSDRN HYFPNSGISS
LGHAIPAAIG ARCFAKDSPT FAILGDGGFQ MCCMEMMTAV NYGIPLNVVV INNGTLSLIR
KNQFQLYGER YIDCDFTNPD FGLLAQSFGV NHYRIETEAD LDRLFAEADL TGTINLIEIL
LDKHAFPRYL SAR
//
