ID   A0A0Q4XWY3_9BURK        Unreviewed;       565 AA.
AC   A0A0Q4XWY3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KQP12834.1};
GN   ORFNames=ASF43_20250 {ECO:0000313|EMBL:KQP12834.1};
OS   Pseudorhodoferax sp. Leaf267.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae.
OX   NCBI_TaxID=1736316 {ECO:0000313|EMBL:KQP12834.1, ECO:0000313|Proteomes:UP000051560};
RN   [1] {ECO:0000313|EMBL:KQP12834.1, ECO:0000313|Proteomes:UP000051560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf267 {ECO:0000313|EMBL:KQP12834.1,
RC   ECO:0000313|Proteomes:UP000051560};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQP12834.1, ECO:0000313|Proteomes:UP000051560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf267 {ECO:0000313|EMBL:KQP12834.1,
RC   ECO:0000313|Proteomes:UP000051560};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQP12834.1}.
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DR   EMBL; LMMV01000025; KQP12834.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q4XWY3; -.
DR   STRING; 1736316.ASF43_20250; -.
DR   Proteomes; UP000051560; 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:UP000051560};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          6..123
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          198..334
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          408..548
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   565 AA;  59445 MW;  5F8621A7AC656D67 CRC64;
     MMTSLNGADA LVRMLQLNGV RHIFGLCGDT SLPFYDAMAR LDHGIDHILT RDERSAGYMA
     DGYARVTGKV GVCEGPSGGG ATYLLPALVE ANESSIAVLG ITSDVSVGSR GKYPLTELDQ
     QALYRPLTKW NTTVDRVDQI PGAVRGAFRA MTTGKPGSAH ICLPYDLQKH EADPADLWAQ
     PGHDRFPAMR SAPDPAAVEQ AAERLAAARA PVIVCGGGVV IAGACEALDA LATLIDAPVC
     TTVSGQGSLA DTHPLNAGVV GANGGITATR EVVQQADLVL FIGCRAGSTS TENWRVPARS
     VTIVHIDVDP MVIGANYRTD VALVGDALLA LQALHGALLP HLAGRPRQAG AGVALARAAR
     AAKQAKFAPL AASLDTPIKP ERVVDLLNKL LPDDAVVVAD PGTPCPYFSA YFNAARSGRQ
     FITNRAQGAL GFSLAAGIGA QVGRPNAPVV SVMGDGSFGF TCGEMETLVR RKIPLKMVVF
     SNAVFGWIKA SQKEGYGQRY FSVDFTRTDH ARVAEAFGVK AWRVSDPAQL EDALRAALRH
     DGPALVDVLS QELQDTAVPV SQWMG
//