ID   A0A163XM99_9BRAD        Unreviewed;       596 AA.
AC   A0A163XM99;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KZD21103.1};
GN   ORFNames=A4A58_15055 {ECO:0000313|EMBL:KZD21103.1};
OS   Tardiphaga robiniae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Tardiphaga.
OX   NCBI_TaxID=943830 {ECO:0000313|EMBL:KZD21103.1, ECO:0000313|Proteomes:UP000076574};
RN   [1] {ECO:0000313|EMBL:KZD21103.1, ECO:0000313|Proteomes:UP000076574}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vaf07 {ECO:0000313|EMBL:KZD21103.1,
RC   ECO:0000313|Proteomes:UP000076574};
RA   Kopat V., Chirak E., Kimeklis A., Andronov E.;
RT   "Microsymbionts genomes from the relict species Vavilovia formosa (Stev.)
RT   Fed.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:KZD21103.1}.
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DR   EMBL; LVYV01000053; KZD21103.1; -; Genomic_DNA.
DR   RefSeq; WP_068737068.1; NZ_LVYV01000053.1.
DR   AlphaFoldDB; A0A163XM99; -.
DR   STRING; 943830.A4A58_15055; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000076574; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000076574};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          4..117
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          201..339
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          405..562
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   596 AA;  65100 MW;  131C51343CD73A1E CRC64;
     MAKMKGGEVI AEYLVKQKVP FVFGICGHGN VGILDALHAV RDKIKLISPR HEQCAGHMAD
     AYFRVKHQPV ATLTSTGPGS ANMVMSLATA LSDSSAFLAI TANVPTSQAN RGPFQELYAH
     NQSDFAQVLR PVVKRSFQPS RVDMLPLALR QGFDTMVTGR PGPVNLDIPY NVFQEEDDVE
     LPALSHVHGG HRPSASDNDI KIALDLLSQA KRPVFFIGHG TTLAEAGPEI SELQQKLGIP
     VITSPNGMGC VPADDPLTLG FIGRNGAYPA NQAGRFSDLV ICIGTRFDDR SSSSWHPGYS
     WNFPSTKLLQ VDIDPAELGR NYPPTLGIIA DAKVFAAQLI AALPKRREIT REGFGAWREE
     VANWTAEWEA FIRPNFSAVT TPIRPEYVVG ALLDVLPDDV ILSLDSGVHH NWFMQFWKPK
     RTQSMLNSWG YSSMGFGVCG VLGAQLAAPD RPCVAVVGDG GFMMAPYVVA TAVEYDLPCV
     WIVWNNFAWG AIRDLQYGLF EGREFGTAFY KGNQGPGGDR YNPDFAAWAR ACGADGVTVT
     RSEDLRGAVE TAIKNRRPCV IDLHVDSEVR PPSTGTWELP PIPYKEPVFG KPHRTT
//