ID A0A0G1U991_9BACT Unreviewed; 602 AA.
AC A0A0G1U991;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KKU90624.1};
GN ORFNames=UY21_C0021G0024 {ECO:0000313|EMBL:KKU90624.1};
OS Microgenomates group bacterium GW2011_GWA1_48_10.
OC Bacteria.
OX NCBI_TaxID=1618496 {ECO:0000313|EMBL:KKU90624.1, ECO:0000313|Proteomes:UP000034718};
RN [1] {ECO:0000313|EMBL:KKU90624.1, ECO:0000313|Proteomes:UP000034718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(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:KKU90624.1}.
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DR EMBL; LCPD01000021; KKU90624.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1U991; -.
DR PATRIC; fig|1618496.3.peg.939; -.
DR Proteomes; UP000034718; 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: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.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..112
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 202..337
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 409..551
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 602 AA; 67313 MW; FE33F1C1C696AC06 CRC64;
MKVKLSDYVV SWLEQKGVRD VFMISGGGIM HLVDSVGRAK KLKYICTQHE QAAAIAAESY
ARLKGLGVCI VTTGPGGTNT ITGVSGAWLD SVPMLVIAGQ VNLSMTAKST GIKGLRQLGD
QEENLVEIIA PITKYAATVE SPEDIEYHLE KALYLATHGR FGPAFVEIPL NIQGSYITEH
KLRKFVAPPL RAKRAQLKKL VRKTIVRLRE ARRPVLLAGN GIRWAGAGKE LQELIQALKI
PVLASVVGYD LVPSSNPYYA GRPGTFGQRA ANFVIQNSDF LLSIGSRLHL YLVTYNYRAF
AREAFKVVVD IDPAELKKPT IKPDISVNAD AKEFIEEMLR QLRKKPLRLK IAEWWQYAKE
LNKKYPVVLP EYWRQKKYVN SYCFVDRLSR VMNPGEVIVV SDGTPLTCTH QALIVKRGQR
LISNLGCAAM GYGLPAAVGA CLANKKRRVI CLEGDGSIQL NLQELQTMKY YNLPIKLFIY
ENEGYLSIKI TQDNYMNGRR VASDPTSGVG YPDFLKVARA YGFRTVKMNT NRDIDTGIKK
VLSYPGPVVC VIKMAPDQPI IPKSKADKRP DGTILAKPLE DMYPFLDRKE FLENMIIKPW
RM
//
