ID A0A1F6BUF6_9BACT Unreviewed; 590 AA.
AC A0A1F6BUF6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3A21_03010 {ECO:0000313|EMBL:OGG40468.1};
OS Candidatus Jorgensenbacteria bacterium RIFCSPLOWO2_01_FULL_45_25b.
OC Bacteria; Candidatus Jorgensenbacteria.
OX NCBI_TaxID=1798471 {ECO:0000313|EMBL:OGG40468.1, ECO:0000313|Proteomes:UP000176996};
RN [1] {ECO:0000313|EMBL:OGG40468.1, ECO:0000313|Proteomes:UP000176996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGG40468.1}.
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DR EMBL; MFKK01000024; OGG40468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6BUF6; -.
DR STRING; 1798471.A3A21_03010; -.
DR Proteomes; UP000176996; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 34..152
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 230..362
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 427..577
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 590 AA; 65546 MW; DCCDBD5033087AF0 CRC64;
MEAEYKTGRR YTKHDRVISK KTMENSEDSK KEVSVARYLV SKIEELGIDT VPVIQGGAIM
KMIDEVGESK KLHYICPNHE QALAMMVDAY ARIRGFGVGM VTSGPGATNL TTGIGCAYYD
SIPCLFITGQ VGMFHVKGER GVRQRGFQET DVVSALKPIT KFAVLLDKGE DARYVFEKAV
HIAKTGRPGP VVIDLPYNVQ REMINPETLR GYVPPEEEKE DKEKLEKETE EVLKKLYKAE
RPLLLIGGGV RIAEKEKEIY EFVKKTELPV VTTWSAADMF PADVPLYLGN IGKSGNASAV
KALQESDVLL CLGVRFTPRT IIHEKKFAVQ TEVIAVDIDR AELEEGIVNP HKKICCDLKE
FVPMMMRCAN GKKMEREGWK RRLNELKAKE YVIHGSLEHS DGYVDPYLFI PMLFEEAPAN
AVFIPEAGAN LIWVMQTYKL KRGQRIFSAW GNSPMGYALP AAIGARIANP NAPVIATIGD
GGFQMNIQEL QTIAGNKIDV KIFILNNKCY GNIIIGATKE FQGRAHGNNA ETGYTAPDFV
KVAKAYGIDT ETITDISEAR EKVRNILGRK GAVIVDVSIN PNQEHVELSL
//
