ID A0A0S7X715_9DELT Unreviewed; 545 AA.
AC A0A0S7X715;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMJ42_03740 {ECO:0000313|EMBL:KPJ58180.1};
OS Deltaproteobacteria bacterium DG_8.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=1703397 {ECO:0000313|EMBL:KPJ58180.1, ECO:0000313|Proteomes:UP000051875};
RN [1] {ECO:0000313|EMBL:KPJ58180.1, ECO:0000313|Proteomes:UP000051875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_8 {ECO:0000313|EMBL:KPJ58180.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KPJ58180.1}.
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DR EMBL; LIZV01000096; KPJ58180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7X715; -.
DR PATRIC; fig|1703397.3.peg.618; -.
DR Proteomes; UP000051875; 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; 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: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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..114
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 189..321
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 383..530
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 545 AA; 59215 MW; 60A68E6B87CF0773 CRC64;
MRSANAVVHA LQKEKVEVVF GIPGFPTIAL YDVLYHSKGI RHVLTRHEQA ASFMAYAYGM
VTGKPGTCLA IDGPGATNMA TGIADAHTGS LPLVAIIGKI PSCNFGKGAV HELDSAFFKP
ITKEIFHIAE PNEIVSTIHK AYTTAATGRK GPVCVEIPMD IFTMEVSPGK VDGNAGGEED
VNHTTVSEIK VAARLLSEAE KPLILAGGGA LSAGASQELT ELAEFLGIPV AVSHMGRGII
PDDHPLALGL LRNNPTLVDF TQQSDVIIAV GFRFSQILTF NWTLKIPRKL IQIDVDPKQI
GKNYPVEVGI VGDAKTELRN LIECLKNKIR KRTTEEYPRF REVTEWKRLL TIRSVSNSVP
IKQLRLIKGI RDCLERDALI ATDVGNAFFW TLFFMEIYHP RTLVCSSSFS AMGCGLPLAI
GAKIAEPDKQ VVCVTGDGGF LMNSQELATA VENNLALPIV IVNDRGYGAI RHIQDHAYQG
RHIASNWVSP DFVQIANGFG AEGMLITKPE DIEPSLRDAL KSDKPTVLDV RVDGMDKLPQ
NRLPG
//
