ID   M0KMU3_9EURY            Unreviewed;       549 AA.
AC   M0KMU3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:EMA21100.1};
GN   ORFNames=C442_10801 {ECO:0000313|EMBL:EMA21100.1};
OS   Haloarcula amylolytica JCM 13557.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=1227452 {ECO:0000313|EMBL:EMA21100.1, ECO:0000313|Proteomes:UP000011623};
RN   [1] {ECO:0000313|EMBL:EMA21100.1, ECO:0000313|Proteomes:UP000011623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 13557 {ECO:0000313|EMBL:EMA21100.1,
RC   ECO:0000313|Proteomes:UP000011623};
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:EMA21100.1}.
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DR   EMBL; AOLW01000019; EMA21100.1; -; Genomic_DNA.
DR   RefSeq; WP_008310280.1; NZ_AOLW01000019.1.
DR   AlphaFoldDB; M0KMU3; -.
DR   PATRIC; fig|1227452.3.peg.2158; -.
DR   Proteomes; UP000011623; 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; 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          1..111
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          187..320
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          385..534
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   549 AA;  57319 MW;  FE6E48716C10412C CRC64;
     MRVSLAVVDR LVANGIDTVF GIPGKQSLPL NEAIGKRDDI RFVVARHETA VSHQAWGYAE
     TSGQIASTVV VPGPGDMNAM NGLKNALNDC TPLVHFAIET EPALRGGDAI HETPPDTYDN
     VVKENILLKN PETTAATIDR AVQVAQTPPK GPVRVGLPKN YLQMDVPLAG ASTPATPSTS
     TVPEQAVAEA AEHLLAAEMP VIMAGGGVRA SGGTAALRSL AERLDAPVVT TYKGKGVLPE
     DHDLSAGVLS GSASPELLDC LADSDAVLAV GSDLDAHGTR GWSVELPETL VHVTIDADDL
     GTGYDPTVGI LADAADAMTA IENKIAAADT APATKTAGTE RAQAVRDATA RRIEPLVDSE
     PPLTSVRVLQ ILRDAVPSDA ITAVDAGGFR VWALNTFEAY GPRSYVNPGS WATMGTGLPS
     AIGAQLANSD TPVVALTGDG GLMMCVHELH TAVAEDLPIT VVVLNNDDYA IISEEAGRSY
     DLDHQAYGWD TTPIDFGTVA AGMGMEAVQA DTASEIRTAV REAVQTDAPT LVEVRTDPTE
     PQASEWMRE
//