ID A0A1F6A904_9BACT Unreviewed; 604 AA.
AC A0A1F6A904;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3D03_05135 {ECO:0000313|EMBL:OGG21044.1};
OS Candidatus Gottesmanbacteria bacterium RIFCSPHIGHO2_02_FULL_40_13.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1798384 {ECO:0000313|EMBL:OGG21044.1, ECO:0000313|Proteomes:UP000177092};
RN [1] {ECO:0000313|EMBL:OGG21044.1, ECO:0000313|Proteomes:UP000177092}
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:OGG21044.1}.
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DR EMBL; MFJN01000030; OGG21044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6A904; -.
DR STRING; 1798384.A3D03_05135; -.
DR Proteomes; UP000177092; 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; 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 1..124
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 204..341
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 406..555
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 604 AA; 66609 MW; CB21708BA30C2D08 CRC64;
MTVSDYLFDF LVSQGIKHVF LITGGAIAFA LDALHGRKDI EYICVAHEQV AAMAAEAYSR
VGPGLGCAIA TSGPGATNLI TGICCAWFDS IPALYITGQV NTYEQRGADP GTKGSRQIGF
QETDVVSIVK PVTKWAVQLD KPENIRLVLE KAVFLAKSGR PGPVLFDLPQ NFQRVKIDPK
KLPRFIPPKK KLYADYGTSL SGKINQTLKL LTSAQRPVLV FGTGVKLAAA ASQAKILIKK
IGIPVILTWG AYDLLEKTHP LLVGSAGVYG NRGANFAIQN SDLILSIGSR LDTRFTGGKP
SHFGRAAKKI VVDIDKDELS KRRGLIPDIE INCDAAVFIG KLLKKIQHYK KQKIDNWLEK
CADWKIRYPA VLPQYYQEKK FVNGYVFIKT LSEELDSKSI IISDDGGHLT WTMQAFEVKK
GQKLFSAFGN SPMGYSFPAS IGASFALGKK EVICIDGDGS IQMNIQDFQT VVHHKLPLKI
FVLNNDGYAI LQQFQETWLG GRFVAASFNQ GLSNPDLIKV AKAYGLKTVL IRNHQELRRK
IRKVLKAKGP VFCEVKINPK QRLIPKLEFG NPLEDLSPHL SREEFKANMI IPPLAESLEV
SPSV
//
