ID   M0MKN0_9EURY            Unreviewed;       566 AA.
AC   M0MKN0;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Acetolactate synthase I/II/III large subunit {ECO:0000313|EMBL:EMA45294.1};
GN   ORFNames=C449_06705 {ECO:0000313|EMBL:EMA45294.1};
OS   Halococcus saccharolyticus DSM 5350.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halococcaceae; Halococcus.
OX   NCBI_TaxID=1227455 {ECO:0000313|EMBL:EMA45294.1, ECO:0000313|Proteomes:UP000011669};
RN   [1] {ECO:0000313|EMBL:EMA45294.1, ECO:0000313|Proteomes:UP000011669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5350 {ECO:0000313|EMBL:EMA45294.1,
RC   ECO:0000313|Proteomes:UP000011669};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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:EMA45294.1}.
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DR   EMBL; AOMD01000018; EMA45294.1; -; Genomic_DNA.
DR   RefSeq; WP_006077198.1; NZ_AOMD01000018.1.
DR   AlphaFoldDB; M0MKN0; -.
DR   STRING; 1227455.C449_06705; -.
DR   PATRIC; fig|1227455.4.peg.1365; -.
DR   InParanoid; M0MKN0; -.
DR   OrthoDB; 6837at2157; -.
DR   Proteomes; UP000011669; 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   GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
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:UP000011669};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          3..109
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          203..341
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          400..541
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          175..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   566 AA;  60571 MW;  E7B89BB68EA45AA1 CRC64;
     MTKVSTEIVR TLERLDVEYL FGYPGGRAIE LLEELAASDI EVVRPRDERE ASVMAEMYGR
     LHRKPGVLTG QGPWIGSIGA IGQMEARLGS SPMVAITEAS ERGDYSTLAP YQQARGDYGG
     FALPKILDGI TKEWWFPRTP NETLRSTQLA FKHATAGRPG PTAVVLDGDA VTAEVPANDD
     PPALWSPEEQ TKNWESSPTA TDVERAAEHL ANADRPVIVA GNGVHAAGAY DELEAVAETY
     DAVVATSYLG KSTIAETHDL AAGVIGSFGH EGANQAVSEA DVLLVVGCRL NPMDTNWQAA
     SFIRPDEQTI LHADIDTRNA GWVYPADVGL IGDAKHSLSA LGEAAAAFAP GNDWARDRAR
     DARESFRVPE CDTDDEPILP QRAVAAIDDI VDENTLVTAD SGNNRFWLLN YLQTPARRTY
     FGSGGVGGMG WAGPAAVSAA ITTDKDVIAV AGDGGFTMTM TCIETAVEYG VAPTFVVLND
     TSLGMVRQMD DEIPGVDFHD TDFVQVAEGF GAEGMRVRSP GDLADPLESA KAADVPTVVD
     VRIDRDEEMV DALQSSFYEE VGGLHE
//